The Enzyme Database

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Accepted name: [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydromethanopterin methyltransferase
Reaction: a [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + tetrahydromethanopterin = N5-methyltetrahydromethanopterin + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein]
Other name(s): mtoA (gene name)
Systematic name: [methylated methoxylated-aromatic-compound-specific corrinoid protein]:tetrahydromethanopterin methyltransferase
Comments: The enzyme has been characterized from several archaeal species. In the methanogenic archaeon Methermicoccus shengliensis the enzyme participates in methanogenesis from methoxylated aromatic compounds, while in the non-methanogenic Archaeoglobus fulgidus it participates in methoxydotrophic growth. The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (MtoC) to tetrahydromethanopterin or tetrahydrosarcinapterin. cf. EC, [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydrofolate methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Kurth, J.M., Nobu, M.K., Tamaki, H., de Jonge, N., Berger, S., Jetten, M.SM., Yamamoto, K., Mayumi, D., Sakata, S., Bai, L., Cheng, L., Nielsen, J.L., Kamagata, Y., Wagner, T. and Welte, C.U. Methanogenic archaea use a bacteria-like methyltransferase system to demethoxylate aromatic compounds. ISME J. 15 (2021) 3549–3565. [DOI] [PMID: 34145392]
2.  Welte, C.U., de Graaf, R., Dalcin Martins, P., Jansen, R.S., Jetten, M.SM. and Kurth, J.M. A novel methoxydotrophic metabolism discovered in the hyperthermophilic archaeon Archaeoglobus fulgidus. Environ. Microbiol. 23 (2021) 4017–4033. [DOI] [PMID: 33913565]
[EC created 2022]

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