2.1.1.90: methanol-corrinoid protein Co-methyltransferase

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For detailed information about methanol-corrinoid protein Co-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.90

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

a [Co(I) methanol-specific corrinoid protein]

a [methyl-Co(III) methanol-specific corrinoid protein]

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

2 Transferases

2.1 Transferring one-carbon groups

2.1.1 Methyltransferases

2.1.1.90 methanol-corrinoid protein Co-methyltransferase

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Results	in table
4	Activating Compound
21	AA Sequence
1	CAS Registry Number
3	Cloned(Commentary)
4	Cofactor
1	Crystallization (Commentary)
1	Expression
2	General Information
1	General Stability
6	Inhibitors
1	kcat/KM [mM/s]
2	KM Value [mM]
13	Metals/Ions
7	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
26	Organism
2	Oxidation Stability
3	Pathway
16	PDB ID
2	pH Optimum
1	pI Value
6	Purification (Commentary)
1	Reaction
1	Reaction Type
22	Reference
1	Specific Activity [micromol/min/mg]
22	Substrates and Products (Substrate)
4	Subunits
32	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Turnover Number [1/s]

Cofactor

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Cofactor on EC 2.1.1.90 - methanol-corrinoid protein Co-methyltransferase

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5-hydroxybenzimidazolylcobamide

3 entries

corrinoid

Methanosarcina barkeri

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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