|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: 220.127.116.11
Enzymes and Genes:
|Methanosarcina barkeri :||methylated [methylamine-specific corrinoid protein]:coenzyme M methyltransferase
In Pathway: methanogenesis from trimethylamine
Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .
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: [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase
Enzyme Commission Synonyms: methyltransferase 2 (ambiguous), MT2 (ambiguous), MT2-A, mtbA (gene name)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 30.793365 [Latendresse13]
Enzyme Commission Summary:
Contains zinc [LeClerc96]. The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyses the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins (cf. EC 18.104.22.168, methylamine—corrinoid protein Co-methyltransferase, EC 22.214.171.124, dimethylamine—corrinoid protein Co-methyltransferase, and EC 126.96.36.199, trimethylamine—corrinoid protein Co-methyltransferase) to coenzyme M, forming the substrate for EC 188.8.131.52, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
Burke95: Burke SA, Krzycki JA (1995). "Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine." J Bacteriol 177(15);4410-6. PMID: 7635826
Ferguson00a: Ferguson DJ, Gorlatova N, Grahame DA, Krzycki JA (2000). "Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri." J Biol Chem 275(37);29053-60. PMID: 10852929
Ferguson97: Ferguson DJ, Krzycki JA (1997). "Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri." J Bacteriol 179(3);846-52. PMID: 9006042
LeClerc96: LeClerc GM, Grahame DA (1996). "Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression." J Biol Chem 1996;271(31);18725-31. PMID: 8702528
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493