Sirohydrochlorin ferrochelatase
From Wikipedia, the free encyclopedia
In enzymology, a sirohydrochlorin ferrochelatase (EC 4.99.1.4) is an enzyme that catalyzes the chemical reaction
- siroheme + 2 H+
sirohydrochlorin + Fe2+
Thus, the two substrates of this enzyme are siroheme and H+, whereas its two products are sirohydrochlorin and Fe2+.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is siroheme ferro-lyase (sirohydrochlorin-forming). Other names in common use include CysG, Met8P, SirB, and sirohydrochlorin ferro-lyase (incorrect). This enzyme participates in porphyrin and chlorophyll metabolism.
[edit] References
- IUBMB entry for 4.99.1.4
- BRENDA references for 4.99.1.4 (Recommended.)
- PubMed references for 4.99.1.4
- PubMed Central references for 4.99.1.4
- Google Scholar references for 4.99.1.4
- 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.

