Information on EC 2.7.4.10 - nucleoside-triphosphate-adenylate kinase

Word Map on EC 2.7.4.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.4.10
-
RECOMMENDED NAME
GeneOntology No.
nucleoside-triphosphate-adenylate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
nucleoside triphosphate + AMP = nucleoside diphosphate + ADP
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Purine metabolism
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:AMP phosphotransferase
Many nucleoside triphosphates can act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-74-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strains BY4741 and D273-10B
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AMP + GTP
ADP + GDP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP
show the reaction diagram
CTP + AMP
CDP + ADP
show the reaction diagram
dGTP + dAMP
dGDP + dADP
show the reaction diagram
-
-
-
-
r
GTP + AMP
GDP + ADP
show the reaction diagram
GTP + IMP
GDP + IDP
show the reaction diagram
-
-
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
nucleoside triphosphate + AMP
nucleoside diphosphate + ADP
show the reaction diagram
-
involved in reaction sequence of substrate level phosphorylation
-
-
r
UTP + AMP
UDP + ADP
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + AMP
nucleoside diphosphate + ADP
show the reaction diagram
-
involved in reaction sequence of substrate level phosphorylation
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activation, 50% as effective as Mg2+
Fe
0.3 mol Fe/mol protein
additional information
-
no activation by EDTA, cysteamine, GSH or high phosphate concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Adenylyl)5-adenosine
-
-
ADP
-
reverse reaction, kinetics
AgNO3
-
weak
AMP
-
free form, Mg2+ reverses
ATP
-
-
GDP
-
reverse reaction, kinetics
GTP
-
kinetics
guanosine(5')pentaphospho(5')adenosine
-
-
HgCl2
-
weak
Mg2+
-
weak, above 4 mM, activates below
N-ethylmaleimide
-
weak
p-hydroxymercuribenzoate
-
weak
P1,P5-di(adenosine-5')pentaphosphate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29
ADP
-
pH 8.0, with GDP
0.033 - 0.21
AMP
1
ATP
-
pH 8.0, with of AMP
9.1
CTP
-
pH 8.0, with of AMP
0.0012
GDP
-
pH 8.0, with ADP
0.056 - 0.359
GTP
0.63
ITP
-
pH 8.0, with AMP
7.4
UTP
-
pH 8.0, with of AMP
additional information
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9
ADP
-
pH 8.5
1.6
AMP
-
pH 8.5
0.73 - 0.74
ATP
0.77
GDP
-
pH 8.5
0.8
GTP
-
pH 8.5
0.00014 - 0.00021
guanosine(5')pentaphospho(5')adenosine
-
0.0114
P1,P5-di(adenosine-5')pentaphosphate
25C, pH 6
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
-
native isoenzyme Adk2p (long) 30C
0.28
-
UTP
17.5
-
-
135
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
IDP, ADP
7.5
-
in presence of ITP + AMP
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.7
-
about half-maximal activity at pH 7 and 9.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
30
-
soluble isoenzyme Adk2p (short)
35 - 55
-
soluble isoenzyme Adk2p (long)
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26060
calculated
26700
calculated without His-tag
52000
-
gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 30000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
x-ray diffraction analysis
-
sitting drop vapor diffusion method, using 1.9-2.1 M ammonium sulfate, 0.1 M Tris-HCl pH 8.0
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
5 min, 2 mg protein/ml, stable in 0.1 N HCl
30 - 65
-
soluble isoenzyme Adk2p (long), 66% of the maximum activity at 30C, about 16% activity at 65C
35
-
soluble isoenzyme Adk2p (short) inactivated
40
-
5 min, 2 mg protein/ml, in 0.1 N HCl, 70% loss of activity
95
-
5 min, 95% inactivation at pH 7.4, 0.15 M imidazole buffer
additional information
-
35% ammonium sulfate, AMP or other substrates enhance thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate or substrates enhance stability
-
freeze-thawing, dilutions, or low ionic strength decreases activity rapidly
-
significant portion of soluble isoenzyme Adk2p (long) remains undigested at 0.02 mg/ml trypsin
-
soluble isoenzyme Adk2p (long) is completely inactivated at 5.6 M urea
-
soluble isoenzyme Adk2p (short) is completely degraded at 0.002 mg/ml trypsin
-
soluble isoenzyme Adk2p (short) is completely inactivated at 1.6 M urea
-
stability increases during purification
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, 3 years
-
-20C to 4C, a few weeks
-
0C, partially purified preparation, several weeks
-
room temperature, 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) Rosetta 2 cells
-
expression in Escherichia coli
expression in Escherichia coli strain M15
isozyme 3
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Show AA Sequence (585 entries)
Please use the Sequence Search for a certain query.