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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
gamma-glutamylmethylamide synthetase,
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gamma-Glutamylmethylamide synthetase
Synthetase, gamma-glutamylmethylamide
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gamma-Glutamylmethylamide synthetase
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gamma-Glutamylmethylamide synthetase
D7R618
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gamma-Glutamylmethylamide synthetase
D7R618
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gamma-Glutamylmethylamide synthetase
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gamma-Glutamylmethylamide synthetase
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gamma-Glutamylmethylamide synthetase
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GMAS
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ATP + L-glutamate + methylamine = ADP + phosphate + N5-methyl-L-glutamine
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L-glutamate:methylamine ligase (ADP-forming)
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ATP + L-Glu + methylamine
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ATP + L-Glu + methylamine
ADP + phosphate + N5-methyl-L-glutamine
ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
ATP + L-glutamate + hydroxylamine
ADP + phosphate + N5-hydroxy-L-glutamine
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30-40% activity of the activity with methylamine for the native and recombinant enzymes
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
L-glutamic acid + ethylamine
theanine
additional information
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ATP + L-Glu + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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ATP + L-Glu + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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ATP + L-Glu + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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a step in theanine biosynthesis
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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the enzyme is involved in the theanine biosynthesis and usable in theanine formation by coupling with the alcoholic fermentation system of bakers yeast, Saccharomyces cerevisiae. Theanine, gamma-glutamyl-ethylamide, is a nonproteininc amino acid
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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72-75% activity of the activity with methylamine for the native and recombinant enzymes
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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the enzyme is involved in the theanine biosynthesis and usable in theanine formation by coupling with the alcoholic fermentation system of bakers yeast, Saccharomyces cerevisiae. Theanine, gamma-glutamyl-ethylamide, is a nonproteininc amino acid
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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72-75% activity of the activity with methylamine for the native and recombinant enzymes
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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a step in theanine biosynthesis
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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N5-methyl-L-glutamine is probably a temporary storage sink for methylamine
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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preferred substrate of the native and recombinant enzymes
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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N5-methyl-L-glutamine is probably a temporary storage sink for methylamine
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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L-glutamic acid + ethylamine
theanine
D7R618
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i.e. gamma-glutamylethylamide
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L-glutamic acid + ethylamine
theanine
D7R618
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i.e. gamma-glutamylethylamide
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L-glutamic acid + ethylamine
theanine
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i.e. gamma-glutamylethylamide
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additional information
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the isolated theanine-forming enzyme predominantly catalyzes the gamma-glutamyl-methylamide forming reaction
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additional information
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ammonia is a poor substrate
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additional information
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ammonia is a poor substrate showing 0.5-0.75% of the activity with methylamine for the native and recombinant enzymes
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additional information
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the isolated theanine-forming enzyme predominantly catalyzes the gamma-glutamyl-methylamide forming reaction
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additional information
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ammonia is a poor substrate showing 0.5-0.75% of the activity with methylamine for the native and recombinant enzymes
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additional information
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ammonia is a poor substrate
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ATP + L-Glu + methylamine
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
L-glutamic acid + ethylamine
theanine
additional information
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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a step in theanine biosynthesis
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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the enzyme is involved in the theanine biosynthesis and usable in theanine formation by coupling with the alcoholic fermentation system of bakers yeast, Saccharomyces cerevisiae. Theanine, gamma-glutamyl-ethylamide, is a nonproteininc amino acid
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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the enzyme is involved in the theanine biosynthesis and usable in theanine formation by coupling with the alcoholic fermentation system of bakers yeast, Saccharomyces cerevisiae. Theanine, gamma-glutamyl-ethylamide, is a nonproteininc amino acid
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ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
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a step in theanine biosynthesis
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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N5-methyl-L-glutamine is probably a temporary storage sink for methylamine
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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N5-methyl-L-glutamine is probably a temporary storage sink for methylamine
