ENZYME entry: EC 6.6.1.2
| Accepted Name |
| Cobaltochelatase.
|
| Alternative Name(s) |
| Hydrogenobyrinic acid a,c-diamide cobaltochelatase. |
| Reaction catalysed |
| ATP + hydrogenobyrinic acid a,c-diamide + Co(2+) + H(2)O <=> ADP + phosphate + cob(II)yrinic acid a,c-diamide + H(2) |
| Comment(s) |
- 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 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 1.16.8.1.
|
| Cross-references |
| BRENDA | 6.6.1.2 |
| EC2PDB | 6.6.1.2 |
| ExplorEnz | 6.6.1.2 |
| PRIAM enzyme-specific profiles | 6.6.1.2 |
| KEGG Ligand Database for Enzyme Nomenclature | 6.6.1.2 |
| IUBMB Enzyme Nomenclature | 6.6.1.2 |
| IntEnz | 6.6.1.2 |
| MEDLINE | Find literature relating to 6.6.1.2 |
| MetaCyc | 6.6.1.2 |
| UniProtKB/Swiss-Prot |
|
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