Any feedback?
Information on EC 3.13.2.1 - adenosylhomocysteinase
for references in articles please use BRENDA:EC3.13.2.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.13.2.1 adenosylhomocysteinaseIUBMB Comments
The enzyme contains one tightly bound NAD+ per subunit. This appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond (for mechanism, click here), cf. EC 5.5.1.4, inositol-3-phosphate synthase.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
s-adenosylhomocysteine hydrolase, adohcy hydrolase, s-adenosyl-l-homocysteine hydrolase, sah hydrolase, adohcyase, sahase, adenosylhomocysteinase, s-adenosylhomocysteinase, pfsahh, s-adenosyl homocysteine hydrolase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosylhomocysteine hydrolase
-
-
-
-
AdoHcy hydrolase
AdoHcyase
AdoHcyHD
AdoHyc hydrolase
AHCY
CUBP
-
-
-
-
Cytokinin binding protein CBP57
-
-
-
-
EC 3.3.1.1
-
-
formerly
-
FgSah1
Liver copper binding protein
-
-
-
-
PaSAHase
PfSAHH
S-adenosyl-L-homocysteine hydrolase
S-adenosylhomocysteinase
-
-
-
-
S-adenosylhomocysteine hydrolase
S-adenosylhomocysteine synthase
-
-
-
-
SAH hydrolase
Sah1p
SAHase
SAHH
SAHH1
tmSAHH
AdoHcyase
-
-
-
-
S-adenosyl-L-homocysteine hydrolase
-
-
-
-
S-adenosylhomocysteine hydrolase
-
-
ambiguous
-
SAHase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
-
-
-
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
catalytic mechanism analysis
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
catalytic mechanism analysis
-
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
catalytic mechanism analysis
-
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
catalytic mechanism analysis
-
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
catalytic mechanism analysis
-
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
catalytic mechanism analysis
-
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
catalytic mechanism analysis
-
-
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
catalytic mechanism analysis
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioether
-
-
-
-
synthesis of thioether
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-homocysteine hydrolase
The enzyme contains one tightly bound NAD+ per subunit. This appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond [2] (for mechanism, click here), cf. EC 5.5.1.4, inositol-3-phosphate synthase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9025-54-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4',5'-dehydroadenosine + H2O
adenosine
-
favors formation of 4',5'-dehydroadenosine, precursor reaction
-
r
3-deazaadenosine + L-homocysteine
3-deazaadenosylhomocysteine
-
-
-
?
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
?
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
?
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
the reversible catalysis depends on the binding of NAD+ to the enzyme
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
Micromonospora faeni
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
through the hydrolysis of S-adenosyl-L-homocysteine, the SAH hydrolase prevents the accumulation of S-adenosyl-L-homocysteine that would otherwise lead to an inhibition of the S-adenosyl-L-methionine-dependent methylation reactions, including those that are required for the maturation (i.e. 5'-capping) of viral mRNAs
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
the enzyme is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?, r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?, r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
reversible hydrolysis, five-step process of SAH hydrolysis by SAHH
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
the enzyme catalyzes the breakdown of S-adenosylhomocysteine, a powerful inhibitor of most transmethylation reactions, to adenosine and L-homocysteine
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
substrate binding site structure, overview
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
substrate binding site structure, overview
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
substrate binding site structure, overview
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
substrate binding site structure, overview
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
additional information
?
-
-
homology-dependent gene silencing gene codes for an S-adenosyl-L-homocysteine hydrolase required for DNA methylation-dependent gene silencing
-
-
?
additional information
?
-
-
enzyme redistributes in response to chemotactic signals
-
-
?
additional information
?
-
-
polymorphism has no effect on the total plasma homocysteine
-
-
?
additional information
?
-
-
enzyme redistributes in response to chemotactic signals
-
-
?
additional information
?
-
-
using a yeast two-hybrid system it shown that AdoHcyase directly interacts with Streptococcal pyrogenic exotoxin B protease. Furthermore, it is shown that AdoHcyase gets cleaved and inactivated by Streptococcal pyrogenic exotoxin B protease, inducing hypermethioninemia
-
-
?
additional information
?
-
-
SAHH interacts with H19 lncRNA in ribonucleoprotein complexes, the SAHH-H19 interaction is specific
-
-
?
additional information
?
-
the enzyme binds the reaction intermediate analogues 3'-oxo-aristeromycin (3KA) and noraristeromycin (NRN), and reacts with 3KA in a Michael addition
-
-
?
additional information
?
-
S-adenosyl-L-homocysteine hydrolase associates with diamine oxidase as part of a larger multienzyme complex that may function in planta as a nicotine metabolic channel
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase associates with diamine oxidase as part of a larger multienzyme complex that may function in planta as a nicotine metabolic channel
-
-
?
additional information
?
-
S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is the key enzyme of methylation metabolism. SAH1 expression is coordinately regulated by genes involved in phospholipid biosynthesis. Sah1p depletion leads to significant changes in lipid metabolism, resulting in accumulation of triglycerides
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is the key enzyme of methylation metabolism. SAH1 expression is coordinately regulated by genes involved in phospholipid biosynthesis. Sah1p depletion leads to significant changes in lipid metabolism, resulting in accumulation of triglycerides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
Micromonospora faeni
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
through the hydrolysis of S-adenosyl-L-homocysteine, the SAH hydrolase prevents the accumulation of S-adenosyl-L-homocysteine that would otherwise lead to an inhibition of the S-adenosyl-L-methionine-dependent methylation reactions, including those that are required for the maturation (i.e. 5'-capping) of viral mRNAs
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
the enzyme is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?, r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?, r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
the enzyme catalyzes the breakdown of S-adenosylhomocysteine, a powerful inhibitor of most transmethylation reactions, to adenosine and L-homocysteine
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
additional information
?
-
-
homology-dependent gene silencing gene codes for an S-adenosyl-L-homocysteine hydrolase required for DNA methylation-dependent gene silencing
-
-
?
additional information
?
-
-
enzyme redistributes in response to chemotactic signals
-
-
?
additional information
?
-
-
polymorphism has no effect on the total plasma homocysteine
-
-
?
additional information
?
-
-
enzyme redistributes in response to chemotactic signals
-
-
?
additional information
?
-
-
using a yeast two-hybrid system it shown that AdoHcyase directly interacts with Streptococcal pyrogenic exotoxin B protease. Furthermore, it is shown that AdoHcyase gets cleaved and inactivated by Streptococcal pyrogenic exotoxin B protease, inducing hypermethioninemia
-
-
?
additional information
?
-
-
SAHH interacts with H19 lncRNA in ribonucleoprotein complexes, the SAHH-H19 interaction is specific
-
-
?
additional information
?
-
S-adenosyl-L-homocysteine hydrolase associates with diamine oxidase as part of a larger multienzyme complex that may function in planta as a nicotine metabolic channel
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase associates with diamine oxidase as part of a larger multienzyme complex that may function in planta as a nicotine metabolic channel
-
-
?
additional information
?
-
S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is the key enzyme of methylation metabolism. SAH1 expression is coordinately regulated by genes involved in phospholipid biosynthesis. Sah1p depletion leads to significant changes in lipid metabolism, resulting in accumulation of triglycerides
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is the key enzyme of methylation metabolism. SAH1 expression is coordinately regulated by genes involved in phospholipid biosynthesis. Sah1p depletion leads to significant changes in lipid metabolism, resulting in accumulation of triglycerides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
enzyme exhibits two classes of active sites, one binding NAD+ weakly and generating full activity very rapidly, the other binding the cofactor more strongly but generating activity only slowly. Final affinity of enzyme for NAD+ is about micromolar. Slow binding exhibits saturation kinetics with a rate constant of 0.006 per s. Dissociation of NAD+ from all binding sites is a single first-order reaction. The cofactor always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme
NAD+
-
enzyme exhibits two classes of active sites, one binding NAD+ weakly and generating full activity very rapidly, the other binding the cofactor more strongly but generating activity only slowly. Slow binding exhibits saturation kinetics with a rate constant of 0.06 per s. Dissociation of NAD+ from all binding sites is a single first-order reaction. The cofactor always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme
NAD+
-
inactivation by (E)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine results in 66% loss of NAD+, by (Z)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine in 27% loss, and by (E)-6-chloro-6-cyano-5,6-didehydro-6-deoxyhomoadenosine in 28% loss, respectively
NAD+
-
the enzyme contains four molecules of tightly-bound NAD+ per tetramer of which about 40% is in the reduced form
NAD+
wild-type, 3.5 mol per mol of tetramer, mutant Y143C, 3.1 mol per mol of tetramer, mutant E115L, 4.6 mol per mol of tetramer
NAD+
-
wild-type, about 81% of cofactor bound as NAD+, mutant A89V, about 70.5% of cofactor bound as NAD+
NAD+
-
comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes. Calculation of association kinetics of NAD+ with human and trypanosomal enzyme
NAD+
comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes. Calculation of association kinetics of NAD+ with human and trypanosomal enzyme. Y430 in the C-terminal extension of human SAHH may slightly influence binding of NAD+ and NADH to apo-SAHH
NAD+
NAD+ binding mode, overview. Two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH, which is important in NAD+ binding, and thus exposes the bound cofactor to the solvent. The difference explains the higher NAD+ requirement of tmSAHH because of the reduced affinity. Binding pocket structure, overview
NAD+
the enzyme tetramer tightly but not covalently binds an NAD+ cofactor, binding structure, overview. The cofactor-binding domain comprises residues 197-351. The basic element of the secondary structure in this domain is a six-stranded parallel beta-sheet in the centre of the domain that is sandwiched by two arrays of three alpha-helices each. The six-stranded parallel beta-sheet is flanked by four alpha-helices and constitutes a characteristic dinucleotide-binding motif or Rossmann fold composed of two betaalphabetaalphabeta units
NAD+
-
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NADH
-
wild-type, about 81% of cofactor bound as NAD+, mutant A89V, about 70.5% of cofactor bound as NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cs+
activates, use of Cs+ cations results in a significant decrease of binding specificity for adenosine and increase of entropy contribution, alters the enzyme kinetics
K+
activates, for most of the reactions, the substrate affinity (KM) is 3-12 times higher in the presence of potassium, alters the enzyme kinetics. Potassium cations ensure the highest activity through the regulation of enzyme dynamics
Na+
Rb+
activates, but is also a noncompetitive inhibitor, alters the enzyme kinetics
additional information
activity and ligand binding of the enzyme are not affected by the presence of any particular alkali ion
Na+
contains a sodium cation in close proximity of the active site
Na+
activates, structure analysis of the cation-binding site in MmSAHH, overview
Na+
activates, use of Na+ cations results in a significant decrease of binding specificity for adenosine and increase of entropy contribution, alters the enzyme kinetics
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-5'-noraristeromycin
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
(1R,2S,3R)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
CAS:1214735-71-3
(1R,2S,3R,5R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)-5-(hydroxymethyl)cyclopentane-1,2-diol
-
-
(1R,2S,3S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopentane-1,2-diol
-
-
(1R,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-methylcyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-6,7-difluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-6-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-7-chloro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-7-methyl-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1S,2R,3S,4S)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2,3-triol
-
-
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)-3-(chloromethyl)cyclopent-3-ene-1,2-diol
-
-
(1S,2R,5R)-5-(6-amino-9H-purin-9-yl)-3-(prop-1-yn-1-yl)cyclopent-3-ene-1,2-diol
-
i.e. prop-1-yn-1-yl-substitued neplanocin A, 81% inhibition at 0.01 mM
(1S,2R,5R)-5-(6-amino-9H-purin-9-yl)-3-phenylcyclopent-3-ene-1,2-diol
-
i.e. phenyl-substitutued neplanoocin A, 64% inhibition at 0.1 mM
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopent-3-ene-1,2-diol
-
-
