Precorrin-2 dehydrogenase

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precorrin-2 dehydrogenase
Identifiers
EC no. 1.3.1.76
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
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MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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In enzymology, precorrin-2 dehydrogenase (EC 1.3.1.76) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
 
H+
Precorrin-2 dehydrogenase
 
H+
 
+ NADH
 

The two substrates of this enzyme are precorrin-2 and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are sirohydrochlorin, reduced NADH, and a proton. [1] [2] [3]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is precorrin-2:NAD+ oxidoreductase. Other names in common use include Met8p, SirC, and CysG. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria and to Cofactor F430.

See also

References

  1. Enzyme 1.3.1.76 at KEGG Pathway Database.
  2. Warren MJ; Raux, E; Brindley, AA; Leech, HK; Wilson, KS; Hill, CP; Warren, MJ (2002). "The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase". EMBO J. 21 (9): 2068–75. doi:10.1093/emboj/21.9.2068. PMC   125995 . PMID   11980703.
  3. Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. doi:10.1039/b108967f. PMID   12195810.