| EC |
2.1.1.272 |
| Accepted name: |
cobalt-factor III methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + cobalt-factor III + reduced acceptor = S-adenosyl-L-homocysteine + cobalt-precorrin-4 + acceptor |
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For diagram of anaerobic corrin biosynthesis (part 1), click here |
| Other name(s): |
CbiH60 (gene name); S-adenosyl-L-methionine:cobalt-factor III 17-methyltransferase (ring contracting) |
| Systematic name: |
S-adenosyl-L-methionine:cobalt-factor III C17-methyltransferase (ring contracting) |
| Comments: |
Isolated from the bacterium Bacillus megaterium. The enzyme, which participates in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis, catalyses a crucial reaction where the tetrapyrrole ring contracts as a result of methylation of C-17. Contains a [4Fe-4S] cluster. It can also convert cobalt-precorrin-3 to cobalt-precorrin-4. The reductant may be thioredoxin. See EC 2.1.1.131, precorrin-3B C17-methyltransferase, for the corresponding enzyme that participates in the aerobic cobalamin biosynthesis pathway. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Moore, S.J., Biedendieck, R., Lawrence, A.D., Deery, E., Howard, M.J., Rigby, S.E. and Warren, M.J. Characterization of the enzyme CbiH60 involved in anaerobic ring contraction of the cobalamin (vitamin B12) biosynthetic pathway. J. Biol. Chem. 288 (2013) 297–305. [DOI] [PMID: 23155054] |
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| [EC 2.1.1.272 created 2013] |
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