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopent-3-ene-1,2-diol
-
-
(1S,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-fluorocyclopentane-1,2-diol
-
-
(2R,3R)-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid
in rats fed by the enzyme inhibitor, the total plasma cholesterol and phospholipids decreases
(2R,3R)-4-(4-amino-1H-imidazo[4,5-c]pyridin-1-yl)-2,3-dihydroxy-N-methylbutanamide
-
(2R,3R)-methyl-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid
in rats fed by the enzyme inhibitor, the total plasma cholesterol and phospholipids decreases
(E)-5'-deoxy-5'-(iodomethylene)adenosine
-
similar inhibitory activity against both Trichosoma vaginalis and trypanosomes, inhibits growth of Trichosoma vaginalis strain T1
(E)-6-chloro-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
mechanism-based inhibitor, covalent labeling of enzyme. Inactivation results in 28% loss of NAD+
(E)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
mechanism-based inhibitor, type I inhibitor. Inactivation results in 66% loss of NAD+
(E)-9-(5-deoxy-5-fluoro-beta-D-threo-pent-4-enofuranosyl)-9H-purin-6-amine
-
competitive
(Z)-5'-deoxy-5'-(iodomethylene)adenosine
-
similar inhibitory activity against both Trichosoma vaginalis and trypanosomes, inhibits growth of Trichosoma vaginalis strain T1
(Z)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
mechanism-based inhibitor, covalent labeling of enzyme. Inactivation results in 27% loss of NAD+
(Z)-9-(5-deoxy-5-fluoro-beta-D-threo-pent-4-enofuranosyl)-9H-purin-6-amine
-
competitive
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
-
1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxycyclopent-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
-
-
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-fluorophenyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
4.56% inhibition at 0.0025 mM; 8.23% inhibition at 0.0025 mM
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-tolyl)-amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
4.89% inhibition at 0.0025 mM
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)-(1-methyl-1H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
30.19% inhibition at 0.0025 mM
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)-(2-methyl-2H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
27.15% inhibition at 0.0025 mM
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(1-methyl-1H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
85.72% inhibition at 0.0025 mM
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(2-methyl-2H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
86.56% inhibition at 0.0025 mM
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(4-tolyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
19.23% inhibition at 0.0025 mM
2-((4-(1H-pyrrol-1-yl)phenyl)(2-((2-(diethylamino)-ethyl)amino)-2-oxoethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
20.16% inhibition at 0.0025 mM
2-((4-(1H-pyrrol-1-yl)phenyl)(2-((2-(ethylamino)-ethyl)amino)-2-oxoethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
79.46% inhibition at 0.0025 mM
2-((4-(1H-pyrrol-1-yl)phenyl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
21.46% inhibition at 0.0025 mM
2-((4-fluorophenyl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)-amino)ethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
2.63% inhibition at 0.0025 mM
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-[(piperidin-2-ylmethyl)amino]ethyl]amino)-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl]amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-([5-chloro-2-(4-chlorophenoxy)phenyl]{2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl}amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-amino-4'-alpha-fluoro-(9-((1'R,2'S,3'R)-2',3'-dihydroxy-cyclopentan-1'-yl)adenine)
-
slight inhibition
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2R)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2S)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(piperidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(propan-2-ylamino)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(3,4-dihydroisoquinolin-2(1H)-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(1,2,3,4-tetrahydronaphthalen-2-yl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(piperidin-4-yl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(trans-4-phenylcyclohexyl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-phenylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[1-(methylsulfonyl)piperidin-4-yl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[4-(2-nitrobenzene-1-sulfonyl)piperazin-1-yl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[4-(methylsulfonyl)piperazin-1-yl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[3-(pyrrolidin-1-yl)propyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[(2-fluorophenyl)methyl]amino]-2-oxoethyl)amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(dimethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(ethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(methylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(piperidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(pyrrolidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[(2-fluorophenyl)methyl]amino}-2-oxoethyl)amino}-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[2-(methylamino)ethyl]amino}-2-oxoethyl)amino}-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
-
-
3-(4-amino-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
3-(6-amino-9H-purin-9-yl)cyclopentane-1,2-diol
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
3-acetylpyridine adenine dinucleotide
-
0.02 mM, 94% residual activity in presence of 0.05 mM NAD, pH 7.4
3-deaza-adenosine
-
the inhibitor of S-adenosyl homocysteine hydrolase prevents oxidative damage and cognitive impairment following folate and vitamin E deprivation in a murine model of age-related, oxidative stress-induced neurodegeneration. The inhibitor might by useful in therapeutic approach to delay neurodegeneration in Alzheimer's disease
3-deazaneplanocin A
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
3-pyridinaldehyde adenine dinucleotide
-
0.02 mM, 77% residual activity in presence of 0.05 mM NAD, pH 7.4
4'-beta-fluoro-(9-((1'R,2'S,3'R)-2',3'-dihydroxy-cyclopentan-1'-yl)adenine)
-
slight inhibition
4-(3-hydroxyprop-1-en-1-yl)-2-methoxyphenol
coniferyl alcohol, molecular docking studies show that coniferyl alcohol is well docked into the active cavity of SAHH. Several H-bonds are formed between them, which stabilize coniferyl alcohol in the active site of rSAHH with a proper conformation
5-(4-amino-1H-imidazo[4,5-c]pyridin-1-yl)cyclopent-3-ene-1,2-diol
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
5-(6-amino-9H-purin-9-yl)cyclopent-3-ene-1,2-diol
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
5-(6-aminopurin-9-yl)-4-fluoro-3-hydroxymethylcyclopent-3-ene-1,2-diol
i.e. fluoroneplanocin A, mechanism-based inhibitor, crystallization data
6'-beta-fluoroaristeromycin
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
9-(5,6-dideoxy-6-iodo-beta-D-ribo-hex-5-ynofuranosyl)-9H-purin-6-amine
i.e. 5',5',6',6'-tetradehydro-6'-deoxy-6'-iodohomoadenosine, strong
9-(6-bromo-5,6-dideoxy-beta-D-ribo-hex-5-ynofuranosyl)-9H-purin-6-amine
i.e. 5',5',6',6'-tetradehydro-6'-deoxy-6'-bromohomoadenosine, partial, 2 mol of the inhibitor is covalently bound to Lys318 of the two subunits of the homotetramer
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine (adenosine-5'-carboxaldehyde)
-
-
9-(S)-(2,3-dihydroxypropyl)-adenine
-
inhibitor of SAH-hydrolase. Application on tobacco seeds during 6 days during the germination period. The transient drug treatment induces dosage-dependent global DNA hypomethylation mitotically transmitted to adult plants, pleiotropic developmental defects including decreased apical dominance, altered leaf and flower symmetry, flower whorl malformations and reduced fertility, and dramatic upregulation of floral organ identity genes NTDEF, NTGLO and NAG1 in leaves
9-[5,6,7,8-tetradeoxy-8-iodo-beta-D-ribo-oct-5(E)-en-7-yno-furanosyl]adenine
-
-
9H-purin-6-amine, 9-(6-chloro-5,6-dideoxy-beta-D-ribo-hex-5-ynofuranosyl)-9H-purin-6-amine
i.e. 5',5',6',6'-tetradehydro-6'-deoxy-6'-chlorohomoadenosine partial, 2 mol of the inhibitor is covalently bound to Lys318 of the two subunits of the homotetramer
adenosine-2',3'-dialdehyde
-
inhibition of the enzyme, mimicks the induction of caspase-like activity and DNA fragmentation induced by adenosine
ADP
-
adenosine analogs exhibit the following trend in the half-maximal inhibitory concentrations: adenosine > AMP > ADP = ATP
AMP
-
adenosine analogs exhibit the following trend in the half-maximal inhibitory concentrations: adenosine > AMP > ADP = ATP
carbocyclic 3-deazaadenosine
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
Cu2+
noncompetitive, binding of Cu2+ results in release of NAD+ cofactors. Cu2+ binds at the central channel and interrupts subunit interactions
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
-
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-3-[(tert-butoxycarbonyl)(methyl)amino]-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]propanoate
63.62% inhibition at 0.2 mM
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
79.87% inhibition at 0.2 mM
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-5-(6-amino-9H-purin-9-yl)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
57.21% inhibition at 0.2 mM
ethyl 3-[(2R,3R,4R,5S)-5-[2-(acetylamino)-6-[(diphenylcarbamoyl)oxy]-9H-purin-9-yl]-4-(acetyloxy)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
87.58% inhibition at 0.2 mM
ethyl 3-[(2R,3S,4R,5R)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-3-[(tert-butoxycarbonyl)amino]-4-hydroxytetrahydrofuran-2-yl]propanoate
81.13% inhibition at 0.2 mM
H19 lncRNA
-
the developmentally regulated H19 lncRNA binds to enzyme S-adenosylhomocysteine hydrolase (SAHH) and inhibits its function both in vivo and in vitro. Binding to U-rich elements of H19 inhibits SAHH activity in vitro. The interaction prevents SAHH from hydrolysing SAH that blocks DNA methylation by DNMT3B at numerous genomic loci. The SAHH-H19 interaction is specific
-
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperazine-1-carboxylate
-
-
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperidine-1-carboxylate
-
-
N-(1-acetylpiperidin-4-yl)-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
-
-
N-(isoindolin-2-yl)-N-methyl-2-((1-methyl-1H-indazol-5-yl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)amino)-acetamide
-
54.24% inhibition at 0.0025 mM
N-(isoindolin-2-yl)-N-methyl-2-((2-methyl-2H-indazol-5-yl)(2-oxo-2-((2-(piperidin-1-yl) ethyl)amino)ethyl)amino)-acetamide
-
38.24% inhibition at 0.0025 mM
N-(isoindolin-2-yl)-N-methyl-2-((2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)(4-tolyl)amino)acetamide
-
6.97% inhibition at 0.0025 mM
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
-
-
N2-[2-[(1-acetylpiperidin-4-yl)(methyl)amino]-2-oxoethyl]-N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[2,3-dihydro-1H-inden-2-yl(ethyl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[methyl(piperidin-4-yl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[methyl(trans-4-phenylcyclohexyl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
inhibitor compound crystal structure determination and analysis, overview. The single crystal X-ray structure of 14n shows an intramolecular eight-membered ring hydrogen bond interaction
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(ethylamino)ethyl]glycinamide hydrochloride
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(methylamino)ethyl]glycinamide hydrochloride
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-piperidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(3-pyrrolidin-1-ylpropyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-methyl(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(dimethylamino)ethyl]glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroisoquinolin-2(1H)-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroisoquinolin-2(1H)-yl]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroquinolin-1(2H)-yl]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methy-(phenyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl(1,2,3,4-tetrahydronaphtalen-2-yl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl-[1-(methylsulfonyl)piperidin-4-yl]amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl-[4-(methylsulfonyl)piperadin-1-yl]amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[[1-(methoxycarbonyl)piperidin-4-yl](methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[[4-(methoxycarbonyl)piperidin-1-yl](methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
nicotinamide 1,N6-ethenoadenine dinucleotide
-
0.02 mM, 95% residual activity in presence of 0.05 mM NAD, pH 7.4
nicotinamide guanine dinucleotide
-
0.02 mM, 96% residual activity in presence of 0.05 mM NAD, pH 7.4
nicotinamide hypoxanthine dinucleotide
-
0.02 mM, 96% residual activity in presence of 0.05 mM NAD, pH 7.4
nicotinic acid adenine dinucleotide
-
0.02 mM, 96% residual activity in presence of 0.05 mM NAD, pH 7.4
reduced 3-acetylpyridine adenine dinucleotide
-
0.02 mM, 52% residual activity in presence of 0.05 mM NAD, pH 7.4
reduced 3-pyridinaldehyde adenine dinucleotide
-
0.02 mM, 9% residual activity in presence of 0.05 mM NAD, pH 7.4
reduced nicotinamide hypoxanthine dinucleotide
-
0.02 mM, 98% residual activity in presence of 0.05 mM NAD, pH 7.4
reduced thionicotinamide adenine dinucleotide
-
0.02 mM, 8% residual activity in presence of 0.05 mM NAD, pH 7.4
tert-butyl (2R)-2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
-
-
tert-butyl 2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]piperidine-1-carboxylate
-
-
tert-butyl 3-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]piperidine-1-carboxylate
-
-
tert-butyl 3-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
-
-
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]ethylcarbamate
-
-
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]methylcarbamate
-
-
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]propan-2-ylcarbamate
-
-
tetraethylene pentamine
-
65% inhibition at 0.0001 mM, 80% inhibition at 0.001 mM
Thionicotinamide adenine dinucleotide
-
0.02 mM, 74% residual activity in presence of 0.05 mM NAD, pH 7.4
Zn2+
