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Information on EC 1.3.1.76 - precorrin-2 dehydrogenase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P15807

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EC Tree
IUBMB Comments
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.
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Saccharomyces cerevisiae
UNIPROT: P15807
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
met8p, siroheme synthase, cysg enzyme, precorrin-2 dehydrogenase, cysg gene product, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cobaltochelatase
-
-
CysG
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-
-
-
Met8p
SirC
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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-
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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
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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
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL 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
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
beta-NAD+-dependent dehydrogenation of precorrin-2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0133
mutant H237A
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
space group C2, a : 156.1 A,b : 81.2 A, c : 104.2 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D141A
site-directed mutagenesis
G22D
site-directed mutagenesis
H237A
site-directed mutagenesis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
MET8 mutants complemented by Salmonella typhimurium cysG, cloned and expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raux, E.; McVeigh, T.; Peters, S.E.; Leustek, T.; Warren, M.J.
The role of Saccharomyces cerevisiae MET1p and MET8p in sirohaem and cobalamin biosynthesis
Biochem. J.
338
701-708
1999
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Warren, M.J.; Raux, E.; Schubert, H.L.; Escalante-Semerena, J.C.
The biosynthesis of adenosylcobalamin (vitamin B12)
Nat. Prod. Rep.
19
390-412
2002
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Schubert, H.L.; Raux, E.; Brindley, A.A.; Leech, H.K.; Wilson, K.S.; Hill, C.P.; Warren, M.J.
The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase
EMBO J.
21
2068-2075
2002
Saccharomyces cerevisiae (P15807), Saccharomyces cerevisiae
Manually annotated by BRENDA team