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mercaptopropionate + methylcob(III)alamin
?
-
-
-
-
?
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
methyl-cob(III)alamin + H2O
methanol + cob(I)alamin
methylcob(III)alamin + H2O
-
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
-
-
?
additional information
?
-
methanol + 5-hydroxybenzimidazolylcobamide
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O
-
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
-
-
?
methanol + 5-hydroxybenzimidazolylcobamide
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O
-
-
?
methanol + 5-hydroxybenzimidazolylcobamide
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O
-
-
?
methanol + 5-hydroxybenzimidazolylcobamide
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O
one of the enzymes responsible for the transmethylation from methanol to coenzyme M
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
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
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
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
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + cob(I)alamin
methyl-cob(III)alamin + H2O
-
-
?
methanol + cob(I)alamin
methyl-cob(III)alamin + H2O
-
-
-
r
methanol + cob(I)alamin
methyl-cob(III)alamin + H2O
catalyzed by beta subunit MtaB alone
-
r
methanol + cob(I)alamin
methyl-cob(III)alamin + H2O
-
-
-
r
additional information
?
-
-
analysis of mtaCB gene regulation in Methanosarcina acetivorans
-
-
?
additional information
?
-
-
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
-
-
-
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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
methyl-cob(III)alamin + H2O
methanol + cob(I)alamin
methylcob(III)alamin + H2O
-
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
-
-
?
additional information
?
-
-
analysis of mtaCB gene regulation in Methanosarcina acetivorans
-
-
?
methanol + 5-hydroxybenzimidazolylcobamide
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O
-
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
-
-
?
methanol + 5-hydroxybenzimidazolylcobamide
Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O
one of the enzymes responsible for the transmethylation from methanol to coenzyme M
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
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
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
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
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
-
?
methanol + cob(I)alamin
methyl-cob(III)alamin + H2O
-
-
-
r
methanol + cob(I)alamin
methyl-cob(III)alamin + H2O
-
-
-
r
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Ba2+
metal-free enzyme preparation has no activity, addition of Ba2+ restores 27% of the original activity
Ca2+
metal-free enzyme preparation has no activity, addition of Ca2+ restores 35% of the original activity
Co2+
metal-free enzyme preparation has no activity, addition of Co+ restores 46% of the original activity
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
Iron
-
presence of 1.7 mol of non-heme iron per mol of enzyme
Mn2+
metal-free enzyme preparation has no activity, addition of Mn2+ restores 27% of the original activity
Ni2+
metal-free enzyme preparation has no activity, addition of Ni2+ restores 21% of the original activity
Sr2+
metal-free enzyme preparation has no activity, addition of Sr2+ restores 20% of the original activity
Mg2+
metal-free enzyme preparation has no activity, addition of Mg2+ restores 66% of the original activity
Mg2+
-
plays a role in binding of the corrinoid prosthetic group and in subunit association
Zn2+
-
0.1 mM used in assay conditions
Zn2+
beta subunit MtaB contains 1 mol Zn2+/mol subunit, Zn2+ can be substituted by Co2+
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Van der Meijden, P.; te Brmmelstroet, B.W.; Poirot, C.M.; van der Drift, C.; Vogels, G.D.
Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri
J. Bacteriol.
160
629-635
1984
Methanosarcina barkeri (Q46EH3), Methanosarcina barkeri
brenda
Van der Meijden, P.; van der Lest, C.; van der Drift, C.; Vogels, G.D.
Reductive activation of methanol: 5-hydroxybenzimidazolylcobamide methyltransferase of Methanosarcina barkeri
Biochem. Biophys. Res. Commun.
118
760-766
1984
Methanosarcina barkeri
brenda
Van der Meijden, P.; Heythuysen, H.J.; Pouwels, A.; Houwen, F.; van der Drift, C.; Vogels, G.D.
Methyltransferases involved in methanol conversion by Methanosarcina barkeri
Arch. Microbiol.