enzyme binding structure, potent noncompetitive inhibition, isothermal titration calorimetry, overview. A tetrahedral zinc binding site, formed by three highly conserved amino acid residues involving S (Cys85), N (His323), and two O (Asp139) ligand atoms, is located in the active site, where, together with the H323-F324 molecular gate, the divalent cation shuts access to the active site of the enzyme
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
-
-
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
-
-
-
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
-
-
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
-
-
-
(6'R)-6'-C-methylneplanocin A
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
-
-
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
-
-
-
2'-deoxyadenosine
time course of PaSAHase inactivation by 2'-deoxyadenosine, influence of K+ and Rb+ ions, overview
2-aminoaristeromycin
-
20fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
2-aminoaristeromycin
-
20fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
2-fluoroaristeromycin
-
24fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
2-fluoroaristeromycin
-
24fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
-
-
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
-
adenosine
-
adenosine analogs exhibit the following trend in the half-maximal inhibitory concentrations: adenosine > AMP > ADP = ATP
ATP
-
adenosine analogs exhibit the following trend in the half-maximal inhibitory concentrations: adenosine > AMP > ADP = ATP
beta-thionicotinamide adenine dinucleotide
-
binding affinity 40 nM, 30% loss of activity after 12 h
beta-thionicotinamide adenine dinucleotide
-
binding affinity 0.0006-0.015 mM, 60% loss of activity after 30 min
beta-thionicotinamide adenine dinucleotide, reduced form
-
binding affinity 40 nM, 30% loss of activity after 12 h
beta-thionicotinamide adenine dinucleotide, reduced form
-
binding affinity 0.0006-0.015 mM, 100% loss of activity after 30 min
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
-
-
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
-
-
-
methyl 4-(adenin-9-yl)-2-hydroxybutanoate
-
i.e. DZ2002, potent reversible type III inhibitor, blocks S-adenosylhomocysteine hydrolase more effectively than type I inhibitor, but cytotoxicity is greatly reduced
methyl 4-(adenin-9-yl)-2-hydroxybutanoate
-
i.e. DZ2002, potent reversible type III inhibitor, blocks S-adenosylhomocysteine hydrolase more effectively than type I inhibitor, but cytotoxicity is greatly reduced
methyl 4-(adenin-9-yl)-2-hydroxybutanoate
-
i.e. DZ2002. The inhibitor suppresses antigen-induced specific immune responses, particularly type 1 helper T cell responses through inhibition of S-adenosyl-L-homocysteine hydrolase and elevation of endogenous S-adenosyl-L-homocysteine
N-(9-[(1R,4S)-4-hydroxycyclopent-2-en-1-yl]-9H-purin-6-yl)benzamide
-
-
-
neplanocin A
strong inhibition, oxidation upon binding to form the complex enzyme/NADH/3'-keto-neplanocin
neplanocin A
NepA, a natural product that is cytotoxic upon long term exposure and shows adenosine deaminase and adenosine kinase activity
neplanocin A
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
ribavirin
-
binds to adenosine-binding site of enzyme and reduces the NAD+ cofactor to NADH. Selective for trypanosomal enzyme over human enzyme, as the slow inactivation step is 5fold faster with the trypanosomal enzyme
ribavirin
-
binds to adenosine-binding site of enzyme and reduces the NAD+ cofactor to NADH. Selective for trypanosomal enzyme over human enzyme, as the slow inactivation step is 5fold faster with the trypanosomal enzyme
tubercidin
-
inhibition of enzyme as well as of chemotaxis and chemotaxis-dependent cell streaming
tubercidin
-
inhibition of enzyme as well as of chemotaxis, at concentrations that have little effect on cell viability
additional information
L-adenosine and L-adenosine-5'-carboxaldehyde oximes are inactive as inhibitors
-
additional information
-
less than 4% inhibition at 0.02 mM, in presence of 0.05 mM NAD, pH 7.4: thionicotinamide adenine dinucleotide, 3-pyridinaldehyde adenine dinucleotide, 3-acetylpyridine adenine dinucleotide, nicotinic acid adenine dinucleotide, nicotinamide hypoxanthine dinucleotide, nicotinamide guanine dinucleotide, nicotinamide 1,N6-ethenoadenine dinucleotide, reduced thionicotinamide adenine dinucleotide, reduced 3-pyridinaldehyde adenine dinucleotide, reduced 3-acetylpyridine adenine dinucleotide, reduced nicotinamide hypoxanthine dinucleotide
-
additional information
-
inactive: 4-amino-1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxycyclopent-2-en-1-yl]pyrimidin-2(1H)-one
-
additional information
-
optimization of a series of S-adenosyl-L-homocysteine hydrolase (AdoHcyase) inhibitors based on non-adenosine analogues leads to very potent compounds
-
additional information
pentanediamide derivatives were designed, synthesized and evaluated as S-adenosyl-L-homocysteine hydrolase inhibitors
-
additional information
structure of the monovalent cation binding site, overview. The major structural difference between the closed/semi-open and open states concerns the conformation of Q65 (PaSAHase numbering). In the open state this residue is located far away from the metal binding loop and its side chain is disordered in at least two conformations
-
additional information
-
structure of the monovalent cation binding site, overview. The major structural difference between the closed/semi-open and open states concerns the conformation of Q65 (PaSAHase numbering). In the open state this residue is located far away from the metal binding loop and its side chain is disordered in at least two conformations
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5alpha-dihydrotestosterone
-
stimulating and stabilizing, promotes formation of ternary complexes, restores specific activity after hypophysectomy
cAMP
-
cAMP at 0.010 mM enhances the hydrolytic activity of native AdoHcy-hydrolase by 35%, whereas the activity of the enzyme in its NAD+ form is not stimulated by cAMP. The cAMP-binding site at the AdoHcy-hydrolase is independent of the NAD+/NADH ratio of the enzyme and is identical with the high affinity-binding site of adenosine. cAMP does not interact with the catalytic site of AdoHcyhydrolase and does not act as an allosteric effector
N-nitrosomethylbenzylamine
-
treatment with 50 microg/ml N-nitrosomethylbenzylamine results in twenty-eight differentially expressed protein spots in HEEC cells. Two tumor suppressor proteins, prohibitin and c-Myc binding protein, are down-regulated in NMBA-treated HEEC cells. S-adenosylhomocysteine hydrolase, is up-regulated in NMBA-treated HEEC cells
adenosine
-
prevents inhibition by (Z)-9-(5-deoxy-5-fluoro-beta-D-erythro-pent-4-enofuranosyl)adenine
NAD+
-
25% activation, restores activity of 2'-deoxyadenosine-, ATP, AMP or cAMP-treated enzyme, stabilizes quaternary structure
NAD+
-
25% activation, restores activity of 2'-deoxyadenosine-, ATP, AMP or cAMP-treated enzyme, stabilizes quaternary structure
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00024
S-adenosyl-DL-homocysteine
30°C, pH 7.6, mutant enzyme A84Q
0.00025
S-adenosyl-DL-homocysteine
30°C, pH 7.6, mutant enzyme C59T
0.00039
S-adenosyl-DL-homocysteine
30°C, pH 7.6, mutant enzyme C59S
0.00473
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM K+
0.00477
S-adenosyl-L-homocysteine
pH 7.5, 20°C, mutant enzyme R24E, 100 mM K+
0.0049
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Rb+
0.00534
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM Na+
0.00614
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM Rb+
0.00682
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM Li+
0.0073
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, without monovalent metal ion
0.0079
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of K+
0.0139
S-adenosyl-L-homocysteine
recombinant wild type enzyme, at pH 7.2 and 37°C
0.0262
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant mutant Q65A, in presence of K+
0.028
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Na+
0.032
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Cs+
0.0638
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Li+
0.1011
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme
additional information
additional information
Michaelis-Menten kinetics, double-reciprocal form of the Michaelis-Menten equation
-
additional information
additional information
-
Michaelis-Menten kinetics, double-reciprocal form of the Michaelis-Menten equation
-
additional information
additional information
thermodynamics and kinetics, recombinant enzyme
-
additional information
additional information
-
thermodynamics and kinetics, recombinant enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
S-adenosyl-L-homocysteine
pH 7.5, 20°C, mutant enzyme R24E, 100 mM K+
0.175
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM Rb+
0.178
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, without monovalent metal ion
0.186
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM K+
0.186
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM Li+
0.192
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM Na+
0.79
S-adenosyl-L-homocysteine
recombinant wild type enzyme, at pH 7.2 and 37°C
17.5
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Rb+
46.6
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Li+
52.9
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme
140
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant mutant Q65A, in presence of K+
213.1
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Cs+
237.3
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Na+
575
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of K+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.2
S-adenosyl-L-homocysteine
pH 7.5, 20°C, mutant enzyme R24E, 100 mM K+
24.3
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, without monovalent metal ion
27.2
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM Li+
28.5
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM Rb+
36
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM Na+
39.3
S-adenosyl-L-homocysteine
pH 7.5, 20°C, wild-type enzyme, 100 mM K+
57
S-adenosyl-L-homocysteine
recombinant wild type enzyme, at pH 7.2 and 37°C
523.24
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme
730.4
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Li+
3571.4
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Rb+
5343.5
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant mutant Q65A, in presence of K+
6659.4
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Cs+
8475
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of Na+
72784.8
S-adenosyl-L-homocysteine
pH 7.5, 20°C, recombinant wild-type enzyme, in presence of K+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
(2R,3R)-4-(4-amino-1H-imidazo[4,5-c]pyridin-1-yl)-2,3-dihydroxy-N-methylbutanamide
at 22°C in 50 mM potassium phosphate buffer, at pH 7.2
0.0015
(2R,3R)-methyl 4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid
at 22°C in 50 mM potassium phosphate buffer, at pH 7.2
0.0015
(2R,3R)-methyl-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid
pH 7.2, 22°C
0.03
(2R,3R)-N-methyl-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanamide
pH 7.2, 22°C
0.0143 - 0.0203
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
0.0124
9-[(1'R,2'S,3'S,4'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-adenine
-
-
0.1185
9-[5,6,7,8-tetradeoxy-8-iodo-beta-D-ribo-oct-5(E)-en-7-yno-furanosyl]adenine
-
37°C, pH 7.2
0.00055
9-[5,6,7,8-tetradeoxy-beta-D-ribo-oct-5(E)-en-7-ynofuranosyl]adenine
-
37°C, pH 7.2
0.0015
(2R,3R)-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid
pH 7.2, 22°C
0.0015
(2R,3R)-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid
at 22°C in 50 mM potassium phosphate buffer, at pH 7.2
0.000116
2-fluoronoraristeromycin
30°C, pH 7.6, mutant enzyme A84Q
0.0143
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
-
0.0203
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
-
-
0.00003
D-eritadenine
at 22°C in 50 mM potassium phosphate buffer, at pH 7.2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
(1R,2S,3R)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000055
(1R,2S,3R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000303
(1R,2S,3R,5R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)-5-(hydroxymethyl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000455
(1R,2S,3S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.00025
(1R,2S,3S)-3-(8-aminoimidazo[1,2-a]pyrazin-3-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.001223
(1R,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-methylcyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.003644
(1R,2S,4r)-4-(4-amino-6,7-difluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.004827
(1R,2S,4r)-4-(4-amino-6-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000016
(1R,2S,4r)-4-(4-amino-7-chloro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000041
(1R,2S,4r)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000236
(1R,2S,4r)-4-(4-amino-7-methyl-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.002124
(1R,2S,4r)-4-(6-amino-2-fluoro-9H-purin-9-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.61 - 0.85
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
-
0.000024
(1S,2R,3S,4S)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2,3-triol
Homo sapiens
-
pH and temperature not specified in the publication
0.000195
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)-3-(chloromethyl)cyclopent-3-ene-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.004125
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopent-3-ene-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000976
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopent-3-ene-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.00969
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopent-3-ene-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000269
(1S,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-fluorocyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000571
(2E)-3-(4-chlorophenyl)prop-2-enoic acid
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000986
(2E)-3-(4-methoxyphenyl)prop-2-enoic acid
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.1
(6'R)-6'-C-methylneplanocin A
Plasmodium falciparum
-
