Precorrin-2 dehydrogenase explained

precorrin-2 dehydrogenase
Ec Number:	1.3.1.76
Go Code:	0043115

In enzymology, a precorrin-2 dehydrogenase is an enzyme that catalyzes the chemical reaction

precorrin-2 + NAD⁺

\rightleftharpoons sirohydrochlorin + NADH + H⁺The two substrates of this enzyme are precorrin-2 and NAD⁺; its three products are sirohydrochlorin, NADH, and H⁺.

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

• Cobalamin biosynthesis

References

• Warren MJ . 2002 . The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase . EMBO J. . 21 . 2068 - 75 . 11980703 . 10.1093/emboj/21.9.2068 . Raux . E . Brindley . AA . Leech . HK . Wilson . KS . Hill . CP . Warren . MJ . 9 . 125995 .
• Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC . 2002 . The biosynthesis of adenosylcobalamin (vitamin B12) . Nat. Prod. Rep. . 19 . 390 - 412 . 12195810 . 10.1039/b108967f . 4 .