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ENZYME entry: EC 220.127.116.11
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|Hydrogenobyrinic acid a,c-diamide cobaltochelatase.|
|ATP + hydrogenobyrinic acid a,c-diamide + Co(2+) + H(2)O <=> ADP + phosphate + cob(II)yrinic acid a,c-diamide + H(2)|
- This enzyme, which forms part of the aerobic cobalamin biosynthesis
pathway, is a type I chelatase, being heterotrimeric and ATP-
- 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.
- Hydrogenobyrinic acid is a very poor substrate.
- ATP can be replaced by dATP or CTP but the reaction proceeds more
- CobN exhibits a high affinity for hydrogenobyrinic acid a,c-diamide.
- The oligomeric protein CobST possesses at least one sulfhydryl group
that is essential for ATP-binding.
- Once the Co(2+) is inserted, the next step in the pathway ensures
that the cobalt is ligated securely by reducing Co(II) to Co(I); this
step is carried out by EC 18.104.22.168.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
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