pH and temperature not specified in the publication
0.06
(E)-5'-deoxy-5'-(iodomethylene)adenosine
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
0.076
(Z)-5'-deoxy-5'-(iodomethylene)adenosine
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
24 - 47.2
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
-
0.000913
1-(bromomethyl)-2,4-difluorobenzene
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.00853
1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxycyclopent-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
-
37°C
0.07882 - 0.5
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-fluorophenyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
0.214
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-tolyl)-amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00761
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)-(1-methyl-1H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.02534
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)-(2-methyl-2H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00048
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(1-methyl-1H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00044
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(2-methyl-2H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.0156
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(4-tolyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.01408
2-((4-(1H-pyrrol-1-yl)phenyl)(2-((2-(diethylamino)-ethyl)amino)-2-oxoethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00073
2-((4-(1H-pyrrol-1-yl)phenyl)(2-((2-(ethylamino)-ethyl)amino)-2-oxoethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.01212
2-((4-(1H-pyrrol-1-yl)phenyl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.5
2-((4-fluorophenyl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)-amino)ethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
IC50 above 0.5 mM, at pH 8.0 and 37°C
0.00015
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-[(piperidin-2-ylmethyl)amino]ethyl]amino)-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.01136
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl]amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
pH 7.2, 37°C
0.01136
2-([5-chloro-2-(4-chlorophenoxy)phenyl]{2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl}amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.0006
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2R)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00011
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2S)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00032
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(piperidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000049
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(propan-2-ylamino)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000013
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000052
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.0002
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(3,4-dihydroisoquinolin-2(1H)-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00038
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
0.000081
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(1,2,3,4-tetrahydronaphthalen-2-yl)acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00034
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
0.1
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(piperidin-4-yl)acetamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 7.2 and 37°C
0.00053
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(trans-4-phenylcyclohexyl)acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.0027
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-phenylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00023
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[1-(methylsulfonyl)piperidin-4-yl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000049
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[4-(methylsulfonyl)piperazin-1-yl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00033
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[3-(pyrrolidin-1-yl)propyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00878
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[(2-fluorophenyl)methyl]amino]-2-oxoethyl)amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
pH 7.2, 37°C
0.00013
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(dimethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00006
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(ethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00007
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(methylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.1
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 7.2 and 37°C
0.017
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00097
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
0.0012
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(piperidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.0015
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(pyrrolidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00878
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[(2-fluorophenyl)methyl]amino}-2-oxoethyl)amino}-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000005
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[2-(methylamino)ethyl]amino}-2-oxoethyl)amino}-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000565
4-chlorobenzene-1-carboperoxoic acid
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000034
4-[(1E)-3-hydroxyprop-1-en-1-yl]-2-methoxyphenol
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.00087
5-(6-aminopurin-9-yl)-3-hydroxymethylcyclopent-3-ene-1,2-diol
Homo sapiens
pH 7.2, 37°C
0.00048
5-(6-aminopurin-9-yl)-4-fluoro-3-hydroxymethylcyclopent-3-ene-1,2-diol
Homo sapiens
pH 7.2, 37°C
0.00767
5-(6-aminopurin-9-yl)-4-fluorocyclopent-3-ene-1,2-diol
Homo sapiens
pH 7.2, 37°C
0.04
adenosine-5'-oxime
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
0.018
Chloroquine
Plasmodium falciparum
-
pH and temperature not specified in the publication
4.51 - 20
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
-
0.144
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-3-[(tert-butoxycarbonyl)(methyl)amino]-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.0796
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.171
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-5-(6-amino-9H-purin-9-yl)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.00043
ethyl 3-[(2R,3R,4R,5S)-5-[2-(acetylamino)-6-[(diphenylcarbamoyl)oxy]-9H-purin-9-yl]-4-(acetyloxy)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.0954
ethyl 3-[(2R,3S,4R,5R)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-3-[(tert-butoxycarbonyl)amino]-4-hydroxytetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.000814
methyl (2E)-3-[4-(bromomethyl)phenyl]prop-2-enoate
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000044
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperazine-1-carboxylate
Homo sapiens
-
at pH 7.2 and 37°C
0.00089
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperidine-1-carboxylate
Homo sapiens
-
at pH 7.2 and 37°C
0.00072
metronidazole
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
0.0046
N-(1-acetylpiperidin-4-yl)-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00203
N-(isoindolin-2-yl)-N-methyl-2-((1-methyl-1H-indazol-5-yl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)amino)-acetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00413
N-(isoindolin-2-yl)-N-methyl-2-((2-methyl-2H-indazol-5-yl)(2-oxo-2-((2-(piperidin-1-yl) ethyl)amino)ethyl)amino)-acetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.1019
N-(isoindolin-2-yl)-N-methyl-2-((2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)(4-tolyl)amino)acetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00053
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
0.0046
N2-[2-[(1-acetylpiperidin-4-yl)(methyl)amino]-2-oxoethyl]-N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.00064
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[2,3-dihydro-1H-inden-2-yl(ethyl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.1
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[methyl(piperidin-4-yl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
above, pH 7.2, 37°C
0.00053
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[methyl(trans-4-phenylcyclohexyl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.1
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
above, pH 7.2, 37°C
0.000013
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.0000085
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(ethylamino)ethyl]glycinamide hydrochloride
Homo sapiens
-
pH 7.2, 37°C
0.000005
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(methylamino)ethyl]glycinamide hydrochloride
Homo sapiens
-
pH 7.2, 37°C
0.00032
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-piperidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.000052
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.00033
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(3-pyrrolidin-1-ylpropyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.1
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-methyl(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
above, pH 7.2, 37°C
0.00013
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(dimethylamino)ethyl]glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.0002
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroisoquinolin-2(1H)-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.017
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroisoquinolin-2(1H)-yl]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.0023
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroquinolin-1(2H)-yl]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.0027
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methy-(phenyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.000081
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl(1,2,3,4-tetrahydronaphtalen-2-yl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.00023
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl-[1-(methylsulfonyl)piperidin-4-yl]amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.000049
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl-[4-(methylsulfonyl)piperadin-1-yl]amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.00089
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[[1-(methoxycarbonyl)piperidin-4-yl](methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.000044
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[[4-(methoxycarbonyl)piperidin-1-yl](methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.2
neoplanocin A
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
0.0006
tert-butyl (2R)-2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.00011
tert-butyl (2S)-2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.00015
tert-butyl 2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]piperidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.0012
tert-butyl 3-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]piperidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.0015
tert-butyl 3-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.00006
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]ethylcarbamate
Homo sapiens
-
pH 7.2, 37°C
0.00007
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]methylcarbamate
Homo sapiens
-
pH 7.2, 37°C
0.000049
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]propan-2-ylcarbamate
Homo sapiens
-
pH 7.2, 37°C
13
(1R,4S)-4-hydroxycyclopent-2-en-1-yl acetate
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
16
(1R,4S)-4-hydroxycyclopent-2-en-1-yl acetate
Homo sapiens
pH and temperature not specified in the publication
-
0.61
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
0.85
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
Homo sapiens
pH and temperature not specified in the publication
-
2.1
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
7.5
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
Homo sapiens
pH and temperature not specified in the publication
-
24
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
Homo sapiens
pH and temperature not specified in the publication
-
47.2
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
0.07882
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-fluorophenyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.5
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-fluorophenyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
IC50 above 0.5 mM, at pH 8.0 and 37°C
0.00038
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
Homo sapiens
-
pH 7.2, 37°C
0.00038
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00034
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
Homo sapiens
-
pH 7.2, 37°C
0.00034
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00097
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
pH 7.2, 37°C
0.00097
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.01
aristeromycin
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
4.51
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
20
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
Homo sapiens
pH and temperature not specified in the publication
-
3.3
N-(9-[(1R,4S)-4-hydroxycyclopent-2-en-1-yl]-9H-purin-6-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
-
18
N-(9-[(1R,4S)-4-hydroxycyclopent-2-en-1-yl]-9H-purin-6-yl)benzamide
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
0.00053
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
Homo sapiens
-
pH 7.2, 37°C
0.00053
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
3.1
noraristeromycin
Plasmodium falciparum
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00003 - 0.0003
-
differs, depending on which organ is examined, hydrolysis of S-adenosyl-L-homocysteine, crude extract
0.00005 - 0.00036
-
differs, depending on which organ is examined, hydrolysis of S-adenosyl-L-homocysteine, crude extract
0.00008 - 0.00091
-
differs, depending on which organ is examined, hydrolysis of S-adenosyl-L-homocysteine, crude extract
0.00008 - 0.00092
-
differs, depending on which organ is examined, hydrolysis of S-adenosyl-L-homocysteine, crude extract
0.00121
-
P. aeruginosa, hydrolysis of S-adenosyl-L-homocysteine, crude extract