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ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
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L-glutamic acid + ethylamine
theanine
D7R618
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i.e. gamma-glutamylethylamide
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L-glutamic acid + ethylamine
theanine
D7R618
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i.e. gamma-glutamylethylamide
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additional information
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the isolated theanine-forming enzyme predominantly catalyzes the gamma-glutamyl-methylamide forming reaction
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additional information
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the isolated theanine-forming enzyme predominantly catalyzes the gamma-glutamyl-methylamide forming reaction
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additional information
no activation by Zn2+ and Ca2+
Mg2+
D7R618
dependent on, cannot be substituted by Mn2+
Mg2+
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requred, slightly stimulating
Mg2+
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Mg2+ or Mn2+ required
Mn2+
activates
Mn2+
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Mn2+ or Mg2+ required
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additional information
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ethylamine inhibits yeast sugar fermentation and recombinant theanine production in vivo in a coupled theanine-foorming reaction with Saccharomyces cerevisiae, which can be overcome by potassium phosphate addition, overview
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0.022 - 0.205
D7R618
different wild-type and mutant strains
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purified recombinant enzyme
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7.5 - 8
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recombinant and native enzymes
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6 - 10
pH 6.0: about 65% of maximal activity, pH 10.0: about 45% of maximal activity
6 - 9
pH 6.0: about 35% of maximal activity, pH 7.0, about 90% of maximal activity, pH 9.0: about 20% of maximal activity
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35 - 55
35°C: about 75% of maximal activity, 55°C: about 60% of maximal activity
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brenda
gene gms
D7R618
UniProt
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gene gms
D7R618
UniProt
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UniProt
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SwissProt
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MS, enzyme is inducible by growth on methylamine, dimethylamine, or trimethylamine
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additional information
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freeze-dried cells
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metabolism
D7R618
GMAS is involved in the gamma-glutamylmethylamine methylamine utilization pathway
metabolism
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GMAS is involved in the gamma-glutamylmethylamine methylamine utilization pathway
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physiological function
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gamma-glutamylmethylamide synthetase is essential for growth on methylamine as a carbon source but not as a nitrogen source
physiological function
gene gmaS is essential for utilization of monomethylamine as a carbon source. A mutant GmaS strain growing with succinate and monomethylamine as a nitrogen source shows residual growth
physiological function
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gamma-glutamylmethylamide synthetase is essential for growth on methylamine as a carbon source but not as a nitrogen source
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48820
D7R618
x * 48820, sequence calcualtion
50000
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x * 49000, about, sequence calculation, x * 50000, recombinnat enzyme, SDS-PAGE
49000
SDS-PAGE
49000
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x * 49000, about, sequence calculation, x * 50000, recombinnat enzyme, SDS-PAGE
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D7R618
x * 48820, sequence calcualtion
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x * 48820, sequence calcualtion
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x * 49000, about, sequence calculation, x * 50000, recombinnat enzyme, SDS-PAGE
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x * 49000, about, sequence calculation, x * 50000, recombinnat enzyme, SDS-PAGE
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the native as well as the recombinant enzyme is most stable at pH 6.0
691366
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24 h, 40% loss of activity
761648
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24 h, complete inactivation
761648
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30
3 h, less than 10% loss of activity
50
3 h, immediate loss of activity
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partially by ammonium sulfate fractionation
D7R618
recombinant enzyme from Escherichia coli strain AD494(DE3) by ammonium sulfate fractionation and anion exchange chromatography
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cloning from a genomic DNA library, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain AD494(DE3), subcloning in Escherichia coli strain JM109
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expression in Escherichia coli strain AD494(DE3)
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gene gms, gsIII-like gene, DNA and amino acid sequence determination and analysis, genetic structure
D7R618
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gamma-glutamylmethylamide synthetase is induced during growth on methylated amines
gamma-glutamylmethylamide synthetase is induced during growth on methylated amines
D7R618
gamma-glutamylmethylamide synthetase is induced during growth on methylated amines
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analysis
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assay for the enzymatic synthesis of gamma-glutamylmethylamide
synthesis
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the enzyme is usable in theanine formation by coupling with the alcoholic fermentation system of bakers yeast, Saccharomyces cerevisiae
synthesis
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the enzyme is enclosed with dried Saccharomyces cerevisiae cells in a dialysis membrane tube to produce theanine from glutamic acid and ethylamine to 100% conversion rate. Six repeats of the reaction are possible in presence of NAD+, overview
synthesis
efficient synthesis of gamma-glutamyl compounds by co-expression of gamma-glutamylmethylamide synthetase and polyphosphate kinase in engineered Escherichia coli
synthesis
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the enzyme is usable in theanine formation by coupling with the alcoholic fermentation system of bakers yeast, Saccharomyces cerevisiae
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Kung, H.F.; Wagner, C.
