| EC |
2.1.1.271 |
| Accepted name: |
cobalt-precorrin-4 methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + cobalt-precorrin-4 = S-adenosyl-L-homocysteine + cobalt-precorrin-5A |
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For diagram of anaerobic corrin biosynthesis (part 1), click here |
| Other name(s): |
CbiF; S-adenosyl-L-methionine:cobalt-precorrin-4 11-methyltransferase |
| Systematic name: |
S-adenosyl-L-methionine:cobalt-precorrin-4 C11-methyltransferase |
| Comments: |
This enzyme, which participates in the anaerobic (early cobalt insertion) cobalamin biosynthesis pathway, catalyses the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A. See EC 2.1.1.133, precorrin-4 C11-methyltransferase, for the equivalent enzyme that participates in the aerobic cobalamin biosynthesis pathway. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Raux, E., Schubert, H.L., Woodcock, S.C., Wilson, K.S. and Warren, M.J. Cobalamin (vitamin B12) biosynthesis--cloning, expression and crystallisation of the Bacillus megaterium S-adenosyl-L-methionine-dependent cobalt-precorrin-4 transmethylase CbiF. Eur. J. Biochem. 254 (1998) 341–346. [DOI] [PMID: 9660189] |
| 2. |
Schubert, H.L., Wilson, K.S., Raux, E., Woodcock, S.C. and Warren, M.J. The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase. Nat. Struct. Biol. 5 (1998) 585–592. [DOI] [PMID: 9665173] |
| 3. |
Kajiwara, Y., Santander, P.J., Roessner, C.A., Perez, L.M. and Scott, A.I. Genetically engineered synthesis and structural characterization of cobalt-precorrin 5A and -5B, two new intermediates on the anaerobic pathway to vitamin B12: definition of the roles of the CbiF and CbiG enzymes. J. Am. Chem. Soc. 128 (2006) 9971–9978. [DOI] [PMID: 16866557] |
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| [EC 2.1.1.271 created 2013] |
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