0.0031 - 0.09
-
differs, depending on which organ is examined, synthesis of S-adenosyl-L-homocysteine, crude extract
0.0033 - 0.0259
-
differs, depending on which organ is examined, synthesis of S-adenosyl-L-homocysteine, crude extract
0.00521
-
IAM 1061, hydrolysis of S-adenosyl-L-homocysteine, crude extract
0.0055 - 0.0588
-
differs, depending on which organ is examined, synthesis of S-adenosyl-L-homocysteine, crude extract
0.0105
-
P. aeruginosa, synthesis of S-adenosyl-L-homocysteine, crude extract
0.0356
-
up to this value, differs, depending on which organ is examined, synthesis of S-adenosyl-L-homocysteine, crude extract
0.3 - 0.9
0.748
1.23
additional information
additional information
-
specific activity is correlated with enzyme-bound NAD+/NADH ratio
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7 - 7.2
7.2
7.4
7.5
7.6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
pH 6.0: about 65% of maximal activity, pH 7.0: about 55% of maximal activity
6 - 8
7 - 9
-
the enzyme retains more than 70% of its activity at pH values between 7.0 and 9.0, with the maximum activity observed for pH 8.0
additional information
6 - 8
-
pH 6.0: about 60% of maximal activity, pH 8.0: about 60% of maximal activity, hydrolysis of S-adenosyl-DL-homocysteine
6 - 8
-
pH 6.0: about 45% of maximal activity, pH 8.0: about 90% of maximal activity, hydrolysis of S-adenosyl-DL-homocysteine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
50
75
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 55
-
35°C: about 60% of maximal activity, 55°C: about 75% of maximal activity, hydrolysis of S-adenosyl-DL-homocysteine
40 - 60
-
40°C: about 50% of maximal activity, 60°C: about 85% of maximal activity, hydrolysis of S-adenosyl-DL-homocysteine
60 - 85
60°C: about 65% of maximal activity, 85°C: about 75% of maximal activity
75 - 105
additional information
75 - 105
75°C: about 50% of maximal activity, 105°C: about 45% of maximal activity
75 - 105
75°C: about 50% of maximalm activity, 105°C: about 45% of maximal activity
additional information
the enzyme is inactive at room temperature, mechanism of thermal activation, overview. calorimetric evaluation of heat-induced conformational changes (at 85°C) and oligomeric state
additional information
-
the enzyme is inactive at room temperature, mechanism of thermal activation, overview. calorimetric evaluation of heat-induced conformational changes (at 85°C) and oligomeric state
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
137125, 137128, 137130, 137140, 137150, 669994, 669997, 670395, 670434, 696415, 697138, 703632, 706990, 710380
-
-
brenda
S-adenosylhomocysteine-synthetic activity significantly increases in animals fed a vitamin B6-free diet, while S-adenosylhomocysteine hydrolytic activity shows no significant difference in animals fed a vitamin B6-free diet or control diet. Enzyme mRNA in the liver does not show changes due to diet
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cell line R 1.1: wild-type, Sahn 12: mutant clone
brenda
-
hypertonic stimulation induces association of S-adenosyl-L-homocysteine hydrolase with the F-actin-rich cell cortex. At intermediate, but not higher levels of hypertonicity, the enzyme further translocates from the cortex to the cytosol in company with a fraction of actin and cofilin. At the same time the cells round up. Acidification of the cells stimulates both the cell rounding and the translocation of S-adenosyl-L-homocysteine hydrolase and actin, whereas alkalinization retards these responses
brenda
-
human kidney fibroblast cell line 293T cells: AdoHcyase protein levels and enzymatic activities are significantly higher in human cells infected with the Streptococcus pyogenes SW510 speB mutant strain than in cells infected with the NZ131 wild-type strain
brenda
additional information
-
carbon monoxide lowers renal adenosylhomocysteinase mRNA expression by 64% without change in enzyme activity during 4 h of exposure
brenda
-
enzyme mRNA in the liver does not show changes due to vitamin B6-free diet
brenda
-
cloning and identification of a root-specific promoter from a mutant line of Arabidopsis thaliana exhibiting root-specific expression
brenda
additional information
-
AtSAHH1 has a much higher expression level than AtSAHH2
brenda
additional information
expressed in intracellular stages of Cryptosporidium
brenda
additional information
-
expressed in intracellular stages of Cryptosporidium
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
hypertonic stimulation induces association of S-adenosyl-L-homocysteine hydrolase with the F-actin-rich cell cortex. At intermediate, but not higher levels of hypertonicity, the enzyme further translocates from the cortex to the cytosol in company with a fraction of actin and cofilin. At the same time the cells round up. Acidification of the cells stimulates both the cell rounding and the translocation of S-adenosyl-L-homocysteine hydrolase and actin, whereas alkalinization retards these responses
brenda
additional information
dynamically associated with cytoplasmic strands
brenda
-
dynamically associated with cytoplasmic strands
-
brenda
-
diffuse in nonmotile amoebae. Concentration with F-actin in pseudopods at the front of motile, chemotaxing cells, but not present in filopodia or at the very leading edge
brenda
-
diffuse in nonmotile amoebae. Concentration with F-actin in pseudopods at the front of motile, chemotaxing cells, but not present in filopodia or at the very leading edge
brenda
-
hypertonic stimulation induces association of S-adenosyl-L-homocysteine hydrolase with the F-actin-rich cell cortex. At intermediate, but not higher levels of hypertonicity, the enzyme further translocates from the cortex to the cytosol in company with a fraction of actin and cofilin. At the same time the cells round up. Acidification of the cells stimulates both the cell rounding and the translocation of S-adenosyl-L-homocysteine hydrolase and actin, whereas alkalinization retards these responses
brenda
-
immunodetection of enzyme in nuclei of single interstitial cells of renal cortex and outer medula of hte hypoxic rat
brenda
additional information
dynamically associated punctate structures, and around chloroplasts. The nucleolus is completely devoid of SAHH1
-
brenda
additional information
-
dynamically associated punctate structures, and around chloroplasts. The nucleolus is completely devoid of SAHH1
-
brenda
additional information
-
dynamically associated punctate structures, and around chloroplasts. The nucleolus is completely devoid of SAHH1
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
malfunction
metabolism
physiological function
additional information
drug target
adenosylhomocysteinase inhibitors are promising complementary therapeutic agents in organ transplantation. Inhibitors (AdOx and DZ2002) alleviate allograft rejection in cardiac transplantation by inhibition of CD4+ T alloimmune response
drug target
-
target for antimalarial agents since the parasite has a specific SAH hydrolase. The inhibition of SAH hydrolase causes the intracellular accumulation of S-adenosyl-L-homocysteine (SAH), elevating the ratio of SAH to S-adenosylmethionine (SAM) and inhibiting SAM-dependent methyltransferase that catalyzes methylation of the capped structure at the 5'-terminus of mRNA, and other methylation reaction which is essential for parasite proliferation. In other words, S-adenosyl-L-homocysteine hydrolase regulates methyltransferase reactions. SAH hydrolase inhibitors can be used for the treatment of different diseases like malaria, cancer, viral infection, etc. by ultimately stopping the synthesis of protein
drug target
target for antimalarial agents since the parasite has a specific SAH hydrolase. The inhibition of SAH hydrolase causes the intracellular accumulation of S-adenosyl-L-homocysteine (SAH), elevating the ratio of SAH to S-adenosylmethionine (SAM) and inhibiting SAM-dependent methyltransferase that catalyzes methylation of the capped structure at the 5'-terminus of mRNA, and other methylation reaction which is essential for parasite proliferation. In other words, S-adenosyl-L-homocysteine hydrolase regulates methyltransferase reactions. SAH hydrolase inhibitors can be used for the treatment of different diseases like malaria, cancer, viral infection, etc. by ultimately stopping the synthesis of protein
evolution
S-adenosyl-L-homocysteine hydrolase (SAHH) is one of the most highly conserved enzymes across kingdoms
evolution
-
S-adenosylhomocysteine hydrolase (SAHH) belongs to a large family of proteins that use NAD(P)+/NAD(P)H as cofactors via the dinucleotide-binding Rossmann-fold (a protein structural motif that binds nucleotides, especially the cofactor NAD+)
evolution
two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs. The differences explain the higher NAD+ requirement of tmSAHH because of the reduced affinity and may be related to the thermostability
evolution
evolutionary conserved enzyme governed by multilevel posttranslational control
evolution
evolutionary conserved enzyme governed by multilevel posttranslational control
evolution
-
two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs. The differences explain the higher NAD+ requirement of tmSAHH because of the reduced affinity and may be related to the thermostability
-
evolution
-
two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs. The differences explain the higher NAD+ requirement of tmSAHH because of the reduced affinity and may be related to the thermostability
-
evolution
-
two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs. The differences explain the higher NAD+ requirement of tmSAHH because of the reduced affinity and may be related to the thermostability
-
evolution
-
evolutionary conserved enzyme governed by multilevel posttranslational control
-
malfunction
-
down-regulation of enzyme expression impairs sterol synthesis leading to 4fold elevated squalene levels. Yeast mutants lacking the enzyme are viable
malfunction
-
knockout mutants show a phenotype of slower growth rate, fewer aerial hyphae, loss of orange pigment, absence of asexual fruiting bodies and conidia, and a significant reduction in virulence
malfunction
-
complete loss of SAHH is embryonic lethal, whereas SAHH dysfunction results in numerous pathological consequences such as developmental abnormalities, neurovascular disorders, myopathy, cancer and childhood death
malfunction
overexpression of enzyme SAHH in mammalian cells leads to hypermethylation of the genome, whereas its inhibition by adenosine periodate or siRNA-mediated knockdown results in hypomethylation of the genome. Hypermethylation is consistent in both gene bodies and repetitive DNA elements leading to aberrant gene regulation. Cells overexpressing SAHH specifically upregulate metabolic pathway genes and down-regulate PPAR and MAPK signaling pathways genes. Alteration of SAHH level affects global DNA methylation levels and gene expression
malfunction
the inhibition of SAHH can lead to intracellular SAH accumulation, which triggers the negative feedback inhibition to suppress the S-adenosyl-L-methionine (SAM)-dependent transmethylation
malfunction
-
deletion of the enzyme (FgSAH1) results in defects in vegetative growth, asexual and sexual reproduction, stress responses, virulence, lipid metabolism, and tolerance against fungicides
malfunction
-
knockout mutants show a phenotype of slower growth rate, fewer aerial hyphae, loss of orange pigment, absence of asexual fruiting bodies and conidia, and a significant reduction in virulence
-
malfunction
-
deletion of the enzyme (FgSAH1) results in defects in vegetative growth, asexual and sexual reproduction, stress responses, virulence, lipid metabolism, and tolerance against fungicides
-
metabolism
-
treatment with 50 microg/ml N-nitrosomethylbenzylamine results in twenty-eight differentially expressed protein spots in HEEC cells. Two tumor suppressor proteins, prohibitin and c-Myc binding protein, are down-regulated in NMBA-treated HEEC cells. S-adenosylhomocysteine hydrolase, is up-regulated in NMBA-treated HEEC cells
metabolism
the enzyme is involved in the activated methyl cycle (AMC) of mammalian cells, overview
metabolism
DJ-1 depletion inhibits the transsulfuration pathway by disrupting the formation of the S-adenosyl homocysteine hydrolase tetramer and impairing its activity
physiological function
-
transient application of inhibitor 9-(S)-(2,3-dihydroxypropyl)-adenine on tobacco seeds during 6 days during the germination period. The transient drug treatment induces dosage-dependent global DNA hypomethylation mitotically transmitted to adult plants, pleiotropic developmental defects including decreased apical dominance, altered leaf and flower symmetry, flower whorl malformations and reduced fertility, and dramatic upregulation of floral organ identity genes NTDEF, NTGLO and NAG1 in leaves
physiological function
the enzyme catalyzes the breakdown of S-adenosylhomocysteine, a powerful inhibitor of most transmethylation reactions, to adenosine and L-homocysteine
physiological function
-
the enzyme can promote apoptosis, inhibit migration and adhesion of esophageal squamous cell carcinoma cells suggesting that it may be involved in carcinogenesis of the esophagus
physiological function
-
the enzyme is required for virulence and multiple traits of phenotype in Cryphonectria parasitica by regulation of the expression of genes involved in key process of the cell
physiological function
-
the enzyme participates in the regulation of flagellar regeneration of Dunaliella salina
physiological function
the enzyme plays a key role promoting transmethylation reactions in the secondary cell walls biosynthesis in trees
physiological function
DNA methylation generates S-adenosyl-L-homocysteine, a strong inhibitor of DNMT1. S-adenosylhomocysteine hydrolase (SAHH) is the only mammalian enzyme capable of hydrolyzing S-adenosyl-L-homocysteine. SAHH binds to DNMT1 during DNA replication and enhances DNMT1 activity in vitro, DNMT1 and SAHH interact directly during S-phase, overview
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions. After methyl-group transfer from SAM, S-adenosyl-L-homocysteine (SAH) is formed as a byproduct, which in turn is hydrolyzed to adenosine (Ado) and homocysteine (Hcy) by SAHase
physiological function
S-adenosyl-L-homocysteine hydrolase LvSAHH regulates inflammatory cytokines expression in shrimp
