| EC |
2.1.1.258 |
| Accepted name: |
5-methyltetrahydrofolate—corrinoid/iron-sulfur protein Co-methyltransferase |
| Reaction: |
a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate |
| Other name(s): |
acsE (gene name) |
| Systematic name: |
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase |
| Comments: |
Catalyses the transfer of a methyl group from the N5 group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. Involved, together with EC 1.2.7.4, anaerobic carbon-monoxide dehydrogenase and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Roberts, D.L., Zhao, S., Doukov, T. and Ragsdale, S.W. The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum. J. Bacteriol. 176 (1994) 6127–6130. [DOI] [PMID: 7928975] |
| 2. |
Doukov, T., Seravalli, J., Stezowski, J.J. and Ragsdale, S.W. Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase. Structure 8 (2000) 817–830. [DOI] [PMID: 10997901] |
| 3. |
Doukov, T.I., Hemmi, H., Drennan, C.L. and Ragsdale, S.W. Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases. J. Biol. Chem. 282 (2007) 6609–6618. [DOI] [PMID: 17172470] |
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| [EC 2.1.1.258 created 2012] |
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