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3-hydroxykynurenine + glyoxylate
xanthurenic acid + glycine
-
-
-
?
glycine + pyruvate
glyoxylate + L-alanine
glycine + pyruvate
L-alanine + glyoxylate
-
-
-
?
kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
-
-
-
?
L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
L-alanine + 2-oxobutyrate
pyruvate + 2-aminobutanoate
-
-
-
-
ir
L-alanine + 3-hydroxypyruvate
pyruvate + L-serine
-
-
-
?
L-alanine + 4-methylthio-2-oxobutyrate
pyruvate + L-methionine
-
poor amino acceptor
-
-
ir
L-alanine + glyoxylate
glycine + pyruvate
L-alanine + glyoxylate
pyruvate + glycine
L-alanine + hydroxypyruvate
pyruvate + L-serine
L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
L-alanine + pyruvate
pyruvate + L-alanine
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
L-aspartate + glyoxylate
2-oxosuccinate + glycine
-
-
-
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
L-glutamate + glyoxylate
2-oxoglutarate + glycine
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
L-glutamine + pyruvate
2-oxoglutaramate + L-alanine
-
-
-
-
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
L-histidine + pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
-
-
-
ir
L-isoleucine + glyoxylate
3-methyl-2-oxopropanoate + glycine
-
isoenzyme 1
-
-
ir
L-leucine + glyoxylate
4-methyl-2-oxopentanoate + glycine
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
L-tyrosine + pyruvate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-alanine
-
-
-
ir
L-valine + glyoxylate
3-methyl-2-oxobutanoate + glycine
-
isoenzyme 1
-
-
ir
Nomega,Nomega-dimethyl-L-arginine + pyruvate
5-(N,N-dimethylcarbamidamido)-2-oxopentanoate + alanine
-
-
-
?
additional information
?
-
glycine + pyruvate
glyoxylate + L-alanine
-
-
-
-
ir
glycine + pyruvate
glyoxylate + L-alanine
-
-
-
ir
L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
-
-
-
-
ir
L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
-
-
-
ir
L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
-
-
-
-
ir
L-alanine + glyoxylate
glycine + pyruvate
transamination half-reaction kinetic parameters
-
-
r
L-alanine + glyoxylate
glycine + pyruvate
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?, r
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
photorespiratory enzyme
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?, r
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
-
key role in the transamination/detoxification of glyoxylate
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
key role in the transamination/detoxification of glyoxylate
-
ir
L-alanine + glyoxylate
pyruvate + glycine
the enzyme is highly specific for catalysing glyoxylate to glycine processing, thereby playing a key role in glyoxylate detoxification
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
the enzyme is highly specific for catalysing glyoxylate to glycine processing
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
high substrate specificity for Ala and glyoxylate
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
high substrate specificity for Ala and glyoxylate
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
-
isoenzyme 1
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
isoenzyme 2 highly specific, little or no activity with other amino donors/acceptors
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
isoenzyme 1
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
isoenzyme 2 highly specific, little or no activity with other amino donors/acceptors
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates
-
ir
L-alanine + glyoxylate
pyruvate + glycine
Scomberomorus sp.
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
?
L-alanine + hydroxypyruvate
pyruvate + L-serine
-
-
-
-
ir
L-alanine + hydroxypyruvate
pyruvate + L-serine
-
-
-
-
ir
L-alanine + hydroxypyruvate
pyruvate + L-serine
-
isoenzyme 1
-
-
ir
L-alanine + hydroxypyruvate
pyruvate + L-serine
-
isoenzyme 1
-
-
ir
L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
-
isoenzyme 1, less effectively acceptor
-
-
ir
L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
-
isoenzyme 1, less effectively acceptor
-
-
ir
L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
-
isoenzyme 1
-
-
ir
L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
-
isoenzyme 1
-
-
ir
L-alanine + pyruvate
pyruvate + L-alanine
-
-
-
?
L-alanine + pyruvate
pyruvate + L-alanine
-
-
-
-
ir
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
-
-
-
ir
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
-
-
ir
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
-
-
?
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
-
-
-
?
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
-
isoenzyme 1
-
-
ir
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
-
isoenzyme 1
-
-
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
-
-
-
-
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
-
-
-
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
-
enzyme catalyzes both beta-elimination and half-transamination of L-cysteine together with pyruvate transamination via a ketimine common intermediate. L-cysteine partitions between the two reactions with a ratio of 2.5
-
?
L-glutamate + glyoxylate
2-oxoglutarate + glycine
-
-
-
?
L-glutamate + glyoxylate
2-oxoglutarate + glycine
-
-
-
?