physiological function
-
S-adenosylhomocysteine hydrolase (SAHH) is the only mammalian enzyme capable of hydrolysing S-adenosylhomocysteine (SAH), a potent feedback inhibitor of S-adenosylmethionine (SAM)-dependent methyltransferases which methylate diverse cellular components, including DNA, RNA, proteins, lipids and neurotransmitters. SAM-dependent methylation is central to the regulation of numerous biological processes. A wide spectrum of cellular components, including DNA, RNA, lipids, proteins and neurotransmitters, is subjected to methylation by SAM-dependent methyltransferases. SAM serves as the methyl-group donor during transmethylation reactions, yielding S-adenosylhomocysteine (SAH) as a by-product, which is a strong feedback inhibitor of most SAM-dependent transmethylation reactions. In mammals, S-adenosylhomocysteine hydrolase (SAHH) is the only known enzyme that catalyses the hydrolysis of SAH to homocysteine and adenosine, thereby relieving the inhibition. H19 lncRNA alters DNA methylation genome wide by regulating S-adenosylhomocysteine hydrolase. H19 lncRNA knockdown activates SAHH, leading to increased DNMT3B-mediated methylation of an lncRNA-encoding gene Nctc1 within the Igf2-H19-Nctc1 locus. Genome-wide methylation profiling reveals methylation changes at numerous gene loci consistent with SAHH modulation by H19. SAHH interacts with H19 in ribonucleoprotein complexes. Mode of regulation, overview. The SAM-dependent DNA methyltransferase DNMT3B contributes to SAHH-mediated, H19-dependent methylation change in core muscle enhancer (CME), CME methylation correlates with enhanced Nctc1 transcription. SAHH is required for H19-dependent alteration in CME methylation and Nctc1 transcription
physiological function
SAHH plays a critical role in the mammalian methylation processes
physiological function
the enzyme is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions
physiological function
essential enzyme involved in the regulation of cellular S-adenosyl-L-methionine-dependent methylation reactions
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
-
S-adenosyl-L-homocysteine hydrolase FgSah1 is required for fungal development and virulence in Fusarium graminearum
physiological function
the enzyme catalyzes the hydrolysis of SAH to homocysteine in the transsulfuration pathway. DJ-1 determines the formation of the S-adenosyl homocysteine hydrolase tetramer and its enzymatic activity by altering the interaction between S-adenosyl homocysteine hydrolase and its negative regulator AHCYL1. DJ-1 depletion inhibits the transsulfuration pathway by disrupting the formation of the S-adenosyl homocysteine hydrolase tetramer and impairing its activity
physiological function
the enzyme is required to maintain trans-methylation reactions in different cellular compartments
physiological function
the enzyme is required to maintain trans-methylation reactions in different cellular compartments
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
the enzyme is required for virulence and multiple traits of phenotype in Cryphonectria parasitica by regulation of the expression of genes involved in key process of the cell
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase FgSah1 is required for fungal development and virulence in Fusarium graminearum
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
the enzyme is required to maintain trans-methylation reactions in different cellular compartments
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
additional information
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
additional information
-
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
additional information
overall structure of the inactive form of TmSAHase, overview
additional information
-
overall structure of the inactive form of TmSAHase, overview
additional information
the substrate-binding domain comprises residues 1-181 and 355-385. It is an alpha/beta-type structure consisting of eight alpha-helices and eight beta-strands. The structural core in the domain is an eight-stranded parallel beta-sheet in the centre of the domain that is sandwiched by two arrays of three alpha-helices each. Conformational changes upon substrate binding, overview
additional information
the substrate-binding domain, built from amino acid residues Gly6-Val221 and Met397-Val426, has an alpha/beta-fold. The central parallel beta-sheet is built from seven beta-strands, structure overview. The C-terminal domain, formed by residues Leu427-Tyr473, has a helix-loop-helix-loop fold. Ligand-induced conformational change. Adenosine-binding site in the ligand-free subunit
additional information
-
a coupled photometric assay for characterization of S-adenosyl-L-homocysteine hydrolases in the physiological hydrolytic direction is developed. The assay is a valuable tool for in vitro characterization of SAHases with biotechnological potential, and for monitoring SAHase activity in diagnostics
additional information
-
overall structure of the inactive form of TmSAHase, overview
-
additional information
-
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
-
additional information
-
overall structure of the inactive form of TmSAHase, overview
-
additional information
-
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
-
additional information
-
overall structure of the inactive form of TmSAHase, overview
-
additional information
-
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
-
Show AA Sequence and Transmembrane Helices (34540 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180000
190000
200000
210000
46000
47000
48000
50000
52000
55000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homotetramer
monomer
tetramer
trimer
additional information
dimer
-
intramolecular cross-linking show that SAH-L is a dimer. The incompatible molecular weight values shown by SDS-PAGE and gel filtration implicate an irregular structure of SAH-L. SAH-L is partially purified in a form lacking the 31 N-terminal residues, and is found to be extremely susceptible to proteases in the region around residue 70
dimer
2 * 46000, SDS-PAGE, the cyanobacterial enzyme is in an equilibrium of two distinct oligomeric states corresponding to its dimeric and tetrameric forms in solution
homotetramer
the protein crystallizes in its biologically relevant tetrameric form, a dimer of two tight dimers (AB and CD)
homotetramer
each subunit of the tetrameric enzyme is composed of three domains, namely the catalytic domain, the NAD+-binding domain and the C-terminal domain
homotetramer
-
each subunit of the tetrameric enzyme is composed of three domains, namely the catalytic domain, the NAD+-binding domain and the C-terminal domain
-
homotetramer
-
each subunit of the tetrameric enzyme is composed of three domains, namely the catalytic domain, the NAD+-binding domain and the C-terminal domain
-
homotetramer
-
each subunit of the tetrameric enzyme is composed of three domains, namely the catalytic domain, the NAD+-binding domain and the C-terminal domain
-
monomer
-
1 * 55000, pore gradient gel electrophoresis, only dimeric form is enzymatically active
tetramer
three subunits are in a closed conformation enforced by complex formation with the adenosine product of the enzymatic reaction. The fourth subunit is ligand-free and has an open conformation. Domain movement of the enzyme induced by the binding of its natural ligands. The centre of the tetramer is formed by the cofactor-binding domains, while the substrate-binding domains are located outside the core of the enzyme, where they are much more mobile than the rigid central part
tetramer
the asymmetric unit of the enzyme (ChSAHase) crystal contains four subunits of the enzyme. They do not form one functional tetrameric unit. They are assembled into two dimers, located at two different crystallographic twofold axes, whose operation recreates two tetramers that are related by non-crystallographic translation
tetramer
-
the asymmetric unit of the enzyme (ChSAHase) crystal contains four subunits of the enzyme. They do not form one functional tetrameric unit. They are assembled into two dimers, located at two different crystallographic twofold axes, whose operation recreates two tetramers that are related by non-crystallographic translation
-
tetramer
4 * 46000, SDS-PAGE, the cyanobacterial enzyme is in an equilibrium of two distinct oligomeric states corresponding to its dimeric and tetrameric forms in solution
additional information
analysis of domain organization of substrate-binding domain, NAD+ cofactor-binding domain and dimerization domain in the subunits, quaternary interactions between the subunits, overview
additional information
the subunit of MmSAHH consists of two large domains separated by a cleft containing a deep pocket, two hinge regions and a small C-terminal domain that is separate from the main body of the subunit and extends to the adjacent subunit. One of the large domains is responsible for cofactorbinding, and the other is necessary for substrate binding. The two large domains are unequal in size. The substrate-binding domain is larger and comprises 212 residues, whereas the cofactor-binding domain comprises 155 residues. Amino acid sequence comparisons
additional information
calorimetric evaluation of heat-induced conformational changes at 85°C and oligomeric state
additional information
-
calorimetric evaluation of heat-induced conformational changes at 85°C and oligomeric state
additional information
-
calorimetric evaluation of heat-induced conformational changes at 85°C and oligomeric state
-
additional information
-
calorimetric evaluation of heat-induced conformational changes at 85°C and oligomeric state
-
additional information
-
calorimetric evaluation of heat-induced conformational changes at 85°C and oligomeric state
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
Lys401 and Lys408 acetylation of the enzyme changes hydrogen bonding patterns in its NAD+ binding regions and reduces its catalytic activity
phosphoprotein
phosphoprotein
-
phosphorylation at Thr2 and Thr221 negatively affects enzymatic activity
phosphoprotein
-
phosphorylation at Thr2 and Thr221 negatively affects enzymatic activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
crystallization is conducted by vapour diffusion in hanging drops at 19°C. Crystal structure is solved at a resolution of 1.74 A, revealing a homotetramer in the asymmetric unit of space group P2(1)2(1)2
hanging drop vapor diffusion method, using 0.2 M ammonium acetate, 20%(w/v) polyethylene glycol 3350, pH 7.1
purified recombinant detagged enzyme, hanging drop vapour diffusion method, mixing of 12 mg/ml protein in 20 mM Tris, pH 8.0, 50 mM NaCl, with reservoir solution consisting of 0.2 M ammonium acetate, 20% w/v PEG 3350, pH 7.1, 18°C, X-ray diffraction structure determination and analysis at 1.74 A reoslution, molecular replacement using the atomic coordinates of chain A of SAHase from Brucella melitensis (PDB ID 3n58) as template, modelling
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
enzyme in ternary complex with the oxidized form of the NAD+ cofactor and adenosine, hanging drop vapor diffusion method, using 15 % (w/v) PEG 8000 and 0.5 M Li2SO4
hanging-drop vapor-diffusion method, crystals are orthorhombic, space group P2(1)2(1)2 with unit cell parameters a = 96.28, b = 102.44, and c = 188.92 A
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
hanging drop vapor diffusion method, using 200 mM sodium formate, 5-20% (w/v) PEG 3350, and 100 mM BisTris, pH 6.0-6.5
hanging-drop vapor-diffusion method, complex of the enzyme with neplanocin A
in complex with mechanism-based inhibitor fluoroneplanocin A. The crystallized enzyme complex shows the closed conformation and turns out to be the intermediate of mechanism-based inhibition. The cofactor depletion by 3'-oxidation of fluoroneplanocin A contributes to the enzyme inhibition along with the irreversible covalent modification of enzyme
performance of Brownian dynamics simulations by building a coarse-grained model based on the holo and ligand-bound structures, in order to study the link between the allosteric communication and functional dynamics. Upon ligand-induced transition, the signal of intra-subunit closure dynamics is transmitted to form inter-subunit contacts, which in turn invoke a precise alignment of active site, followed by the dimer-dimer rotation that compacts the whole tetrameric structure. Analysis provides evidence of both induced fit and population shift mechanisms, and also shows that the transition state ensemble is akin to the ligand-bound state. Besides the formation of enzyme-ligand contacts at the active site, the allosteric couplings from the residues distal to the active site is vital to the enzymatic function
purified enzyme in complex with inhibitor N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(methylamino)ethyl]glycinamide hydrochloride, sitting drop vapor diffusion method, using a reservoir solution composed of 100 mM HEPES, pH 7.5, 13% w/v PEG 4000, 10% v/v 2-PrOH, and 0.5% v/v EtOAc, X-ray diffraction structure determination and analysis at 2.7 A resolution, modelling
-
substrate-free wild-type enzyme exhibits reorientational motions on time scales of 10-20 and 80-90 ns. The faster motion is attributed to the domain motion, and the slower motion is attributed to the tumbling of enzyme. The domain motion is present in enzyme complexes with NADH/3'-keto-adenosine and NAD+/3'-deoxyadenosine, but absent in complexwith NADH/3-keto-neplaocin A
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
crystals of LlSAHase in complex with adenosine are obtained by the hanging-drop vapour-diffusion method using 20% (w/v) PEG 4000 and 10% (v/v) 2-propanol as precipitants in 0.1 M Tris-HCl buffer pH 8.0. The crystals are tetragonal, space group P43212, with unit-cell parameters a = 122.4, c = 126.5 A and contained two protein molecules in the asymmetric unit, corresponding to the functional dimeric form of the enzyme. Atomic resolution (1.17 A) X-ray diffraction data are collected using synchrotron radiation
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
purified enzyme SAHH in complex with adenosine and with two reaction intermediate analogues, 3'-keto-aristeromycin (3KA) and noraristeromycin (NRN), X-ray diffraction structure determination and analysis at resolutions of 1.55, 1.55, and 1.65 A, respectively