134
238-242
1983
Methanosarcina barkeri
brenda
Van der Meijden, P.; van der Drift, C.; Vogels, G.D.
Methanol conversion in Eubacterium limosum
Arch. Microbiol.
138
360-364
1984
Eubacterium limosum, Methanothermobacter thermautotrophicus
-
brenda
Taylor, C.D.; Wolfe, R.S.
A simplified assay for coenzyme M (HSCH2CH2SO3). Resolution of methylcobalamin-coenzyme M methyltransferase and use of sodium borohydride
J. Biol. Chem.
249
4886-4890
1974
Methanobacterium bryantii
brenda
Sauer, K.; Thauer, R.K.
Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Zinc dependence and thermodynamics of the methanol:cob(I)alamin methyltransferase reaction
Eur. J. Biochem.
249
280-285
1997
Methanosarcina barkeri (Q46EH3), Methanosarcina barkeri
brenda
Sauer, K.; Harms, U.; Thauer, R.K.
Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties, and encoding genes of the corrinoid protein MT1
Eur. J. Biochem.
243
670-677
1997
Methanosarcina barkeri (Q46EH3), Methanosarcina barkeri
brenda
Bose, A.; Pritchett, M.A.; Rother, M.; Metcalf, W.W.
Differential regulation of the three methanol methyltransferase isozymes in Methanosarcina acetivorans C2A
J. Bacteriol.
188
7274-7283
2006
Methanosarcina acetivorans
brenda
Pritchett, M.A.; Metcalf, W.W.
Genetic, physiological and biochemical characterization of multiple methanol methyltransferase isozymes in Methanosarcina acetivorans C2A
Mol. Microbiol.
56
1183-1194
2005
Methanosarcina acetivorans
brenda
Hagemeier, C.H.; Krer, M.; Thauer, R.K.; Warkentin, E.; Ermler, U.
Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex
Proc. Natl. Acad. Sci. USA
103
18917-18922
2006
Methanosarcina barkeri (Q46EH3)
brenda
Opulencia, R.B.; Bose, A.; Metcalf, W.W.
Physiology and posttranscriptional regulation of methanol:coenzyme M methyltransferase isozymes in Methanosarcina acetivorans C2A
J. Bacteriol.
191
6928-6935
2009
Methanosarcina acetivorans
brenda
Hoeppner, A.; Thomas F, Rueppel, A.; Hensel, R.; Blankenfeldt W, Bayer P, Faust A.
Structure of the corrinoid:coenzyme M methyltransferase MtaA from Methanosarcina mazei
Acta Crystallogr. Sect. D
68
1549-1557
2012
Methanosarcina mazei (Q8PXZ6), Methanosarcina mazei
brenda
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
J. Biol. Chem.
271
22346-2251
1996
Methanosarcina barkeri, Methanosarcina barkeri DSM 800
brenda
Dong, M.; Gonzalez, T.; Klems, M.; Steinberg, L.; Chen, W.; Papoutsakis, E.; Bahnson, B.
In vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex
Biotechnol. Prog.
33
1243-1249
2017
Methanosarcina barkeri (Q48949 and Q46EH3 and Q46EH4), Methanosarcina barkeri, Methanosarcina barkeri DSM 804 (Q48949 and Q46EH3 and Q46EH4)
brenda
Dziewit, L.; Pyzik, A.; Romaniuk, K.; Sobczak, A.; Szczesny, P.; Lipinski, L.; Bartosik, D.; Drewniak, L.
Novel molecular markers for the detection of methanogens and phylogenetic analyses of methanogenic communities
Front. Microbiol.
6
694
2015
Methanosarcina barkeri, Methanosarcina mazei, Methanosphaera stadtmanae, Methanomethylovorans hollandica
brenda
Fu, H.; Goettge, M.; Metcalf, W.
Biochemical characterization of the methylmercaptopropionate Cob(I)alamin methyltransferase from Methanosarcina acetivorans
J. Bacteriol.
201
e00130-19
2019
Methanosarcina acetivorans
brenda