L-glutamate + glyoxylate
2-oxoglutarate + glycine
-
-
-
-
ir
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
-
-
-
-
ir
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
-
isoenzyme 1
-
-
ir
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
-
isoenzyme 1
-
-
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
-
-
-
-
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
-
-
-
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
-
isoenzyme 1
-
-
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
-
isoenzyme 1
-
-
ir
L-leucine + glyoxylate
4-methyl-2-oxopentanoate + glycine
-
isoenzyme 1
-
-
ir
L-leucine + glyoxylate
4-methyl-2-oxopentanoate + glycine
-
isoenzyme 1
-
-
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
-
-
-
-
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
-
-
-
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
-
isoenzyme 1
-
-
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
-
isoenzyme 1
-
-
ir
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
-
-
-
-
ir
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
-
-
-
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
-
-
-
-
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
-
-
-
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
-
-
-
?
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
-
isoenzyme 1
-
-
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
-
isoenzyme 1
-
-
ir
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
-
-
-
-
ir
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
isoenzyme 1
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
isoenzyme 1
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
Scomberomorus sp.
-
-
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
-
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
isoenzyme 1
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
isoenzyme 1
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
isoenzyme 1
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
isoenzyme 1
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
Scomberomorus sp.
-
-
-
-
ir
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
-
-
-
-
ir
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
-
-
-
ir
L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
-
-
-
-
ir
L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
-
-
-
ir
L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
-
-
-
ir
L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
-
isoenzyme 1
-
-
ir
L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
-
isoenzyme 1
-
-
ir
additional information
?
-
-
aminoadipate, asparagine, aspartate, glutamate, isoleucine, lysine, threonine and valine are no substrates
-
-
?
additional information
?
-
enzymatic activity is not detected using beta-alanine as the amino donor with either pyruvate or glyoxylate as amino acceptors
-
-
-
additional information
?
-
-
enzymatic activity is not detected using beta-alanine as the amino donor with either pyruvate or glyoxylate as amino acceptors
-
-
-
additional information
?
-
enzymatic activity is not detected using beta-alanine as the amino donor with either pyruvate or glyoxylate as amino acceptors
-
-
-
additional information
?
-
-
isoenzyme 1, little or no activity with 2-oxoglutarate as amino acceptor and alanine, serine, glutamic acid, isoleucine, methionine, glutamine, asparagine, valine, aspartic acid, leucine, phenylalanine, tyrosine, histidine, tryptophan or 5-hydroxytryptophan
-
-
?
additional information
?
-
aminoadipate, asparagine, aspartate, glutamate, isoleucine, lysine, threonine and valine are no substrates
-
-
?
additional information
?
-
-
aminoadipate, asparagine, aspartate, glutamate, isoleucine, lysine, threonine and valine are no substrates
-
-
?
additional information
?
-
-
isoenzyme 1, little or no activity with 2-oxoglutarate as amino acceptor and alanine, serine, glutamic acid, isoleucine, methionine, glutamine, asparagine, valine, aspartic acid, leucine, phenylalanine, tyrosine, histidine, tryptophan or 5-hydroxytryptophan
-
-
?
additional information
?
-
-
enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification
-
-
?
additional information
?
-
enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification
-
-
?
additional information
?
-
alanine:glyoxylate aminotransferase is able to catalyze the alpha,beta-elimination of beta-chloro-L-alanine with a catalytic efficiency similar to that of the physiological transaminase reaction with L-alanine. The enzyme catalyzes both the alpha,beta-elimination and half-transamination of the natural amino acid L-cysteine together with pyruvate half-transamination
-
-
?
additional information
?
-
enzyme is able to catalyze the alpha,beta-elimination of beta-chloro-L-alanine with a kcat value of 0.74 per s and a Km value of 0.51 mM
-
-
?
additional information
?
-
-
mitochondrially localized human AGXT2 is able to effectively metabolize asymmetric dimethylarginine in vivo
-
-
?
additional information
?
-
the enzyme is also active as serine-pyruvate aminotransferase, EC 2.6.1.51
-
-
-
additional information
?
-
-
isoenzyme 1, little or no activity with 2-oxoglutarate as amino acceptor and alanine, serine, glutamic acid, isoleucine, methionine, glutamine, asparagine, valine, aspartic acid, leucine, phenylalanine, tyrosine, histidine, tryptophan or 5-hydroxytryptophan
-
-
?
additional information
?
-
-
isoenzyme 1, little or no activity with 2-oxoglutarate as amino acceptor and alanine, serine, glutamic acid, isoleucine, methionine, glutamine, asparagine, valine, aspartic acid, leucine, phenylalanine, tyrosine, histidine, tryptophan or 5-hydroxytryptophan
-
-
?
additional information
?
-
-
2-oxoglutarate is not an amino acceptor, little or no activity with asparagine, glutamine, glutamate, threonine, cysteine, methionine, arginine, leucine, valine, isoleucine, phenylalanine, tryptophan, histidine or tyrosine as amino donors
-
-
?
additional information
?
