Precorrin-2 dehydrogenase
From Wikipedia, the free encyclopedia
In enzymology, a precorrin-2 dehydrogenase (EC 1.3.1.76) is an enzyme that catalyzes the chemical reaction
- precorrin-2 + NAD+ sirohydrochlorin + NADH + H+
Thus, the two substrates of this enzyme are precorrin 2 and NAD+, whereas its 3 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 participates in porphyrin and chlorophyll metabolism.
[edit] References
- IUBMB entry for 1.3.1.76
- BRENDA references for 1.3.1.76 (Recommended.)
- PubMed references for 1.3.1.76
- PubMed Central references for 1.3.1.76
- Google Scholar references for 1.3.1.76
- Warren MJ (2002). "The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase". EMBO. J. 21: 2068–75. doi: . PMID 11980703.
- Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19: 390–412. doi: . PMID 12195810.