gamma-Glutamylamide. A new intermediate in the metabolism of methylamine
J. Biol. Chem.
244
4136-4140
1969
Pseudomonas sp.
brenda
Levitch, M.E.
The demonstration of two discrete enzymes catalyzing the synthesis of glutamine and gamma-glutamylmethylamide in the Pseudomonas MS
Biochem. Biophys. Res. Commun.
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609-614
1977
Pseudomonas sp.
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Levitch, M.E.
An assay for the enzymatic synthesis of gamma-glutamylmethylamide
Anal. Biochem.
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463-467
1977
Pseudomonas sp.
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Yamamoto, S.; Wakayama, M.; Tachiki, T.
Cloning and expression of Methylovorus mays No. 9 gene encoding gamma-glutamylmethylamide synthetase: an enzyme usable in theanine formation by coupling with the alcoholic fermentation system of bakers yeast
Biosci. Biotechnol. Biochem.
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101-109
2008
Methylovorus mays, Methylovorus mays No. 9
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Yamamoto, S.; Morihara, Y.; Wakayama, M.; Tachiki, T.
Theanine production by coupled fermentation with energy transfer using gamma-glutamylmethylamide synthetase of Methylovorus mays No. 9
Biosci. Biotechnol. Biochem.
72
1206-1211
2008
Methylovorus mays, Methylovorus mays No. 9
brenda
Latypova, E.; Yang, S.; Wang, Y.S.; Wang, T.; Chavkin, T.A.; Hackett, M.; Schaefer, H.; Kalyuzhnaya, M.G.
Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5
Mol. Microbiol.
75
426-439
2010
Methyloversatilis universalis (D7R618), Methyloversatilis universalis, Methyloversatilis universalis FAM5 (D7R618), Methyloversatilis universalis FAM5
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Yamamoto, S.; Morihara, Y.; Wakayama, M.; Tachiki, T.
Repeated batch production of theanine by coupled fermentation with energy transfer using membrane-enclosed gamma-glutamylmethylamide synthetase and dried yeast cells
Biosci. Biotechnol. Biochem.
73
2800-2802
2009
Methylovorus mays
brenda
Gruffaz, C.; Muller, E.E.; Louhichi-Jelail, Y.; Nelli, Y.R.; Guichard, G.; Bringel, F.
Genes of the N-methylglutamate pathway are essential for growth of Methylobacterium extorquens DM4 with monomethylamine
Appl. Environ. Microbiol.
80
3541-3550
2014
Methylorubrum extorquens (C7CGX7)
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Nayak, D.D.; Marx, C.J.
Methylamine utilization via the N-methylglutamate pathway in Methylobacterium extorquens PA1 involves a novel flow of carbon through C1 assimilation and dissimilation pathways
J. Bacteriol.
196
4130-4139
2014
Methylorubrum extorquens, Methylorubrum extorquens PA1
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Pan, X.; Yu, J.; Du, Q.; Zeng, S.; Liu, J.; Jiao, Q.; Zhang, H.
Efficient synthesis of gamma-glutamyl compounds by co-expression of gamma-glutamylmethylamide synthetase and polyphosphate kinase in engineered Escherichia coli
J. Ind. Microbiol. Biotechnol.
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573-583
2020
Methylovorus mays (A9ZPH9)
brenda
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