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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90mercaptopropionate + methylcob(III)alamin - Methanosarcina acetivorans ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90more analysis of mtaCB gene regulation in Methanosarcina acetivorans Methanosarcina acetivorans ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90more coenzyme M does not serve as a methyl acceptor. Methylation of cob(I)alamin with methanol, dimethylsulfide, dimethylamine, and methyl-CoM is not observed, even at high substrate concentrations Methanosarcina acetivorans ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90methanol + a [Co(I) methanol-specific corrinoid protein] - Methanosarcina barkeri a [methyl-Co(III) methanol-specific corrinoid protein] + H2O - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90methanol + a [Co(I) methanol-specific corrinoid protein] - Methanosarcina mazei a [methyl-Co(III) methanol-specific corrinoid protein] + H2O - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90methanol + a [Co(I) methanol-specific corrinoid protein] - Methanosphaera stadtmanae a [methyl-Co(III) methanol-specific corrinoid protein] + H2O - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90methanol + a [Co(I) methanol-specific corrinoid protein] - Methanomethylovorans hollandica a [methyl-Co(III) methanol-specific corrinoid protein] + H2O - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90methanol + a [Co(I) methanol-specific corrinoid protein] first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme Methanosarcina barkeri a [methyl-Co(III) methanol-specific corrinoid protein] + H2O - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90methanol + a [Co(I) methanol-specific corrinoid protein] - Methanosarcina mazei DSM 3647 a [methyl-Co(III) methanol-specific corrinoid protein] + H2O - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.90methanol + a [Co(I) methanol-specific corrinoid protein] - Methanosarcina barkeri DSM 800 a [methyl-Co(III) methanol-specific corrinoid protein] + H2O - ?
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