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

MetaCyc Reaction: 2.1.1.258

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

EC Number: 2.1.1.258

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 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) 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.

Citations: [Roberts94, Doukov00, Doukov07]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R02289

Relationship Links: BRENDA:EC:2.1.1.258, ENZYME:EC:2.1.1.258, IUBMB-ExplorEnz:EC:2.1.1.258

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


References

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 Fri Feb 12, 2016, biocyc13.