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2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
2-oxo-4-methylthiobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
2-oxo-4-methylthiobutanoate + L-glutamate
L-methionine + ?
-
Substrates: -
Products: -
?
2-oxo-4-methylthiobutanoate + L-isoleucine
L-methionine + 2-oxo-methylvalerate
-
Substrates: -
Products: -
?
2-oxo-4-methylthiobutanoate + L-leucine
L-methionine + 2-oxo-isocaproate
-
Substrates: -
Products: -
r
2-oxo-4-methylthiobutanoate + L-phenylalanine
L-methionine + 2-oxo-3-phenylpropanoate
2-oxo-4-methylthiobutanoate + L-phenylalanine
L-methionine + ?
-
Substrates: -
Products: -
?
2-oxo-4-methylthiobutanoate + L-tryptophan
L-methionine + 3-(1H-indol-3-yl)-2-oxopropanoate
2-oxo-4-methylthiobutanoate + L-tyrosine
L-methionine + 4-hydroxyhenylpyruvate
-
Substrates: -
Products: -
r
2-oxo-4-methylthiobutanoate + L-valine
L-methionine + 2-oxo-isovalerate
-
Substrates: -
Products: -
?
4-methyl-2-oxopentanoate + ?
L-methionine + a 2-oxo acid
Substrates: 41% activity at 2 mM compared to 2-oxo-4-methylthiobutanoate
Products: -
r
5-methylthio-2-oxopentanoate + ?
L-methionine + a 2-oxo acid
Substrates: 48% activity at 0.1 mM and 53% activity at 2 mM compared to 2-oxo-4-methylthiobutanoate
Products: -
r
L-histidine + a 2-oxo acid
?
Substrates: 88% activity compared to L-methionine (at 1 mM)
Products: -
?
L-homomethionine + a 2-oxo acid
?
Substrates: 37% activity at 1 mM and 65% activity at 5 mM compared to L-methionine
Products: -
r
L-leucine + a 2-oxo acid
2-oxo-4-methylthiobutanoate + an L-amino acid
Substrates: 29% activity at 1 mM and 62% activity at 5 mM compared to 2-oxo-4-methylthiobutanoate
Products: -
r
L-leucine + a 2-oxo acid
?
Substrates: 11% activity compared to L-methionine (at 1 mM)
Products: -
?
L-methionine + 2-oxo-isocaproate
2-oxo-4-methylthiobutanoate + L-leucine
-
Substrates: -
Products: -
r
L-methionine + 2-oxoglutarate
2-oxo-4-methylthiobutanoate + L-glutamate
-
Substrates: -
Products: -
r
L-methionine + a 2-oxo acid
2-oxo-4-methylthiobutanoate + an L-amino acid
Substrates: recombinant enzyme shows high efficiency with L-methionine (100% activity at 1 and 5 mM)
Products: -
r
L-methionine + a 2-oxo acid
?
Substrates: the enzyme shows a preference for L-methionine (100% activity at 1 mM L-methionine)
Products: -
?
L-phenylalanine + a 2-oxo acid
?
Substrates: 57% activity compared to L-methionine (at 1 mM)
Products: -
?
L-tyrosine + a 2-oxo acid
?
Substrates: 9% activity compared to L-methionine (at 1 mM)
Products: -
?
additional information
?
-
2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
Substrates: recombinant enzyme shows high activity with 2-oxo-4-methylthiobutanoate (100% activity at 0.1 and 2 mM)
Products: -
r
2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
-
Substrates: a wide range of L-amino acids are effective donors, with Asp, Glu, Phe, His, Ile, Leu, Asn, Gln, Trp, and Tyr all producing more than 0.5 nM of L-methionine/min/mg of protein. Glu, Phe, Trp, and Tyr are the preferred amino donors, catalyzing the formation of above 1100 nM L-methionine/min/mg of protein
Products: -
?
2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
-
Substrates: a wide range of L-amino acids are effective donors, with Asp, Glu, Phe, His, Ile, Leu, Asn, Gln, Trp, and Tyr all producing more than 0.5 nM of L-methionine/min/mg of protein. Glu, Phe, Trp, and Tyr are the preferred amino donors, catalyzing the formation of above 1100 nM L-methionine/min/mg of protein
Products: -
?
2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
-
Substrates: isoleucine, leucine, and valine are the most effective substrates while glutamate and phenylalanine are also active as amino donors. Tyrosine and tryptophan have a much lesser ability to transaminate 2-oxo-4-methylthiobutanoate and all other L-amino acids are inactive
Products: -
?
2-oxo-4-methylthiobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
Substrates: while L-glutamate is capable of producing the highest maximum initial velocity for L-methionine production from 2-oxo-4-methylthiobutanoate, it is 5-10fold poorer in terms of substrate specificity when compared with L-tyrosine, L-tryptophan, and L-phenylalanine
Products: -
?
2-oxo-4-methylthiobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
Substrates: while L-glutamate is capable of producing the highest maximum initial velocity for L-methionine production from 2-oxo-4-methylthiobutanoate, it is 5-10fold poorer in terms of substrate specificity when compared with L-tyrosine, L-tryptophan, and L-phenylalanine
Products: -
?
