| EC |
2.1.1.379 |
| Accepted name: |
[methyl coenzyme M reductase]-L-arginine C-5-methyltransferase |
| Reaction: |
2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine + reduced acceptor = S-adenosyl-L-homocysteine + L-methionine + 5′-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine + acceptor |
| Other name(s): |
methanogenesis marker protein 10; Mmp10 |
| Systematic name: |
S-adenosyl-L-methionine:[methyl coenzyme M reductase]-L-arginine C-5-(S)-methyltransferase |
| Comments: |
The enzyme, present in methanogenic archaea, catalyses a modification of an L-arginine residue at the active site of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase (better known as methyl-coenzyme M reductase), which catalyses the last and methane-releasing step of methanogenesis. The enzyme is a radical AdoMet (radical SAM) enzyme and contains a [4Fe-4S] cluster and a Coα-[α-(5-hydroxybenzimidazolyl)]-cobamide cofactor. The methyl group, which is derived from S-adenosyl-L-methionine, is transferred to the cob(I)amide cofactor, forming methylcob(III)amide as an intermediate carrier, before being transferred to the arginine residue. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Deobald, D., Adrian, L., Schone, C., Rother, M. and Layer, G. Identification of a unique radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase. Sci. Rep. 8:7404 (2018). [DOI] [PMID: 29743535] |
| 2. |
Radle, M.I., Miller, D.V., Laremore, T.N. and Booker, S.J. Methanogenesis marker protein 10 (Mmp10) from Methanosarcina acetivorans is a radical S-adenosylmethionine methylase that unexpectedly requires cobalamin. J. Biol. Chem. 294 (2019) 11712–11725. [DOI] [PMID: 31113866] |
| 3. |
Lyu, Z., Shao, N., Chou, C.W., Shi, H., Patel, R., Duin, E.C. and Whitman, W.B. Posttranslational methylation of arginine in methyl coenzyme M reductase has a profound impact on both methanogenesis and growth of Methanococcus maripaludis. J. Bacteriol. 202 (2020) . [DOI] [PMID: 31740491] |
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| [EC 2.1.1.379 created 2021] |
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