|Gene:||mtmC||Accession Number: G-9439 (MetaCyc)|
Species: Methanosarcina barkeri
In vitro reconstitution of CoM methylation with methylamine was achieved with three purified proteins: a monomethylamine corrinoid protein (MMCP), the "A" isozyme of methylated [methylamine-specific corrinoid protein]:coenzyme M methyltransferase (MT2-A), and methylamine--corrinoid protein Co-methyltransferase (MMAMT). MMAMT is a 170-kDa protein with 52-kDa subunits, which is rate-limiting for methyl transfer until at a 2-fold molar excess over MMCP.
MMCP and MMAMT formed a complex detectable by size exclusion high pressure liquid chromatography [Burke97].
Molecular Weight of Polypeptide: 23.067 kD (from nucleotide sequence), 29 kD (experimental) [Burke95 ]
Relationship Links: Entrez-Nucleotide:RELATED-TO:AF013713 , InterPro:IN-FAMILY:IPR003759 , InterPro:IN-FAMILY:IPR006158 , InterPro:IN-FAMILY:IPR012741 , PDB:Structure:3EZX , Pfam:IN-FAMILY:PF02310 , Pfam:IN-FAMILY:PF02607 , Prosite:IN-FAMILY:PS51332 , Prosite:IN-FAMILY:PS51337 , Smart:IN-FAMILY:SM01018
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
Burke97: Burke SA, Krzycki JA (1997). "Reconstitution of Monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri." J Biol Chem 272(26);16570-7. PMID: 9195968
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