Biology:(Methyl-Co(III) methylamine-specific corrinoid protein):coenzyme M methyltransferase

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Short description: Class of enzymes
(Methyl-Co(III) methylamine-specific corrinoid protein):coenzyme M methyltransferase
Identifiers
EC number2.1.1.247
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

(Methyl-Co(III) methylamine-specific corrinoid protein):coenzyme M methyltransferase (EC 2.1.1.247, methyltransferase 2, MT2, MT2-A, mtbA (gene)) is an enzyme with systematic name methylated monomethylamine-specific corrinoid protein:coenzyme M methyltransferase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

[methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M ⇌ methyl-CoM + [Co(I) methylamine-specific corrinoid protein]

This enzyme contains zinc.

References

  1. "Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine". Journal of Bacteriology 177 (15): 4410–6. August 1995. PMID 7635826. 
  2. "Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression". The Journal of Biological Chemistry 271 (31): 18725–31. August 1996. doi:10.1074/jbc.271.31.18725. PMID 8702528. 
  3. "Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri". Journal of Bacteriology 179 (3): 846–52. February 1997. doi:10.1128/jb.179.3.846-852.1997. PMID 9006042. 
  4. "Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine". Journal of Bacteriology 180 (13): 3432–40. July 1998. PMID 9642198. 
  5. "Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri". The Journal of Biological Chemistry 275 (37): 29053–60. September 2000. doi:10.1074/jbc.m910218199. PMID 10852929. 

External links