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
crystal structure of SAHH in complex with adenosine (ADO) and nicotinamide adenine dinucleotide and with three inhibitors is shown: 3'-keto aristeromycin, 2-fluoroadenosine, and 3-deazaadenosine. The 3'-keto aristeromycin complex is the first reported structure of SAHH complexed with this inhibitor, and confirms the oxidation of the 3'-hydroxyl to a planar keto group, consistent with its prediction as a mechanism-based inhibitor. The 2.0 A resolution structure of the complex of SAHH cocrystallized with S-adenosylhomocysteine is reported. Binding of homocysteine forces a rotation of His363 around the backbone to flip out of contact with the 5 hydroxyl of the adenosine and opens access to a nearby channel that leads to the surface. This complex suggests that His363 acts as a switch that opens up to permit binding of substrate, then closes down after release of the cleaved homocysteine
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
crystal structure of PfSAHH complexed with the reaction product adenosine. Crystals belong to an orthorhombic space group P2(1)2(1)2(1) with cell dimensions of a = 77.09 A, b = 86.15 A, and c = 333.8 A
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
vapor diffusion method. Crystals belong to an orthothombic space group P2(1)2(1)2(1) with the cell dimensions of a = 76.66 A, b = 86.31 A, c = 335.6 A, four subunits per asymmetric unit, 2.8 A resolution
-
purified recombinant detagged wild-type and mutant enzymes free or in complex with 2'- or 3'-deoxyadenosine, adenosine, or Zn2+, hanging drop vapor diffusion method, 20 mg/ml protein in 100 mM KCl or RbCl, 25 mM HEPES-KOH, pH 7.5, 1 mM TCEP-HCl, mixing with 2 mM of adenosine (Ado/K+/Zn2+), 2'-deoxyadenosine (2'-dAdo/K+/Zn2+ or 2'-dAdo/Rb+), or 3'-deoxyadenosine (3'-dAdo/K+) at 4°C, for crystallization mixing of 0.002 ml of 10 mg/ml protein-ligand solution with 0.002 ml of reservoir solution containing 20% w/v PEG8000 and 50 mM KH2PO4 (Ado/K+/Zn2+ and 2'-dAdo/K+/Zn2+), or 20% w/v PEG8000 and 50 mM RbH2PO4 (2'-dAdo/Rb+), or 15% w/v PEG8000, 50 mM KH2PO4 and 20% v/v glycerol (3'-dAdo/K+), 19°C, X-ray diffraction structure determination and analysis at 1.35 A (3'-dAdo/K+), 1.45 A (2'-dAdo/Rb+), 1.60 A (Ado/K+/Zn2+), or 1.75 A (2'-Ado/K+/Zn2+) resolution, molecular replacement using a subunit of Homo sapiens SAHase as search model (PDB ID 1LI4, chain A)
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
in complex with (2R,3R)-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid and NAD+, batch method with 15% (w/v) PEG 8000, 50 mM MES buffer pH 6.5, and 2% (v/v) glycerol
molecular dynamics simulations of substrate-free enzyme in solution. The four substrate-binding domains retain internal structures similar to the crystal conformation. The domains within each subunit fluctuate between open and closed conformations, while at the tetramer level 80% of the domain motions are perpendicular to the direction of the open-to-closed structure transition. Domain reorientation in solution are the sum of a faster and a slower component of 20-50 ps and 8-23 ns, respectively
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
purified recombinant enzyme free or in complex with adenosine, hanging drop vapour diffusion method, mixing of 0.002 ml of 6 mg/ml protein in 100 mM NaCl, and 25 mM Tris-HCl, pH 8.0, with 0.002 ml of reservoir solution containing 20 mM MgCl2 or CaCl2, 0.1 M sodium acetate, pH 4.6 or pH 5.3, and 30% v/v MPD for crystal structure 1 or 2, respectively, with or without addition of adenosine, 18°C, X-ray diffraction structure determination and analysis at 1.75-1.90 A resolution, molecular replacement using the substrate-binding (residues 18-181 and 355-421) and cofactor-binding (182-354) domains of a model of Homo sapiens SAHase (PDB ID 1LI4) as search model
purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 150 mM NaCl, 25 mM Tris-HCl, pH 7.5, 10 mM DTT, and 2 mM NAD+ with 0.001 ml of reservoir solution containing 4.3 M NaNO3, and 0.1 M NaAc, pH 4.6, and equilibration against 0.3 ml of reservoir solution at room temperature, method optimization, X-ray diffraction structure determination and analysis at 2.04 A resolution. Crystals of tmSAHH in complex with both SAH and NAD+ are obtained by soaking and cocrystallization with resolution at 2.85 A. Molecular replacement using the Rattus norvegicus SAHH structure, PDB ID 1B3R, as search model
sitting drop vapor diffusion method, using 0.3 M calcium acetate hydrate, 0.1 M sodium cacodylate trihydrate pH 6.5, and 8% (w/v) polyethylene glycol 8000
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
-
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M291T
positional cloning identifies a causative mutation in the gene encoding Ahcy (missense mutation in exon 8, mutation resides in the NAD-binding domain), leading to hepatic steatosis and liver degeneration. Reduced Ahcy activity in mutants leads to elevated levels of S-adenosylhomocysteine (SAH) and of its metabolic precursor S-adenosylmethionine. Elevated SAH in mutant larvae is associated with mitochondrial defects and increased expression of tnfa and pparg, an ortholog of the mammalian lipogenic gene. Antisense knockdown of tnfa rescues hepatic steatosis and liver degeneration in mutant larvae
A89V
-
more than 70% decrease in enzyme activity and decrease in unfolding temperature by 5.5°C. Subunits assemble similarly to wild-type, but electrophoretic mobility is faster than wild-type
A89V/T84S
-
restores most of the catalytic activity of mutant A89V due to loss of sterical incompatibility of V89 and T84
D293A
the mutant shows reduced catalytic efficiency with S-adenosyl-L-homocysteine compared to the wild type enzyme and no reaction with L-homocysteine
D86E
replacing Asp86 with negatively charged Glu86 in mutant protein maintains enzymatic activity to 70% of wild-type, Km (mM) (S-adenosyl-L-homocysteine) similar to wild-type
D86G
protein tends to form enzymatically inactive aggregates and the loss of a single negative charge as a result of the mutation is involved in enzyme inactivation
E115L
about 30-40% loss of activity both for hydrolysis and synthesis of S-adenosylhomocysteine
H353A
mutation changes the hinge-dynamics of enzyme, domain motion cannot be detected
N27K
the mutant shows reduced catalytic efficiency with S-adenosyl-L-homocysteine compared to the wild type enzyme and no reaction with L-homocysteine
Q85A
-
kcat/Km is 13.45fold lower then wild-type value. Ki-value for noraristeromycin is 4.46fold higher than wild-type value, Ki-value for 2-fluoronoraristeromycin is 5.6fold higher than wild-type value
R49C
mutant shows dramatically reduced AHCY activity, mutant protein forms intermolecular disulfide bonds, leading to macromolecular structures that can be prevented by reducing agent DTT
R49C/D86G
a new missense mutation is found in the AHCY gene from a case of AHCY deficiency in an infant girl who died at age four months
T60A
-
kcat/Km is 1.23 fold lower then wild-type value. Ki-value for noraristeromycin is 3.3fold lower than wild-type value, Ki-value for 2-fluoronoraristeromycin is 23fold lower than wild-type value
T60C
-
kcat/Km is 2.3fold lower then wild-type value. Ki-value for noraristeromycin is 1.2fold higher than wild-type value, Ki-value for 2-fluoronoraristeromycin 11fold lower than wild-type value
T60S
-
kcat/Km is 1.6fold higher then wild-type value. Ki-value for noraristeromycin is 2.3fold lower than wild-type value, Ki-value for 2-fluoronoraristeromycin is 50fold lower than wild-type value
Y143C
about 70% loss of activity both for hydrolysis and synthesis of S-adenosylhomocysteine
Y430A
mutation alters the NAD+ association and dissociation kinetics, increasing the cofactor equilibrium dissociation constant from approximately 10 nM to about 800 nM
Q65A
A84Q
kcat/Km is 1.2fold higher then wild-type value. Ki-value for noraristeromycin is 1.2fold lower than wild-type value, Ki-value for 2-fluoronoraristeromycin is 1.3fold lower than wild-type value
C59S
kcat/Km is 1.5fold lower then wild-type value. Ki-value for noraristeromycin is 1.1fold higher than wild-type value, Ki-value for 2-fluoronoraristeromycin is 1.2fold lower than wild-type value
C59T
kcat/Km is 1.1fold higher then wild-type value. Ki-value for noraristeromycin is 1.4fold lower than wild-type value, Ki-value for 2-fluoronoraristeromycin more than 6.5fold higher than wild-type value
R24E
substrate affinity (Km) is not affected by the R24E substitution
K431A
-
mutant loses its cofactor binding affinity but retains the wild type's tetrameric structure
Y435A
-
mutation alters the NAD+ association and dissociation kinetics, Y435A increases the cofactor equilibrium dissociation constant from approximately 100 nM to about 1 mM
additional information
Q65A
site-directed mutagenesis, the mutant shows altered metal binding compared to the wild-type
Q65A
-
site-directed mutagenesis, the mutant shows altered metal binding compared to the wild-type
-
Q65A
-
site-directed mutagenesis, the mutant shows altered metal binding compared to the wild-type
-
Q65A
-
site-directed mutagenesis, the mutant shows altered metal binding compared to the wild-type
-
Q65A
-
site-directed mutagenesis, the mutant shows altered metal binding compared to the wild-type
-
Q65A
-
site-directed mutagenesis, the mutant shows altered metal binding compared to the wild-type
-
Q65A
-
site-directed mutagenesis, the mutant shows altered metal binding compared to the wild-type
-
Q65A
-
site-directed mutagenesis, the mutant shows altered metal binding compared to the wild-type
-
additional information
-
identification of mutants affected in biocontrol properties. Mutant, M9-22 fails to biocontrol, is impaired in both growth in minimal medium and siderophore production, and fails to produce detectable levels of agrocin 84. The chromosomal gene ahcY, which encodes S-adenosyl-L-homocysteine hydrolase, is disrupted in this mutant
additional information
-
identification of mutants affected in biocontrol properties. Mutant, M9-22 fails to biocontrol, is impaired in both growth in minimal medium and siderophore production, and fails to produce detectable levels of agrocin 84. The chromosomal gene ahcY, which encodes S-adenosyl-L-homocysteine hydrolase, is disrupted in this mutant
-
additional information
-
a T-DNA insertion mutant of AtSAHH1 and the RNAi plants (dsAtSAHH2) accumulate a higher level of cytokinins, exhibited phenotypic changes similar to those of cytokinin-overproducers, and their global DNA methylation status is reduced. Cytokinins positively regulate the transmethylation pathway genes, including AtSAHH1, adenosine kinase1, and this regulation involves the cytokinin activity. Expression of three cytosine DNA methyltransferase genes examined is inducible by cytokinin treatment. Changing of endogenous cytokinin levels by transgene expression results in alterations of DNA methylation status in the sahh1-1 background, suggesting that cytokinins promote DNA methylation
additional information
-
HEK-293 cell lines stably overexpressing AdoHcyase are generated. 2-5fold overexpression of AdoHcyase is well tolerated by the cell, while greatly enhanced AdoHcyase activity results in adenosine-induced apoptosis. The fact that enhanced AdoHcyase activity does not increase transmethylation activity suggests that AdoHcyase activity under physiological conditions is not rate limiting for efficient transmethylation
additional information
comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes
additional information
-
SAHH inactivation in human IMR-90 cells and HEK-293 cells confers resistance to both p53 and p16INK4-induced proliferation arrest. SAHH inactivation inhibits p53 transcriptional activity and impairs DNA damage-induced transcription of p21Cip1
additional information
-
SAHH inactivation in mouse embryonic fibroblast cells and NIH3T3 cells confers resistance to both p53 and p16INK4-induced proliferation arrest. SAHH inactivation inhibits p53 transcriptional activity and impairs DNA damage-induced transcription of p21Cip1
additional information
-
SAHH mRNA is lost in 50% of tumor tissues from 206 patients with different kinds of tumors in comparison with normal tissue counterparts
additional information
knockdown of LvSAHH in shrimps affects expression levels of LvRack1, LvToll1, LvToll2, LvToll3 and LvIL-16 transcripts after infection with Vibrio alginolyticus
additional information
-
knockdown of LvSAHH in shrimps affects expression levels of LvRack1, LvToll1, LvToll2, LvToll3 and LvIL-16 transcripts after infection with Vibrio alginolyticus
additional information
-
down-regulation of SAH1 expression in yeast leads to accumulation of S-adenosyl-L-homocysteine and decreased de novo phosphatidylcholine synthesis in vivo. This decrease is accompanied by an increase in triacylglycerol levels, demonstrating that Sah1-regulated methylation has a major impact on cellular lipid homeostasis. In cells with down-regulated Sah1 activity major alterations in the expression of the inositol-3-phosphate synthase gene as well as in the localization of Opi1, a negative regulatory factor of phospholipid synthesis, which binds and is retained in the endoplasmic reticulum membrane by phosphatidic acid in conjunction with VAMP/synaptobrevin-associated protein, Scs2 is found
additional information
-
comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
wild-type in 70% formic acid for 24 h at 37°C: cleavage into 2 peptides of 26000 and 21000 Da
137138
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
50
55
75
80 - 100
-
the apparent melting temperature is 87.6°C. After 10 min incubation at 80, 85, 90, 95, and 100°C the enzyme shows residual activity of about 97%, 70%, 20%, 8%, and 1%, respectively
90
95
50
15 min, wild-type, stable, mutant E115L, 43% loss of activity, mutant Y143C, 50% loss of activity
55
15 min, wild-type, 50% loss of activity, complete loss of activity for mutants Y143C and E115L
75
the enzyme exhibits extreme thermostability and retains 95% enzyme activity after incubation at 75°C for 2 h
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after exposure to 10.4 GHz microwave radiation at 90°C the enzyme retains 18% activity after 40 min irradiation compared to a control incubated at the same temperature without irradiation. Addition of KCl or KH2PO4 to the enzymatic solution exposed to microwaves does not cause any further effect on enzyme inactivation.
