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EC 6.6.1.2 Details
EC number
6.6.1.2
Accepted name
cobaltochelatase
Reaction
ATP + hydrogenobyrinate a,c-diamide + Co2+ + H2O = ADP + phosphate + cob(II)yrinate a,c-diamide + H+
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)
CAS registry number
81295-49-0
Comment
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 4.99.1.3, sirohydrochlorin cobaltochelatase, for the cobaltochelatase that participates in the anaerobic cobalamin biosynthesis pathway.
History
created 2004
EC Tree
1.1.3.1 created 1961, deleted 1984
1.1.3.22 created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22, modified 1989, deleted 2004
1.1.3.25 created 1986, deleted 2005
1.1.3.26 created 1989, deleted 2002
1.1.3.31 created 1992, deleted 2003
1.1.3.32 created 1999, deleted 2002
1.1.3.33 created 1999, deleted 2002
1.1.3.34 created 1999, deleted 2002
1.1.3.35 created 1999, deleted 2002
1.1.3.36 created 1999, deleted 2002
1.1.99.15 created 1978, deleted 1980
1.1.99.17 created 1982, deleted 2003