Sirohydrochlorin cobaltochelatase
The enzyme sirohydrochlorin cobaltochelatase (EC 4.99.1.3) catalyzes the reaction
- cobalt-sirohydrochlorin + 2 H+ = sirohydrochlorin + Co2+
| sirohydrochlorin cobaltochelatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.99.1.3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In the forward direction of reactions towards cobalamin in anaerobic bacteria, the two substrates of this enzyme are sirohydrochlorin and Co2+; its two products are cobalt-sirohydrochlorin and H+.
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 is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria such as Salmonella typhimurium and Bacillus megaterium. It has also been identified as the enzyme which inserts nickel into sirohydrochlorin in the biosynthesis of cofactor F430, reaction EC 4.99.1.11.[1]
See also
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1TJN and 2DJ5.
References
- Moore SJ, Sowa ST, Schuchardt C, Deery E, Lawrence AD, Ramos JV, et al. (March 2017). "Elucidation of the biosynthesis of the methane catalyst coenzyme F430". Nature. 543 (7643): 78–82. Bibcode:2017Natur.543...78M. doi:10.1038/nature21427. PMC 5337119. PMID 28225763.
Further reading
- Schubert HL, Raux E, Wilson KS, Warren MJ (August 1999). "Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis". Biochemistry. 38 (33): 10660–9. doi:10.1021/bi9906773. PMID 10451360.
- Brindley AA, Raux E, Leech HK, Schubert HL, Warren MJ (June 2003). "A story of chelatase evolution: identification and characterization of a small 13-15-kDa "ancestral" cobaltochelatase (CbiXS) in the archaea". The Journal of Biological Chemistry. 278 (25): 22388–95. doi:10.1074/jbc.M302468200. PMID 12686546.
- Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (August 2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Natural Product Reports. 19 (4): 390–412. doi:10.1039/b108967f. PMID 12195810.