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IUBMB Comments A pyridoxal-phosphate protein. The enzyme, found in both prokaryotes and eukaryotes, catalyses the last reaction in a methionine salvage pathway. In mammals this activity is catalysed by the multifunctional glutamine transaminase K (cf . EC 2.6.1.64 , glutamine—phenylpyruvate transaminase).
Synonyms 101251438 , mtnE , Solyc11g013170, Solyc11g013170.1, YkrV, ZEAMMB73_Zm00001d020696 ,
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Solyc11g013170
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locus name
Solyc11g013170.1
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locus name
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ZEAMMB73_Zm00001d020696
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mtnE
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YkrV
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L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate = 2-oxoglutaramate + L-methionine
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MetaCyc
S-methyl-5-thio-alpha-D-ribose 1-phosphate degradation I
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L-glutamine:4-(methylsulfanyl)-2-oxobutanoate aminotransferase
A pyridoxal-phosphate protein. The enzyme, found in both prokaryotes and eukaryotes, catalyses the last reaction in a methionine salvage pathway. In mammals this activity is catalysed by the multifunctional glutamine transaminase K (cf. EC 2.6.1.64, glutamine---phenylpyruvate transaminase).
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L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
L-histidine + 4-(methylsulfanyl)-2-oxobutanoate
3-((1H-imidazo)-4-yl)-2-oxopropanoate + L-methionine
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Substrates: -
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additional information
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L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
Substrates: -
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L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
Substrates: -
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L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
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Substrates: -
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L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
Substrates: -
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additional information
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Substrates: only L-glutamine is accepted as amino donor
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additional information
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Substrates: only L-glutamine is accepted as amino donor
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additional information
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Substrates: enzyme is almost completely specific for glutamine as amino donor, other amino acids giving no more than 1% of the activity measured with glutamine
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L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
Substrates: -
?
L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
Substrates: -
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4-(methylsulfanyl)-2-oxobutanoate
4-(methylsulfanyl)-2-oxobutanoate
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4-(methylsulfanyl)-2-oxobutanoate
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4-(methylsulfanyl)-2-oxobutanoate
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0.07 - 1.91
4-(methylsulfanyl)-2-oxobutanoate
0.07
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 25°C
0.22
4-(methylsulfanyl)-2-oxobutanoate
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pH 7.5, 25°C
1.91
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 37°C
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0.12 - 2.32
4-(methylsulfanyl)-2-oxobutanoate
0.12
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 25°C
0.15
4-(methylsulfanyl)-2-oxobutanoate
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pH 7.5, 25°C
2.32
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 37°C
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0.71 - 1.73
4-(methylsulfanyl)-2-oxobutanoate
0.71
4-(methylsulfanyl)-2-oxobutanoate
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pH 7.5, 25°C
1.26
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 37°C
1.73
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 25°C
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0.38 - 3.73
4-(methylsulfanyl)-2-oxobutanoate
0.38
4-(methylsulfanyl)-2-oxobutanoate
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pH 7.5, 25°C
1.61
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 25°C
3.73
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 37°C
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UniProt
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UniProt
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cf. EC 2.6.1.1
UniProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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MTNE_BACSU
Bacillus subtilis (strain 168)
398
0
44043
Swiss-Prot
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A0A1D6I5Q5_MAIZE
512
0
55661
TrEMBL
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
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Berger, B.; English, S.; Chan, G.; Knodel, M.
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
J. Bacteriol.
185
2418-2431
2003
Bacillus subtilis (O31665), Bacillus subtilis 168 (O31665)
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Ellens, K.; Richardson, L.; Frelin, O.; Collins, J.; Ribeiro, C.; Hsieh, Y.; Mullen, R.; Hanson, A.
Evidence that glutamine transaminase and omega-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants
Phytochemistry
113
160-169
2015
Bacillus subtilis (O31665), Bacillus subtilis 168 (O31665), Solanum lycopersicum, Zea mays (A0A1D6I5Q5)
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