EC - 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase
Other name:
acsE (gene name)
Systematic name:
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase



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, carbon-monoxide dehydrogenase (ferredoxin) and EC, 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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102036


  1. Roberts, D. L., Zhao, S., Doukov, T., 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 : 6127-6130 (1994). [PMID: 7928975]
  2. Doukov, T., Seravalli, J., Stezowski, J. J., Ragsdale, S. W.
    Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.
    Structure 8 : 817-830 (2000). [PMID: 10997901]
  3. Doukov, T. I., Hemmi, H., Drennan, C. L., 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 : 6609-6618 (2007). [PMID: 17172470]

[EC created 2012]