| EC |
2.1.1.289 |
| Accepted name: |
cobalt-precorrin-7 (C5)-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + cobalt-precorrin-7 = S-adenosyl-L-homocysteine + cobalt-precorrin-8 |
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For diagram of anaerobic corrin biosynthesis (part 2), click here |
| Other name(s): |
CbiE |
| Systematic name: |
S-adenosyl-L-methionine:precorrin-7 C5-methyltransferase |
| Comments: |
This enzyme catalyses the methylation at C-5 of cobalt-precorrin-7, a step in the anaerobic (early cobalt insertion) adenosylcobalamin biosynthesis pathway. The equivalent activity in the aerobic adenosylcobalamin biosynthesis pathway is catalysed by the bifunctional enzyme EC 2.1.1.132, precorrin-6B C5,15-methyltransferase (decarboxylating). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Santander, P.J., Kajiwara, Y., Williams, H.J. and Scott, A.I. Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway. Bioorg. Med. Chem. 14 (2006) 724–731. [DOI] [PMID: 16198574] |
| 2. |
Moore, S.J., Lawrence, A.D., Biedendieck, R., Deery, E., Frank, S., Howard, M.J., Rigby, S.E. and Warren, M.J. Elucidation of the anaerobic pathway for the corrin component of cobalamin (vitamin B12). Proc. Natl. Acad. Sci. USA 110 (2013) 14906–14911. [DOI] [PMID: 23922391] |
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| [EC 2.1.1.289 created 2010] |
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