2-oxo-4-methylthiobutanoate + L-phenylalanine
L-methionine + 2-oxo-3-phenylpropanoate
-
Substrates: -
Products: -
?
2-oxo-4-methylthiobutanoate + L-phenylalanine
L-methionine + 2-oxo-3-phenylpropanoate
-
Substrates: -
Products: -
?
2-oxo-4-methylthiobutanoate + L-tryptophan
L-methionine + 3-(1H-indol-3-yl)-2-oxopropanoate
-
Substrates: -
Products: -
?
2-oxo-4-methylthiobutanoate + L-tryptophan
L-methionine + 3-(1H-indol-3-yl)-2-oxopropanoate
-
Substrates: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not use L-isoleucine (at 1 mM), L-valine (at 1 and 5 mM), 4-methyl-2-oxopentanoate (at 0.1 mM), 6-methylthio-2-oxohexanoate, 3-methyl-2-oxopentanoate, and 3-methyl-2-oxobutyrate as substrates (at 0.1 mM each)
Products: -
?
additional information
?
-
Substrates: the enzyme does not use L-tryptophan, L-valine, L-asparagine, L-glutamate, and L-arginine as substrates
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not use L-tryptophan, L-valine, L-asparagine, L-glutamate, and L-arginine as substrates
Products: -
?
additional information
?
-
-
Substrates: the purified enzyme is unable to effectively utilize systems containing L-glutamate and oxaloacetate, L-glutamate and pyruvate, or L-alanine and 2-oxoglutarate
Products: -
?
additional information
?
-
-
Substrates: the purified enzyme is unable to effectively utilize systems containing L-glutamate and oxaloacetate, L-glutamate and pyruvate, or L-alanine and 2-oxoglutarate
Products: -
?
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0.045 - 4.2
2-oxo-4-methylthiobutanoate
2.85
L-isoleucine
-
apparent Km value, at pH 7.4, 37°C
2.5
L-leucine
-
apparent Km value, at pH 7.4, 37°C
0.93
L-methionine
recombinant enzyme, pH and temperature not specified in the publication
2.01 - 7.44
L-phenylalanine
1.42
L-tryptophan
-
recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C
2.01
L-tyrosine
-
recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C
1.77
L-valine
-
apparent Km value, at pH 7.4, 37°C
0.045
2-oxo-4-methylthiobutanoate
recombinant enzyme, pH and temperature not specified in the publication
2.46
2-oxo-4-methylthiobutanoate
-
recombinant enzyme, with L-tyrosine as cosubstrate, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C
4.2
2-oxo-4-methylthiobutanoate
-
apparent Km value, with L-leucine as cosubstrate, at pH 7.4, 37°C
9.53
L-glutamate
-
apparent Km value, at pH 7.4, 37°C
11.93
L-glutamate
-
recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C
2.01
L-phenylalanine
-
recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37°C
7.44
L-phenylalanine
-
apparent Km value, at pH 7.4, 37°C
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Venos, E.S.; Knodel, M.H.; Radford, C.L.; Berger, B.J.
Branched-chain amino acid aminotransferase and methionine formation in Mycobacterium tuberculosis
BMC Microbiol.
4
39
2004
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Schuster, J.; Knill, T.; Reichelt, M.; Gershenzon, J.; Binder, S.
Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis
Plant Cell
18
2664-2679
2006
Arabidopsis thaliana (Q9LE06)
brenda
Martinez-Cuesta, M.C.; Pelaez, C.; Eagles, J.; Gasson, M.J.; Requena, T.; Hanniffy, S.B.
YtjE from Lactococcus lactis IL1403 Is a C-S lyase with alpha, gamma-elimination activity toward methionine
Appl. Environ. Microbiol.
72
4878-4884
2006
no activity in Lactococcus lactis, no activity in Lactococcus lactis IL1403
brenda
Dolzan, M.; Johansson, K.; Roig-Zamboni, V.; Campanacci, V.; Tegoni, M.; Schneider, G.; Cambillau, C.
Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function
FEBS Lett.
571
141-146
2004
Escherichia coli (P77806), Escherichia coli
brenda
Heilbronn, J.; Wilson, J.; Berger, B.J.
Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumonia
J. Bacteriol.
181
1739-1747
1999
Klebsiella pneumoniae, Klebsiella pneumoniae ATCC 13883
brenda
Tavares, C.D.J.; Sharabi, K.; Dominy, J.E.; Lee, Y.; Isasa, M.; Orozco, J.M.; Jedrychowski, M.P.; Kamenecka, T.M.; Griffin, P.R.; Gygi, S.P.; Puigserver, P.
The methionine transamination pathway controls hepatic glucose metabolism through regulation of the GCN5 acetyltransferase and the PGC-1alpha transcriptional coactivator
J. Biol. Chem.
279
10635-10645
2016
Mus musculus, Mus musculus C57BL/6
brenda