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MetaCyc Reaction: 2.1.1.258

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 2.1.1.258

Enzymes and Genes:

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

In Pathway: reductive acetyl coenzyme A pathway

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. 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): 16.661118 Inferred 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: [Roberts94a, Doukov00, Doukov07]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

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."

Roberts94a: 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 SRI International Pathway Tools version 19.0 on Tue Jun 30, 2015, BIOCYC13A.