-
freezing and thawing in absence of glycerol causes formation of multimers, low thiol concentrations and exposure to atmospheric O2 fortifies aggregate formation
-
isozymes become unstable after DEAE-cellulose chromatography, ternary tRNA complexes are most stable form of enzymes, testosterone promotes formation of ternary complexes and prevents inactivation, hyperphysectomy leads to dissociation of ternary complexes and to loss of specific activity, stability of enzyme also improved by 5alpha-dihydrotestosterone
-
the enzyme is stable in the presence of urea 6 M when pre-incubated at room temperature for 48 h
-
the immobilization of the enzyme on Eupergit C does not alter its specific activity
-
unstable in solutions containing low level of protein, stabilization with bovine serum albumin
-
unusual stability in protein denaturants and detergents, complete recombinant enzyme
-
wild-type and D244E rather resistant to inactivation by trypsin, wild-type resistant to chymotrypsin, D224E loses 63% of activity after treatment with chymotrypsin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
-
6 M, 48 h at room temperature, no loss of activity
urea
urea
the enzyme is stable in the presence of urea 6 M when pre-incubated at room temperature for 48 h
urea
-
the enzyme is stable in the presence of urea 6 M when pre-incubated at room temperature for 48 h
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol essential for enzymatic activity, in absence 50% loss of activity
-
137134
reducing agent such as 2-mercaptoethanol essential for maintenance of catalytic activity
reducing agent such as 2-mercaptoethanol essential for maintenance of catalytic activity
-
137130
reducing agent such as 2-mercaptoethanol essential for maintenance of catalytic activity
-
137130
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, progressive inactivation especially in absence of reducing agents as e.g. 2-mercaptoethanol
-20°C, 20 mM Tris-HC1, pH 8, containing 1 mM EDTA, stable for at least 2 months
-
-20°C, 50 mM phosphate buffer pH 6.5, at least 3 months, no loss of activity
-
-20°C, pH 6.5, 50 mM phosphate buffer, stable for at least 3 months
-20°C, stability of the adenosine binding site is reduced from Kd 6.8 to 29 nM within 4 months
-
-20°C, wild-type enzyme is robust and retains activity for at least one year with several freeze-thaw cycles. Mutant A89V, stable for about 1 month
-
-20°C, with 5 mM beta-mercaptoethanol and 2 mg/ml bovine serum albumin, stable for several months
-
-80°C, intestinal mucosa enzyme, crude preparation, stable for at least 1 week
-
-80C, storage in liquid nitrogen also possible, 2-20 mg enzyme per ml, stable for at least 1 year
0°C, stable in 100 mM potassium phosphate containing 5 mM dithiothreitol, with 1 mM dithiothreitol the enzyme is stable for 1 month but losing activity thereafter rapidly
-
4°C, sterilized enzyme at a concentration of 2-4 mg/ml, in buffer C, stable for at least 2 months
-
4°C, the enzyme is spontaneously inactivated in one month, in the presence of 10% glycerol the stability of the enzyme increases up to 80%
-
-18C, progressive inactivation especially in absence of reducing agents as e.g. 2-mercaptoethanol
-
-18C, progressive inactivation especially in absence of reducing agents as e.g. 2-mercaptoethanol
-
-80C, storage in liquid nitrogen also possible, 2-20 mg enzyme per ml, stable for at least 1 year
-
-80C, storage in liquid nitrogen also possible, 2-20 mg enzyme per ml, stable for at least 1 year
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex S200 gel filtration
immobilized nickel-affinity column chromatography, and gel filtration
Ni-NTA column chromatography
partial
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3) by nickel affinity chromatography, followed by tag cleavage through TEV protease, dialysis, another step of nickel affinity chromatography, ammonium sulfate fractionation, and ultrafiltration, gel filtration, and again ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by nickel affinity chromatography and dialysis
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-CodonPlus(DE3) by nickel affinity chromatography followed by tag cleavage through TEV protease, dialysis, another step of nickel affinity chromatography, ammonium sulfate fractionation, gel filtration, and ultrafiltration
recombinant His6-tagged enzyme from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography, tag cleavage by TEV protease, another step of nickel-affinity chromatography to remove the His-tag debris and His-tagged TEV protease, followed by gel filtration
recombinant His6-tagged enzyme from Pichia pastoris by nickel affinity chromatography
tangential ultrafiltration and immobilized metal affinity chromatography
-
to homogeneity
truncated recombinant enzyme: 71.7fold, complete recombinant enzyme: to homogeneity
-
using Ni-NTA chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Escherichia as a C-terminal His-tagged fusion protein. SAH-L is partially purified in a form lacking the 31 N-terminal residues, and is found to be extremely susceptible to proteases
-
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells
expression in Escherichia coli
expression in Escherichia coli BL21
expression in Escherichia coli, fusion protein
expression of mutant enzymesC59T, C59S and A84Q in Escherichia coli
gene ahcY, phylogenetic analysis, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-CodonPlus(DE3)
gene sahH, codon-optimized gene, recombinant expression of C-terminally His6-tagged enzyme in Pichia pastoris under control of the strong AOX1 promoter
gene sahH, COS7 cells are transfected with plasmids encoding GFP-tagged SAHH and DsRed-tagged DNMT1 for a co-localization studies between DNMT1 and SAHH, which shows that both DsRed-DNMT1 and GFP-SAHH are co-localized and appear in the nucleus
gene sahH, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)
gene sahH, sequence comparisons and phylogenetic tree, quantitative real-time PCR enzyme expression analysis, recombinant expression of FLAG-tagged enzyme in Escherichia coli strain BL21
gene sahH, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
into Escherichia coli
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 Star (DE3)
expressed in Escherichia coli as a His-tagged fusion protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
LvSAHH mRNA expression levels in hepatopancreas and gill are significantly upregulated from 6 to 48 h after Vibrio alginolyticus strain ATCC33787 injection and reach the highest level after 24 h
the enzyme is downregulated in esophageal squamous cell carcinoma cells compared with normal esophageal epithelial cells
-
the enzyme is upregulated both at the protein and the transcription levels during pH shock-triggered flagellar regeneration of Dunaliella salina
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
drug development
because of the prominent role of SAM-dependent transmethylation in capped methylated structure production at the 5'-terminus of viral mRNA, SAHH inhibitors could be developed to be broad-spectrum antiviral agents
medicine
molecular biology
agriculture
-
high priority genes for follow-up biochemical and physiological studies on the mechanisms of Al tolerance in maize are AltSB like ZmASL, aluminum-activated malate transporter ALMT2, S-adenosyl-L-homocysteinase SAHH, and malic enzyme ME
agriculture
-
quantitative, high-throughput biocontrol assay that can be applied to the screening of large numbers of mutants of strain K84 under conditions that mimic the control of crown gall disease in the field by this widely successful biocontrol agent. The basis for this bioassay relies on the careful optimization of the populations of the biocontrol agent and the challenge pathogen, and gives a reproducible 100% level of infection in the absence of the biocontrol agent and 100% control when strain K84 is introduced
agriculture
-
quantitative, high-throughput biocontrol assay that can be applied to the screening of large numbers of mutants of strain K84 under conditions that mimic the control of crown gall disease in the field by this widely successful biocontrol agent. The basis for this bioassay relies on the careful optimization of the populations of the biocontrol agent and the challenge pathogen, and gives a reproducible 100% level of infection in the absence of the biocontrol agent and 100% control when strain K84 is introduced
-
analysis
-
simple colorimetric method for the sensitive detection of S-adenosylhomocysteine hydrolase activity and inhibition using fluorosurfactant-capped gold nanoparticles. After hydrolysis of S-adenosylhomocysteine, the produced homocysteine molecules are bound to the surface of Au nanoparticles through the formation of Au-S bonds. The approach has a minimum detectable concentration of 100 units/l, or about 6 nM. The addition of adenosine analogs to a solution containing S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase results in the suppression of hydrolyzed S-adenosylhomocysteine-induced nanoparticle aggregation
medicine
-
development of a specific inhibitor for Plasmodium falciparum SAH hydrolase as a chemotherapeutic agent against malaria
medicine
-
SAH hydrolase is an attractive target for antiparasitic and antiviral drug design
medicine
SAHH inhibitors are expected to provide a new type of chemotherapeutic agent against malaria
medicine
-
adenosine-induced apoptosis is likely due to intracellular action of enzyme resulting in altered gene expression and is independent of AMP-activated kinase and adenosine receptors
medicine
-
carbon monoxide lowers renal adenosylhomocysteinase mRNA expression by 64% without change in enzyme activity during 4 h of exposure. Immunodetection of enzyme in nuclei of single interstitial cells of renal cortex and outer medula of the hypoxic rat
medicine
in rats fed by the enzyme inhibitors (2R,3R)-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid and (2R,3R)-methyl-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid, the total plasma cholesterol and phospholipids decrease by 36-40% and 23%, respectively
medicine
-
S-adenosylhomocysteine-synthetic activity significantly increases in animals fed a vitamin B6-free diet, while S-adenosylhomocysteine hydrolytic activity shows no significant difference in animals fed a vitamin B6-free diet or control diet. Enzyme mRNA in the liver does not show changes due to diet
medicine
-
the cofactor NAD+ always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme
medicine
-
the cofactor NAD+ always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme
medicine
AHCY polymorphisms and AHCY inhibitors, which are promising in treating autoimmunity and other disorders, may be a risk factor for steatosis, particularly in patients with diabetes, obesity and liver disorders such as hepatitis C infection
medicine
-
Sah1 activity has a major impact on cellular lipid homeostasis, and its deficiency results in dysregulated lipid metabolism, leading to an imbalance of phospholipid and triacylglycerol synthesis, with implications for mammalian lipid-associated disorders
medicine
identification of 39 polymorphisms by sequencing 240 DNA samples from Caucasian-American, African-American, Han Chinese-American and Mexican-American subjects. Four single nucleotide polymorphisms are associated with decreased expression
medicine
-
in lymphoblastoid cell lines from patients with Down syndrome, an increase in NAD(P)H:quinone oxidoreductase and S-adenosylhomocysteine hydrolase activities is found
medicine
-
over-expression of Down-syndrome associated kinase Dyrk1a increases the hepatic NAD(P)H:quinone oxidoreductase and S-adenosylhomocysteine hydrolase activities, concomitant with decreased level of plasma homocysteine in three mice models overexpressing Dyrk1a. These effects are abolished by treatment with harmine, the most potent and specific inhibitor of Dyrk1a
medicine
-
identification of 27 immunogenic proteins from the two-dimensional electrophoresis immunoblot profiles by liquid chromatography tandem MS and expression of the gene encoding one immunodominant protein of interest, S-adenosyl-L-homocysteine hydrolase in Escherichia coli. The recombinant protein induces a strong antibody response in BALB/c mice, and the polyclonal antibody recognizes a band of approximately 52 kDa in the immunoblots of soluble protein extracts from five Brucella strains. The recombinant protein significantly stimulates the production of interferon-gamma and interleukin-2, and induces a high level of protection against Brucella melitensis 16M challenge at 4 weeks postchallenge
medicine
-
identification of 27 immunogenic proteins from the two-dimensional electrophoresis immunoblot profiles by liquid chromatography tandem MS and expression of the gene encoding one immunodominant protein of interest, S-adenosyl-L-homocysteine hydrolase in Escherichia coli. The recombinant protein induces a strong antibody response in BALB/c mice, and the polyclonal antibody recognizes a band of approximately 52 kDa in the immunoblots of soluble protein extracts from five Brucella strains. The recombinant protein significantly stimulates the production of interferon-gamma and interleukin-2, and induces a high level of protection against Brucella melitensis 16M challenge at 4 weeks postchallenge
-
molecular biology
-
a coupled fluorescent assay for histone methyltransferase utilizes S-adenosylhomocysteine hydrolase to hydrolyze the methyltransfer product S-adenosylhomocysteine to homocysteine and adenosine. The homocysteine concentration is then determined through conjugation of its free sulfhydryl moiety to a thiol-sensitive fluorophore. the assay allows rapid and facile determination of histine methyltransferase kinetics and can be adapted to measure the enzymatic activity of a wide variety of S-adenosylmethionine-dependent methyltransferases
molecular biology
-
AdoHcyase overexpression results in elevated adenosine levels and decreased cell viability. Furthermore, AdoHcyase overexpressing cells show different features typical for apoptosis (cell detachment, caspase-like activity, DNA fragmentation), suggesting that cell death is due to apoptosis
molecular biology
-
Streptococcal pyrogenic exotoxin B cleaves human S-adenosylhomocysteine hydrolase and induces hypermethioninemia
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.13.2.1)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
