2.1.1.90: methanol-corrinoid protein Co-methyltransferase
This is an abbreviated version!
For detailed information about methanol-corrinoid protein Co-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.90
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2.1.1.90
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methanosarcina
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barkeri
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mtab
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corrinoids
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prosthetic
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methanogenic
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hydrogenase
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archaea
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cobialamin
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methane
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methanogenesis
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cobalt
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methylcobiiialamin
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2-mercaptoethanesulfonic
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corrinoid-containing
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acetivorans
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methyltransferases
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methylcobalamin
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thauer
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hs-com
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inhabit
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mazei
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trimethylamine
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ferredoxin
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demethylated
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cobiamide
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cobalamin-dependent
- 2.1.1.90
- methanosarcina
- barkeri
- mtab
- corrinoids
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prosthetic
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methanogenic
- hydrogenase
- archaea
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cobialamin
- methane
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methanogenesis
- cobalt
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methylcobiiialamin
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2-mercaptoethanesulfonic
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corrinoid-containing
- acetivorans
- methyltransferases
- methylcobalamin
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thauer
- hs-com
-
inhabit
- mazei
- trimethylamine
- ferredoxin
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demethylated
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cobiamide
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cobalamin-dependent
Reaction
Synonyms
Cob(I)alamin methyltransferase, methanol cobalamin methyltransferase, methanol-5-hydroxybenzimidazolylcobamide Co-methyltransferase, methanol-coenzyme M-methyltransferase complex, methanol:5-hydroxy-benzimidazolylcobamide methyltransferase, methanol:5-hydroxybenzimidazolylcobamide methyltransferase, methanol:coenzyme M methyltransferase, methanol:CoM methyltransferase complex, methyltransferase, methanol-cobalamin, MMPA:cob(I)alamin methyltransferase, MT 1, MT1, MtaABC, MtaB, MtpA
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Natural Substrates Products
Natural Substrates Products on EC 2.1.1.90 - methanol-corrinoid protein Co-methyltransferase
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REACTION DIAGRAM
methanol + 5-hydroxybenzimidazolylcobamide
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
methanol + cob(I)alamin
methylcob(III)alamin + H2O
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methylation of free cob(I)alamin by methylmercaptopropionate, which is the physiologically relevant direction, is observed only in the presence of very high levels of methylmercaptopropionate
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additional information
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analysis of mtaCB gene regulation in Methanosarcina acetivorans
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Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O
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methanol catabolism in Methanosarcina species requires the concerted effort of methanol:5-hydroxybenzimidazolylcobamide methyltransferase (MtaB), a corrinoid-containing methyl-accepting protein (MtaC) and Co-methyl-5-hydroxybenzimidazolylcobamide:2-mercapto-ethanesulfonic acid methyltransferase (MtaA). Methanosarcina acetivorans possesses three operons encoding putative methanol-specific MtaB and corrinoid proteins: mtaCB1, mtaCB2 and mtaCB3. Deletion mutants lacking the three operons, in all possible combinations, are constructed and characterized. Strains deleted for any two of the operons grow on methanol, whereas strains lacking all three do not
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methanol + 5-hydroxybenzimidazolylcobamide
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O
one of the enzymes responsible for the transmethylation from methanol to coenzyme M
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a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
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methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
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methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
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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
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methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
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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
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methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
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methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
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?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
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?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
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methyl-cob(III)alamin + H2O
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r
methanol + cob(I)alamin
methyl-cob(III)alamin + H2O
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r