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IUBMB 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]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.
Reaction Schemes
2
+
a [methyl coenzyme-M reductase]-L-arginine
+
=
+
+
+
a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine
+
Synonyms
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methanogenesis marker protein 10
MA4551
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methanogenesis marker 10
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methanogenesis marker 10
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methanogenesis marker protein 10
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methanogenesis marker protein 10
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methanogenesis marker protein 10
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MMP10
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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
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S-adenosyl-L-methionine:[methyl coenzyme M reductase]-L-arginine C-5-(S)-methyltransferase
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 Coalpha-[alpha-(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.
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2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine285 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine285 + acceptor
2 S-adenosyl-L-methionine + [methyl coenzyme-M reductase subunit McrA]-L-arginine275 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + [methyl coenzyme-M reductase subunit McrA]-(5S)-C-methyl-L-arginine275 + acceptor
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Substrates: -
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2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine285 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine285 + acceptor
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Substrates: -
?
2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine285 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine285 + acceptor
Substrates: -
?
2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine285 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine285 + acceptor
Substrates: -
?
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2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine285 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine285 + acceptor
2 S-adenosyl-L-methionine + [methyl coenzyme-M reductase subunit McrA]-L-arginine275 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + [methyl coenzyme-M reductase subunit McrA]-(5S)-C-methyl-L-arginine275 + acceptor
-
Substrates: -
?
2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine285 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine285 + acceptor
-
Substrates: -
?
2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine285 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine285 + acceptor
Substrates: -
?
2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine285 + reduced acceptor
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine285 + acceptor
Substrates: -
?
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Cobalamin
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required for activity
methylcobalamin
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required
S-adenosyl-L-methionine
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dependent on
S-adenosyl-L-methionine
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required
S-adenosyl-L-methionine
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Fe2+
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the enzyme contain 5.09 iron ions per polypeptide
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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metabolism
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the enzyme plays an important role in methanogenesis
malfunction
enzyme knockout strains show impaired growth under stress conditions such as the presence of 0.2 mM hydrogen peroxide or elevated temperature (42°C)
malfunction
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enzyme knockout strains show impaired growth under stress conditions such as the presence of 0.2 mM hydrogen peroxide or elevated temperature (42°C)
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MCRAM_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
415
0
46721
Swiss-Prot
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MCRAM_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
411
0
45222
Swiss-Prot
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?
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x * 46300, calculated from amino acid sequence
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G140A/G144A/G146A
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the mutant sustains a 15.8% loss in Arg275 methylation as compared to the wild type enzyme
H375F
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the mutant sustains a 0.5% loss in Arg275 methylation as compared to the wild type enzyme
H375F/DELTAN371
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the mutant sustains a 42.5% loss in Arg275 methylation as compared to the wild type enzyme
H375G
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the mutant sustains a 0.8% loss in Arg275 methylation as compared to the wild type enzyme
N212A/D213A
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the mutant sustains a 35% loss in Arg275 methylation as compared to the wild type enzyme
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cobalt-Talon resin column chromatography
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expressed in Escherichia coli BL21(DE3) cells
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Lyu, Z.; Shao, N.; Chou, C.W.; Shi, H.; Patel, R.; Duin, E.C.; 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
e00654-19
2020
Methanococcus maripaludis
brenda
Radle, M.I.; Miller, D.V.; Laremore, T.N.; 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
11712-11725
2019
Methanosarcina acetivorans
brenda
Jarrett, J.T.
Surprise! A hidden B12 cofactor catalyzes a radical methylation
J. Biol. Chem.
294
11726-11727
2019
Methanosarcina acetivorans
brenda
Deobald, D.; Adrian, L.; Schne, C.; Rother, M.; 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
Methanosarcina acetivorans (Q8THG6), Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834 (Q8THG6)
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