Information on EC 1.3.1.76 - precorrin-2 dehydrogenase

Word Map on EC 1.3.1.76
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 expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.3.1.76
-
RECOMMENDED NAME
GeneOntology No.
precorrin-2 dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
precorrin-2 + NAD+ = sirohydrochlorin + NADH + H+
show the reaction diagram
first step; This enzyme catalyses the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cob(II)yrinate a,c-diamide biosynthesis I (early cobalt insertion)
-
-
siroheme biosynthesis
-
-
heme metabolism
-
-
vitamin B12 metabolism
-
-
Porphyrin and chlorophyll metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
precorrin-2:NAD+ oxidoreductase
This enzyme catalyses the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction.
CAS REGISTRY NUMBER
COMMENTARY hide
227184-47-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSM509
SwissProt
Manually annotated by BRENDA team
strain CR252
-
-
Manually annotated by BRENDA team
strain CR252
-
-
Manually annotated by BRENDA team
formerly Rhizobium leguminosarum biovar phaseoli, wild-type strain CE3, mutant strain CTNUX8
SwissProt
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
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
show the reaction diagram
additional information
?
-
-
large multifunctional protein that catalyzes four diverse reactions, 2 S-adensyl-L-methionine-dependent methylations, NAD+-dependent tetrapyrrole dehydrogenation and metal chelation
-
?
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
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
enzyme catalyzes cobalt insertion leading to B12 synthesis
Fe2+
-
enzyme catalyzes iron insertion leading to siroheme synthesis
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00088
-
dehydrogenase activity, mutant S128D
0.00993
-
dehydrogenase activity, wild-type
0.0133
mutant H237A
0.0332
-
dehydrogenase activity, mutant S128A
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27990
-
predicted gene derived molecular mass
29000
-
SDS-PAGE
45000
gel filtration
60000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method
space group C2, a : 156.1 A,b : 81.2 A, c : 104.2 A
orthorhombic space group P2(1)2(1)2(1), unit cell dimensions a = 60.73 A, b = 121.49 A, c = 130.79 A
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+ chelating column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as recombinant protein
-
expressed in Escherichia coli BL21(DE3)pLysS(codon+) cells
MET8 mutants complemented by Salmonella typhimurium cysG, cloned and expressed in Escherichia coli
-
recombinantly overproduced in Escherichia coli
-
sequenced and overproduced, sirABC gene cluster complements Escherichia coli cysG mutants
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D141A
site-directed mutagenesis
G22D
site-directed mutagenesis
H237A
site-directed mutagenesis
K270I
-
site-directed mutagenesis
L250A
-
site-directed mutagenesis
N385A
-
site-directed mutagenesis
S128A
-
site-directed mutagenesis
S128D
-
site-directed mutagenesis
Show AA Sequence (805 entries)
Please use the Sequence Search for a certain query.