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Physiology and posttranscriptional regulation of methanol:coenzyme M methyltransferase isozymes in Methanosarcina acetivorans C2A

Opulencia, R.B.; Bose, A.; Metcalf, W.W.; J. Bacteriol. 191, 6928-6935 (2009)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanosarcina acetivorans
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Expression
Organism
Commentary
Expression
Methanosarcina acetivorans
methanol-specific methyltransferase MT1 isozymes are encoded by three operons mtaCB1, mtaCB2, and mtaCB3. When expressed from the strong PmtaC1 or PmtaC2 promoter, each of the MtaC and MtaB proteins supports growth and methane production at wild-type levels. In contrast, all mtaCB operons exhibit poorer growth and lower rates of methane production when PmtaC3 controlls their expression. All combinations of MtaC, MtaB, and MtaA can form functional methyltransferase MT1/MT2 complexes. Variations in enzyme activity correlate with differences in protein abundance. The mtaCBA transcripts show different stabilities, which are strongly influenced by the growth substrate
additional information
Expression (protein specific)
Organism
Commentary
Expression
Methanosarcina acetivorans
methanol-specific methyltransferase MT1 isozymes are encoded by three operons mtaCB1, mtaCB2, and mtaCB3. When expressed from the strong PmtaC1 or PmtaC2 promoter, each of the MtaC and MtaB proteins supports growth and methane production at wild-type levels. In contrast, all mtaCB operons exhibit poorer growth and lower rates of methane production when PmtaC3 controlls their expression. All combinations of MtaC, MtaB, and MtaA can form functional methyltransferase MT1/MT2 complexes. Variations in enzyme activity correlate with differences in protein abundance. The mtaCBA transcripts show different stabilities, which are strongly influenced by the growth substrate
additional information
Other publictions for EC 2.1.1.90
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
726582
Hoeppner
Structure of the corrinoid:coe ...
Methanosarcina mazei
Acta Crystallogr. Sect. D
68
1549-1557
2012
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698630
Opulencia
Physiology and posttranscripti ...
Methanosarcina acetivorans
J. Bacteriol.
191
6928-6935
2009
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680470
Bose
Differential regulation of the ...
Methanosarcina acetivorans
J. Bacteriol.
188
7274-7283
2006
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682524
Hagemeier
Insight into the mechanism of ...
Methanosarcina barkeri
Proc. Natl. Acad. Sci. USA
103
18917-18922
2006
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Pritchett
Genetic, physiological and bio ...
Methanosarcina acetivorans
Mol. Microbiol.
56
1183-1194
2005
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485665
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
249
280-285
1997
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485666
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
243
670-677
1997
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727819
Daas
Activation mechanism of methan ...
Methanosarcina barkeri, Methanosarcina barkeri DSM 800
J. Biol. Chem.
271
22346-2251
1996
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Van der Meijden
Purification and properties of ...
Methanosarcina barkeri
J. Bacteriol.
160
629-635
1984
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485661
Van der Meijden
Reductive activation of methan ...
Methanosarcina barkeri
Biochem. Biophys. Res. Commun.
118
760-766
1984
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485663
Van der Meijden
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Methanol conversion in Eubacte ...
Eubacterium limosum, Methanothermobacter thermautotrophicus
Arch. Microbiol.
138
360-364
1984
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485662
Van der Meijden
Methyltransferases involved in ...
Methanosarcina barkeri
Arch. Microbiol.
134
238-242
1983
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485664
Taylor
A simplified assay for coenzym ...
Methanobacterium bryantii
J. Biol. Chem.
249
4886-4890
1974
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