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
-
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
-
prosthetic
-
methanogenic
- hydrogenase
- archaea
-
cobialamin
- methane
-
methanogenesis
- cobalt
-
methylcobiiialamin
-
2-mercaptoethanesulfonic
-
corrinoid-containing
- acetivorans
- methyltransferases
- methylcobalamin
-
thauer
- hs-com
-
inhabit
- mazei
- trimethylamine
- ferredoxin
-
demethylated
-
cobiamide
-
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
ECTree
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Systematic Name
Systematic Name on EC 2.1.1.90 - methanol-corrinoid protein Co-methyltransferase
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methanol:5-hydroxybenzimidazolylcobamide Co-methyltransferase
The enzyme, which catalyses the transfer of methyl groups from methanol to a methanol-specific corrinoid protein (MtaC), is involved in methanogenesis from methanol. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. Free cob(I)alamin can substitute for the corrinoid protein in vitro [2].
Inactivated by oxygen and other oxidizing agents, and reactivated by catalytic amounts of ATP and hydrogen.