Literature summary for 2.1.1.90 extracted from

Daas, P.J.; Hagen, W.R.; Keltjens, J.T.; van der Drift, C.; Vogels, G.D.
Activation mechanism of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri (1996), J. Biol. Chem., 271, 22346-2251.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cobalt	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	Methanosarcina barkeri
Iron	presence of 1.7 mol of non-heme iron per mol of enzyme	Methanosarcina barkeri
Mg2+	plays a role in binding of the corrinoid prosthetic group and in subunit association	Methanosarcina barkeri

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
121000	-	gradient PAGE, gel filtration	Methanosarcina barkeri
122000	-	gel filtration	Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
methanol + a [Co(I) methanol-specific corrinoid protein]	Methanosarcina barkeri	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	a [methyl-Co(III) methanol-specific corrinoid protein] + H2O	-	?
methanol + a [Co(I) methanol-specific corrinoid protein]	Methanosarcina barkeri DSM 800	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	a [methyl-Co(III) methanol-specific corrinoid protein] + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Methanosarcina barkeri	-	-	-
Methanosarcina barkeri DSM 800	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Methanosarcina barkeri

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
methanol + a [Co(I) methanol-specific corrinoid protein]	-	Methanosarcina barkeri	a [methyl-Co(III) methanol-specific corrinoid protein] + H2O	-	?
methanol + 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	-	?
methanol + a [Co(I) methanol-specific corrinoid protein]	-	Methanosarcina barkeri DSM 800	a [methyl-Co(III) methanol-specific corrinoid protein] + H2O	-	?
methanol + 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 DSM 800	a [methyl-Co(III) methanol-specific corrinoid protein] + H2O	-	?

Synonyms

Synonyms	Comment	Organism
methanol:5-hydroxybenzimidazolylcobamide methyltransferase	-	Methanosarcina barkeri
MT1	-	Methanosarcina barkeri

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Methanosarcina barkeri

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Methanosarcina barkeri

Cofactor

Cofactor	Comment	Organism	Structure
corrinoid	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

pI Value

Organism	Comment	pI Value Maximum	pI Value
Methanosarcina barkeri	isoelectric focusing	-	4.5

General Information

General Information	Comment	Organism
physiological function	first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in Methanosarcina barkeri	Methanosarcina barkeri

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Release 2023.1 (January 2023)