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available in iTunes store
Updated BioCyc iOS App now
available in iTunes store

MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:

Moorella thermoacetica: methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferaseInferred from experiment: acsE

In Pathway: reductive acetyl coenzyme A pathway

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase

Enzyme Commission Synonyms: acsE (gene name)

Standard Gibbs Free Energy (ΔrG in kcal/mol): 16.661118Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
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.

Citations: [Roberts94, Doukov00, Doukov07]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R02289

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:

Revised 04-Sep-2012 by Caspi R, SRI International


Doukov00: Doukov T, Seravalli J, Stezowski JJ, Ragsdale SW (2000). "Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase." Structure 8(8);817-30. PMID: 10997901

Doukov07: Doukov TI, Hemmi H, Drennan CL, Ragsdale SW (2007). "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(9);6609-18. PMID: 17172470

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Roberts94: Roberts DL, Zhao S, Doukov T, Ragsdale SW (1994). "The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum." J Bacteriol 176(19);6127-30. PMID: 7928975

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc13.