The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydrofolate methyltransferase
Reaction: a [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + tetrahydrofolate = N5-methyltetrahydrofolate + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein]
Other name(s): mtvA (gene name)
Systematic name: [methylated methoxylated-aromatic-compound-specific corrinoid protein]:tetrahydrofolaten methyltransferase
Comments: The enzyme, found in acetogenic bacteria, participates in a pathway for the degradation of methoxylated aromatic compounds (methoxydotrophic growth). The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (MtvC) to tetrahydrofolate. cf. EC, [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydromethanopterin methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Kaufmann, F., Wohlfarth, G. and Diekert, G. O-demethylase from Acetobacterium dehalogenans—substrate specificity and function of the participating proteins. Eur. J. Biochem. 253 (1998) 706–711. [DOI] [PMID: 9654069]
2.  Naidu, D. and Ragsdale, S.W. Characterization of a three-component vanillate O-demethylase from Moorella thermoacetica. J. Bacteriol. 183 (2001) 3276–3281. [DOI] [PMID: 11344134]
3.  Pierce, E., Xie, G., Barabote, R.D., Saunders, E., Han, C.S., Detter, J.C., Richardson, P., Brettin, T.S., Das, A., Ljungdahl, L.G. and Ragsdale, S.W. The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum). Environ. Microbiol. 10 (2008) 2550–2573. [DOI] [PMID: 18631365]
[EC created 2022]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald