Involvement of an activation protein in the methanol:2-mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri

@article{Daas1993InvolvementOA,
  title={Involvement of an activation protein in the methanol:2-mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri},
  author={Piet J. H. Daas and Kasper A.A. Gerrits and Jan T. Keltjens and Chris van der Drift and Godfried D. Vogels},
  journal={Journal of Bacteriology},
  year={1993},
  volume={175},
  pages={1278 - 1283}
}
Methanol:5-hydroxybenzimidazolylcobamide methyltransferase (MT1) is the first of two enzymes required for transfer of the methyl group of methanol to 2-mercaptoethanesulfonic acid in Methanosarcina barkeri. MT1 binds the methyl group of methanol to its corrinoid prosthetic group only when the central cobalt atom of the corrinoid is present in the highly reduced Co(I) state. However, upon manipulation of MT1 and even during catalysis, the enzyme becomes inactivated as the result of Co(I… Expand
Activation Mechanism of Methanol:5-Hydroxybenzimidazolylcobamide Methyltransferase from Methanosarcina barkeri*
TLDR
The activation mechanism is discussed within the context of a proposed model and compared to those described for other corrinoid-containing methyl group transferring proteins. Expand
Purification and Properties of an Enzyme Involved in the ATP-dependent Activation of the Methanol:2-Mercaptoethanesulfonic Acid Methyltransferase Reaction in Methanosarcina barkeri*
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The first to report on the presence, isolation, and function of a phosphorylated protein in a methanogenic archaeon is reported, indicating that MAP acts as a catalyst. Expand
Involvement of methyltransferase-activating protein and methyltransferase 2 isoenzyme II in methylamine:coenzyme M methyltransferase reactions in Methanosarcina barkeri Fusaro
TLDR
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The enzyme system catalyzing the formation of methyl-coenzyme M from methanol and coenzyme M in Methanosarcina barkeri is composed of the three different polypeptides MtaA, MtaB and MtaC of whichExpand
Involvement of methyltransferases enzymes during the energy metabolism of the anaerobic archaeon methanosarcina semesiae sp. Nov.
The methyl group transfer from dimethylsulfide (DMS), trimethylamine and methanol to 2-mercaptoethanesulfonic acid (coenzyme M) were investigated from cell extracts of Methanosarcina semesiae sp.Expand
Veratrol-O-demethylase of Acetobacterium dehalogenans: ATP-dependent reduction of the corrinoid protein
TLDR
The ATP-dependent reduction of the corrinoid protein of the veratrol O-demethylase was shown to be dependent on titanium(III) citrate as electron donor and on an activating enzyme, and ADP, AMP, or GTP could not replace ATP in the activation reaction. Expand
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TLDR
The results suggested an active site geometry in which coenzyme M is bound both by S-coordination to zinc, and electrostatic interaction of the sulfonate with a cationic group on the enzyme. Expand
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TLDR
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TLDR
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TLDR
The reducing system of hydrogenase and ferredoxin was able to reduce dithiols, like dithiodiethanesulfonate and cystine to their monomers, in the presence of a corrinoid, which acts as an electron carrier. Expand
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Findings suggest that the corrinoid is a prosthetic group of MTa, a high-molecular-weight complex of at least 2000 kDa and between 900 to 1500 kDa when purified in the absence and presence of the detergent CHAPS, respectively, which may be homologous to theCorrinoid membrane protein purified before from M. thermoautotrophicum strain Marburg. Expand
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TLDR
Methanol is converted to methane by crude extracts of Methanosarcina barkeri by methanol:2-mercaptoethanesulfonic acid methyltransferase, which has an optimum at pH 6.5 and is not inhibited by 2-bromoethanelytic acid. Expand
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Methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri has been purified to approximately 90% homogeneity by ion-exchange chromatography on DEAE-cellulose and QAE-A50Expand
Methyl-coenzyme M, an intermediate in methanogenic dissimilation of C1 compounds by Methanosarcina barkeri
TLDR
Extracts of Methanosarcina barkeri possess a specific methyltransferase that catalyzes the transfer of the methyl group of methanol to 2-mercaptoethanesulfonic acid, which results in the formation of 2-(methylthio)ethanes sulfuronic acid. Expand
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Methanosarcina barkeri grew on methanol plus H(2) and depended strictly on the presence of sodium ions in the medium, which required for the biosynthesis of cellular constituents. Expand
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