Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	2 proteins
Enzyme class ^help_outline	EC 2.1.1.246 [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase
GO Molecular Function ^help_outline	GO:1990088 [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase

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Name ^help_outline coenzyme M Identifier CHEBI:58319 Charge -1 Formula C2H5O3S2 InChIKey^help_outline ZNEWHQLOPFWXOF-UHFFFAOYSA-M SMILES^help_outline [O-]S(=O)(=O)CCS 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline methyl-Co(III)-[methanol-specific corrinoid protein] Identifier RHEA-COMP:17571 Reactive part ^help_outline
- Name ^help_outline Co-methyl-Co-5-hydroxybenzimidazolylcob(III)amide Identifier CHEBI:16379 Charge 0 Formula C61H87CoN13O15P InChIKey^help_outline VPKSATWUTVJDMY-CXCINMATSA-L SMILES^help_outline NC(=O)CC[C@@H]1C2=[N+]3[Co-3]456([N+]7=C([C@H](C(C)(C)C7=C2)CCC(N)=O)C(C)=C2N4[C@H]([C@@H]([C@]2(CCC(NC[C@@H](C)OP(=O)(O[C@H]2[C@H]([C@@H](n4c7c(cc(O)cc7)[n+]5c4)O[C@@H]2CO)O)[O-])=O)C)CC(N)=O)[C@]2([C@@](CC(N)=O)([C@@H](C(=[N+]62)C(C)=C3[C@]1(CC(N)=O)C)CCC(N)=O)C)C)C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 2 reaction(s) Find proteins in UniProtKB for this molecule
Name^help_outline Co(I)-[methanol-specific corrinoid protein] Identifier RHEA-COMP:17570 Reactive part ^help_outline
- Name ^help_outline 5-hydroxybenzimidazolylcob(I)amide Identifier CHEBI:60494 Charge -1 Formula C60H84CoN13O15P InChIKey^help_outline CZOAGDFHXVBGHF-NCVPRIERSA-L SMILES^help_outline [H][C@]12[C@H](CC(N)=O)[C@@]3(C)CCC(=O)NC[C@@H](C)OP([O-])(=O)O[C@H]4[C@@H](O)[C@H](O[C@@H]4CO)n4c[n+](c5cc(O)ccc45)[Co-4]456N1C3=C(C)C1=[N+]4C(=CC3=[N+]5C(=C(C)C4=[N+]6[C@]2(C)[C@@](C)(CC(N)=O)[C@@H]4CCC(N)=O)[C@@](C)(CC(N)=O)[C@@H]3CCC(N)=O)C(C)(C)[C@@H]1CCC(N)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 2 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge 1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline methyl-coenzyme M Identifier CHEBI:58286 Charge -1 Formula C3H7O3S2 InChIKey^help_outline FGMRHOCVEPGURB-UHFFFAOYSA-M SMILES^help_outline CSCCS([O-])(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:45208	RHEA:45209	RHEA:45210	RHEA:45211
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	2 proteins
EC numbers ^help_outline	2.1.1.246
Gene Ontology ^help_outline	GO:1990088
KEGG ^help_outline				R10000
MetaCyc ^help_outline				RXN-8096

Publications

Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri: physicochemical characterization, cloning, sequence analysis, and heterologous gene expression.

Leclerc G.M., Grahame D.A.

A comparative study was made on the physicochemical characteristics of two isozymes of methylcobamide:-coenzyme M methyltransferase (MT2). Both isozymes catalyzed S-methylation of 2-thioethanesulfonate (coenzyme M) and exhibited similar apparent Km values for coenzyme M of 35 microM (MT2-A) and 20 ... >> More

A comparative study was made on the physicochemical characteristics of two isozymes of methylcobamide:-coenzyme M methyltransferase (MT2). Both isozymes catalyzed S-methylation of 2-thioethanesulfonate (coenzyme M) and exhibited similar apparent Km values for coenzyme M of 35 microM (MT2-A) and 20 microM (MT2-M). Weak binding to methylcobalamin was indicated by the apparent Km of 14 mM for both isozymes. Cob(I)alamin was established as the major product of the reaction, demonstrating heterolytic cleavage of the methylcobamide carbon-cobalt bond. The isozymes were shown to be zinc-containing metalloproteins. Metal ion chelators strongly inhibited both isozymes. A variety of coenzyme M analogs were tested for activity and/or inhibition. One alternative substrate 3-mercaptopropionate was discovered, with apparent Km 9 mM (MT2-A) and 10 mM (MT2-M). The results suggested an active site geometry in which coenzyme M is bound both by S-coordination to zinc, and electrostatic interaction of the sulfonate with a cationic group on the enzyme. Methanosarcina barkeri genes cmtA and cmtM encoding both isozymes were cloned and sequenced. Both genes encoded proteins with 339 amino acids and predicted molecular masses of 36-37 kDa. Active forms of both isozymes were expressed in Escherichia coli. A conserved segment with the potential for metal binding was found. The possibility of zinc involvement in catalysis of coenzyme M methylation is considered. << Less

J. Biol. Chem. 271:18725-18731(1996) [PubMed] [EuropePMC]

This publication is cited by 1 other entry.
Methylcobalamin: coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli.

Harms U., Thauer R.K.

Methanosarcina barkeri is known to contain two methyltransferase isoenzymes, here designated MtaA and MtbA, which catalyze the formation of methyl-coenzyme M from methylcobalamin and coenzyme M. The genes encoding the two soluble 34-kDa proteins have been cloned and sequenced. mtaA and mtbA wee fo ... >> More

Methanosarcina barkeri is known to contain two methyltransferase isoenzymes, here designated MtaA and MtbA, which catalyze the formation of methyl-coenzyme M from methylcobalamin and coenzyme M. The genes encoding the two soluble 34-kDa proteins have been cloned and sequenced. mtaA and mtbA wee found to be located in different parts of the genome, each forming a monocystronic transcription unit. Northern blot analysis revealed that mtaA is preferentially transcribed when M. barkeri is grown on methanol and the mtbA gene when the organism is grown on H2/CO2 or trimethylamine. Comparison of the deduced amino acid sequences revealed the sequences of the two isoenzymes to be 37% identical. Both isoenzymes showed sequence similarity to uroporphyrinogen III decarboxylase from Escherichia coli. The mtaA gene was tagged with a sequence encoding six His placed bp before the mtaA start codon, and was functionally overexpressed in E. coli. 25% of the E. coli protein was found to be active methyltransferase which could be purified in two steps to apparent homogeneity with a 70% yield. << Less

Eur. J. Biochem. 235:653-659(1996) [PubMed] [EuropePMC]

RHEA:45208 coenzyme M + methyl-Co(III)-[methanol-specific corrinoid protein] = Co(I)-[methanol-specific corrinoid protein] + H(+) + methyl-coenzyme M

Enzymes

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Cross-references

Publications

Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri: physicochemical characterization, cloning, sequence analysis, and heterologous gene expression.

Methylcobalamin: coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli.