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show all sequences of 2.1.1.156

Characterization and regulation of the osmolyte betaine synthesizing enzymes GSMT and SDMT from halophilic methanogen Methanohalophilus portucalensis

Lai, S.J.; Lai, M.C.; PLoS ONE 6, e25090 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene Mpgsmt, DNA and amino acid sequence determination and analysis and sequence comparisons, phylogenetic analysis of GSMT, expression of complete gene cluster of Mpgsmt-sdmt in Escherichia coli strain BL21(DE3) and in strain MKH13 deficient in betaine transport, the recombinant enzyme is functional to synthesize and accumulate betaine and confers elevated survival ability in betaine transport deficient mutant strain MKH13 under high salt stress. The recombinantly expressed enzyme shows 10000fold lower catalytic efficiency compared with the enzyme isolated from the original cells
Methanohalophilus portucalensis
Inhibitors
Inhibitors
Commentary
Organism
Structure
betaine
feedback inhibition
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine
product inhibition
Methanohalophilus portucalensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.78
-
S-adenosyl-L-methionine
pH 7.3, 37C, recombinant enzyme, with sarcosine
Methanohalophilus portucalensis
8.26
-
S-adenosyl-L-methionine
pH 7.3, 37C, recombinant enzyme, with glycine
Methanohalophilus portucalensis
2320
-
glycine
pH 7.3, 37C, recombinant enzyme
Methanohalophilus portucalensis
3020
-
sarcosine
pH 7.3, 37C, recombinant enzyme
Methanohalophilus portucalensis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
dramatic activating effects of sodium and potassium ions on the in vitro methyltransferase activities of MpGSMT
Methanohalophilus portucalensis
additional information
level of potassium and sodium ions may modulate the substrate binding activity of MpGSMT through the conformational change
Methanohalophilus portucalensis
Na+
dramatic activating effects of sodium and potassium ions on the in vitro methyltransferase activities of MpGSMT
Methanohalophilus portucalensis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29040
-
2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation
Methanohalophilus portucalensis
35000
-
2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation
Methanohalophilus portucalensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Methanohalophilus portucalensis
the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
?
-
-
-
additional information
Methanohalophilus portucalensis FDF1
the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
?
-
-
-
S-adenosyl-L-methionine + glycine
Methanohalophilus portucalensis
-
S-adenosyl-L-homocysteine + sarcosine
-
-
?
S-adenosyl-L-methionine + glycine
Methanohalophilus portucalensis FDF1
-
S-adenosyl-L-homocysteine + sarcosine
-
-
?
S-adenosyl-L-methionine + sarcosine
Methanohalophilus portucalensis
-
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
?
S-adenosyl-L-methionine + sarcosine
Methanohalophilus portucalensis FDF1
-
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanohalophilus portucalensis
F6KV61
GSMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-
Methanohalophilus portucalensis FDF1
F6KV61
GSMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-
Purification (Commentary)
Commentary
Organism
recombinant MpGSMT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Methanohalophilus portucalensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
720836
Methanohalophilus portucalensis
?
-
-
-
-
additional information
the enzyme from Methanohalophilus portucalensis possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
720836
Methanohalophilus portucalensis
?
-
-
-
-
additional information
the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
720836
Methanohalophilus portucalensis FDF1
?
-
-
-
-
additional information
the enzyme from Methanohalophilus portucalensis possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
720836
Methanohalophilus portucalensis FDF1
?
-
-
-
-
S-adenosyl-L-methionine + glycine
-
720836
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine + sarcosine
-
-
-
?
S-adenosyl-L-methionine + glycine
-
720836
Methanohalophilus portucalensis FDF1
S-adenosyl-L-homocysteine + sarcosine
-
-
-
?
S-adenosyl-L-methionine + sarcosine
-
720836
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
-
?
S-adenosyl-L-methionine + sarcosine
-
720836
Methanohalophilus portucalensis FDF1
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation
Methanohalophilus portucalensis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Methanohalophilus portucalensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Methanohalophilus portucalensis
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
binding motifs and substrate binding sites from gsmt, overview
Methanohalophilus portucalensis
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Methanohalophilus portucalensis
sequence calculation
7
4.5
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.05
-
pH 7.3, 37C, recombinant enzyme, with glycine
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine
0.07
-
pH 7.3, 37C, recombinant enzyme, with sarcosine
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine
Cloned(Commentary) (protein specific)
Commentary
Organism
gene Mpgsmt, DNA and amino acid sequence determination and analysis and sequence comparisons, phylogenetic analysis of GSMT, expression of complete gene cluster of Mpgsmt-sdmt in Escherichia coli strain BL21(DE3) and in strain MKH13 deficient in betaine transport, the recombinant enzyme is functional to synthesize and accumulate betaine and confers elevated survival ability in betaine transport deficient mutant strain MKH13 under high salt stress. The recombinantly expressed enzyme shows 10000fold lower catalytic efficiency compared with the enzyme isolated from the original cells
Methanohalophilus portucalensis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
binding motifs and substrate binding sites from gsmt, overview
Methanohalophilus portucalensis
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.05
-
pH 7.3, 37C, recombinant enzyme, with glycine
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine
0.07
-
pH 7.3, 37C, recombinant enzyme, with sarcosine
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
betaine
feedback inhibition
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine
product inhibition
Methanohalophilus portucalensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.78
-
S-adenosyl-L-methionine
pH 7.3, 37C, recombinant enzyme, with sarcosine
Methanohalophilus portucalensis
8.26
-
S-adenosyl-L-methionine
pH 7.3, 37C, recombinant enzyme, with glycine
Methanohalophilus portucalensis
2320
-
glycine
pH 7.3, 37C, recombinant enzyme
Methanohalophilus portucalensis
3020
-
sarcosine
pH 7.3, 37C, recombinant enzyme
Methanohalophilus portucalensis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
dramatic activating effects of sodium and potassium ions on the in vitro methyltransferase activities of MpGSMT
Methanohalophilus portucalensis
additional information
level of potassium and sodium ions may modulate the substrate binding activity of MpGSMT through the conformational change
Methanohalophilus portucalensis
Na+
dramatic activating effects of sodium and potassium ions on the in vitro methyltransferase activities of MpGSMT
Methanohalophilus portucalensis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29040
-
2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation
Methanohalophilus portucalensis
35000
-
2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation
Methanohalophilus portucalensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Methanohalophilus portucalensis
the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
?
-
-
-
additional information
Methanohalophilus portucalensis FDF1
the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
?
-
-
-
S-adenosyl-L-methionine + glycine
Methanohalophilus portucalensis
-
S-adenosyl-L-homocysteine + sarcosine
-
-
?
S-adenosyl-L-methionine + glycine
Methanohalophilus portucalensis FDF1
-
S-adenosyl-L-homocysteine + sarcosine
-
-
?
S-adenosyl-L-methionine + sarcosine
Methanohalophilus portucalensis
-
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
?
S-adenosyl-L-methionine + sarcosine
Methanohalophilus portucalensis FDF1
-
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant MpGSMT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Methanohalophilus portucalensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
720836
Methanohalophilus portucalensis
?
-
-
-
-
additional information
the enzyme from Methanohalophilus portucalensis possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
720836
Methanohalophilus portucalensis
?
-
-
-
-
additional information
the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
720836
Methanohalophilus portucalensis FDF1
?
-
-
-
-
additional information
the enzyme from Methanohalophilus portucalensis possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities
720836
Methanohalophilus portucalensis FDF1
?
-
-
-
-
S-adenosyl-L-methionine + glycine
-
720836
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine + sarcosine
-
-
-
?
S-adenosyl-L-methionine + glycine
-
720836
Methanohalophilus portucalensis FDF1
S-adenosyl-L-homocysteine + sarcosine
-
-
-
?
S-adenosyl-L-methionine + sarcosine
-
720836
Methanohalophilus portucalensis
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
-
?
S-adenosyl-L-methionine + sarcosine
-
720836
Methanohalophilus portucalensis FDF1
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation
Methanohalophilus portucalensis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Methanohalophilus portucalensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Methanohalophilus portucalensis
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Methanohalophilus portucalensis
sequence calculation
7
4.5
Expression
Organism
Commentary
Expression
Methanohalophilus portucalensis
betaine downregulates GSMT expression enhanced with increasing temperature, transcription unit and transcription level of Mpgsmt-sdmt is reduced under temperature stresses up to 37C, but recovers at 45C to the level at 20C
down
General Information
General Information
Commentary
Organism
additional information
conserved glycine- and sarcosine-binding residue Arg167, binding site structures, overview. The level of potassium and sodium ions may modulate the substrate binding activity of MpGSMT through the conformational change
Methanohalophilus portucalensis
physiological function
GSMT from a halophilic methanoarchaeon regulates betaine biosynthesis pathway by a distinct mechanism. GSMT catalyzes the first enzymatic step in synthesis of the osmolyte betaine in halophilic archaea, GSMT may also play a major role in coupling the salt-in and compatible solute (osmolyte) osmoadaptative strategies in halophilic methanogens for adapting to high salt environments
Methanohalophilus portucalensis
General Information (protein specific)
General Information
Commentary
Organism
additional information
conserved glycine- and sarcosine-binding residue Arg167, binding site structures, overview. The level of potassium and sodium ions may modulate the substrate binding activity of MpGSMT through the conformational change
Methanohalophilus portucalensis
physiological function
GSMT from a halophilic methanoarchaeon regulates betaine biosynthesis pathway by a distinct mechanism. GSMT catalyzes the first enzymatic step in synthesis of the osmolyte betaine in halophilic archaea, GSMT may also play a major role in coupling the salt-in and compatible solute (osmolyte) osmoadaptative strategies in halophilic methanogens for adapting to high salt environments
Methanohalophilus portucalensis
Expression (protein specific)
Organism
Commentary
Expression
Methanohalophilus portucalensis
betaine downregulates GSMT expression enhanced with increasing temperature, transcription unit and transcription level of Mpgsmt-sdmt is reduced under temperature stresses up to 37C, but recovers at 45C to the level at 20C
down
Other publictions for EC 2.1.1.156
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)
733736
Niu
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Co-expression of ApGSMT and Ap ...
Aphanothece halophytica
Environ. Exp. Bot.
104
16-25
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1
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2
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1
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2
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1
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734932
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Transgenic Arabidopsis express ...
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4
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5
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4
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1
1
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734671
He
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Aphanothece halophytica
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31
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1
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2
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1
1
1
1
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720836
Lai
Characterization and regulatio ...
Methanohalophilus portucalensis, Methanohalophilus portucalensis FDF1
PLoS ONE
6
e25090
2011
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1
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2
4
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3
2
6
-
2
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1
-
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8
1
1
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1
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1
-
1
2
-
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1
1
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2
2
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4
-
3
2
6
-
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1
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8
1
1
-
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-
1
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-
1
1
2
2
1
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-
719715
Kimura
Glycine betaine biosynthesized ...
Myxococcus xanthus
J. Bacteriol.
192
1467-1470
2010
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1
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1
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1
2
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1
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2
1
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1
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1
1
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1
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1
2
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2
1
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2
2
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671647
Lu
Identification of glycine beta ...
Synechococcus sp. WH 8102
Arch. Microbiol.
186
495-506
2006
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1
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4
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3
2
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6
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1
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5
1
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2
1
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1
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4
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3
2
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1
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5
1
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2
1
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659286
Waditee
Isolation and functional chara ...
Aphanothece halophytica
J. Biol. Chem.
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4932-4942
2003
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1
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2
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12
9
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5
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9
2
1
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18
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657578
Nyyssola
Characterization of glycine sa ...
Halorhodospira halochloris
Appl. Environ. Microbiol.
67
2044-2050
2001
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1
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3
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3
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6
1
1
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659145
Nyyssola
Extreme halophiles synthesize ...
Actinopolyspora halophila, Halorhodospira halochloris
J. Biol. Chem.
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22196-22201
2000
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