The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

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, 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: BRENDA, EXPASY, KEGG, MetaCyc
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. [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. [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. [PMID: 17172470]
[EC created 2012]

Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald