The Enzyme Database

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Accepted name: cobaltochelatase
Reaction: ATP + hydrogenobyrinate a,c-diamide + Co2+ + H2O = ADP + phosphate + cob(II)yrinate a,c-diamide + H+
For diagram of the enzyme's role in corrin biosynthesis, click here
Other name(s): hydrogenobyrinic acid a,c-diamide cobaltochelatase; CobNST; CobNCobST; hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming)
Systematic name: hydrogenobyrinate-a,c-diamide:cobalt cobalt-ligase (ADP-forming)
Comments: This enzyme, which forms part of the aerobic (late cobalt insertion) cobalamin biosynthesis pathway, is a type I chelatase, being heterotrimeric and ATP-dependent. It comprises two components, one of which corresponds to CobN and the other is composed of two polypeptides, specified by cobS and cobT in Pseudomonas denitrificans, and named CobST [1]. Hydrogenobyrinate is a very poor substrate. ATP can be replaced by dATP or CTP but the reaction proceeds more slowly. CobN exhibits a high affinity for hydrogenobyrinate a,c-diamide. The oligomeric protein CobST possesses at least one sulfhydryl group that is essential for ATP-binding. See EC, sirohydrochlorin cobaltochelatase, for the cobaltochelatase that participates in the anaerobic cobalamin biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81295-49-0
1.  Debussche, L., Couder, M., Thibaut, D., Cameron, B., Crouzet, J. and Blanche, F. Assay, purification, and characterization of cobaltochelatase, a unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans. J. Bacteriol. 174 (1992) 7445–7451. [DOI] [PMID: 1429466]
2.  Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390–412. [PMID: 12195810]
[EC created 2004]

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