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Information on EC - cobaltochelatase

for references in articles please use BRENDA:EC6.6.1.2
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EC Tree
     6 Ligases
         6.6 Forming nitrogen—metal bonds
             6.6.1 Forming coordination complexes
IUBMB Comments
This enzyme, which forms part of the aerobic 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 . Hydrogenobyrinic acid 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 hydrogenobyrinic acid a,c-diamide. The oligomeric protein CobST possesses at least one sulfhydryl group that is essential for ATP-binding. Once the Co2+ 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, cob(II)yrinic acid a,c-diamide reductase.
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The enzyme appears in viruses and cellular organisms
CbiK, CbiXL, cobalt chelatase, cobaltochelatase, CobN-CobST, CobNST, CobN–CobST, gene cobN/gene cobS cobaltochelatase, holocobalamin synthase, hydrogenobyrinic acid a,c-diamide cobaltochelatase, more
ATP + hydrogenobyrinic acid a,c-diamide + Co2+ + H2O = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
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