Sirohydrochlorin cobaltochelatase
From Wikipedia, the free encyclopedia
In enzymology, a sirohydrochlorin cobaltochelatase (EC 4.99.1.3) is an enzyme that catalyzes the chemical reaction
- cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+
Thus, the two substrates of this enzyme are cobalt-sirohydrochlorin and H+, whereas its two products are sirohydrochlorin and Co2+.
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 cobalt-sirohydrochlorin cobalt-lyase (sirohydrochlorin-forming). Other names in common use include CbiK, CbiX, CbiXS, anaerobic cobalt chelatase, cobaltochelatase [ambiguous], and sirohydrochlorin cobalt-lyase (incorrect). This enzyme participates in porphyrin and chlorophyll metabolism.
Contents |
[edit] Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1TJN and 2DJ5.
[edit] References
- IUBMB entry for 4.99.1.3
- BRENDA references for 4.99.1.3 (Recommended.)
- PubMed references for 4.99.1.3
- PubMed Central references for 4.99.1.3
- Google Scholar references for 4.99.1.3
- Schubert HL, Raux E, Wilson KS, Warren MJ (1999). "Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis". Biochemistry. 38: 10660–9. doi:. PMID 10451360.
- Brindley AA, Raux E, Leech HK, Schubert HL, Warren MJ (2003). "A story of chelatase evolution: identification and characterization of a small 13-15-kDa "ancestral" cobaltochelatase (CbiXS) in the archaea". J. Biol. Chem. 278: 22388–95. doi:. PMID 12686546.
- 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.