-
-
utilizes only glyoxylate as amino acceptor, hydroxypyruvate, 2-oxoglutarate, phenylpyruvate and 2-oxo-4-methyl-thiobutyrate are inactive, only L-alanine as amino donor, L-serine, L-threonine, L-glutamic acid, L-glutamine, L-aspartic acid, L-asparagine, L-ornithine, L-leucine, L-valine, L-isoleucine, L-histidine, L-phenylalanine, L-tryptophan and L-tyrosine are no substrates
-
-
?
additional information
?
-
-
strict specificity for L-alanine and glyoxylate as substrates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2.7
2-oxobutyrate
-
pH 8.0, 37°C, alanine as amino donor
18
3-hydroxykynurenine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
3.7
kynurenine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
1
L-cysteine
pH 7.4, Km value of L-cysteine is decreased by 40fold and 200fold in comparison with those of L-alanine and L-serine
additional information
additional information
-
60
2-aminobutyrate
-
pH 8.0, 37°C, glyoxylate as amino acceptor
100
2-aminobutyrate
-
pH 8.0, 37°C, pyruvate as amino acceptor
22
glycine
pH 7.4, 25°C, wild-type enzyme
22
glycine
wild-type, 25°C
0.038
glyoxylate
pH 7.4, 25°C
0.07
glyoxylate
-
pH 8.2, 37°C, isoenzyme 1, alanine as amino donor
0.1
glyoxylate
-
pH 8.2, 37°C, isoenzyme 1, alanine as amino donor
0.13
glyoxylate
-
pH 8.2, 37°C, isoenzyme 1, alanine as amino donor
0.13
glyoxylate
-
G41V, pH not specified in the publication, temperature not specified in the publication
0.14
glyoxylate
cosubstrate L-glutamate, pH 7.5, 25°C
0.15
glyoxylate
-
pH 7.0, 27°C, alanine as amino donor
0.15
glyoxylate
mutant G82E, 25°C
0.15
glyoxylate
pH 7.4, 25°C, mutant enzyme G82E
0.15
glyoxylate
-
G82E, pH not specified in the publication, temperature not specified in the publication
0.18
glyoxylate
pH 8.0, 37°C
0.18
glyoxylate
recombinant mutant R118A, pH 7.4, 25°C
0.2
glyoxylate
-
pH 8.2, 37°C, isoenzyme 1, alanine as amino donor
0.2
glyoxylate
recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C
0.21
glyoxylate
cosubstrate L-glutamate, pH 7.5, 25°C
0.22
glyoxylate
minor allele wild type enzyme
0.22
glyoxylate
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
0.22
glyoxylate
recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C
0.23
glyoxylate
pH 7.4, 25°C, wild-type enzyme
0.23
glyoxylate
-
pH 8.0, 37°C, recombinant His-AGT, L-alanine as amino donor
0.23
glyoxylate
wild-type, 25°C
0.23
glyoxylate
major allele wild type enzyme
0.23
glyoxylate
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
0.23
glyoxylate
recombinant mutant I56N-Ma, pH 7.4, 25°C
0.23
glyoxylate
recombinant wild-type enzyme AGT-Ma, pH 7.4, 25°C
0.25
glyoxylate
minor allele mutant enzyme F152I
0.25
glyoxylate
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
0.28
glyoxylate
major allele wild mutant enzyme F152I
0.28
glyoxylate
-
F152I, pH not specified in the publication, temperature not specified in the publication
0.28
glyoxylate
recombinant mutant F240S, pH 7.4, 25°C
0.31
glyoxylate
cosubstrate L-alanine, pH 7.5, 25°C
0.32
glyoxylate
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
0.34
glyoxylate
major allele wild mutant enzyme F152A
0.36
glyoxylate
-
pH 7.4, 37°C, alanine as amino donor
0.39
glyoxylate
-
pH 8.0, 37°C, recombinant AGT-His, L-alanine as amino donor
0.41
glyoxylate
-
G41R, pH not specified in the publication, temperature not specified in the publication
0.44
glyoxylate
-
pH 8.0, 37°C, alanine as amino donor
0.51
glyoxylate
cosubstrate L-alanine, pH 7.5, 25°C
0.56
glyoxylate
at pH 8.0 and 30°C
0.6
glyoxylate
recombinant mutant I56N-Mi, pH 7.4, 25°C
0.67
glyoxylate
-
pH 8.0, 37°C, 2-aminobutyrate as amino donor
0.7
glyoxylate
-
pH 8.2, 37°C, isoenzyme 2, alanine as amino donor
0.71
glyoxylate
recombinant mutant F238S, pH 7.4, 25°C
0.72
glyoxylate
-
pH 8.0, 37°C, alanine as amino donor
0.88
glyoxylate
recombinant mutant P11R/I56N-Ma, pH 7.4, 25°C
0.9
glyoxylate
in 50 mM NaPO4 (pH 8.0), at 70°C
1
glyoxylate
-
pH 8.2, 37°C, isoenzyme 2, alanine as amino donor
1
glyoxylate
recombinant mutant P11R-Ma, pH 7.4, 25°C
1.6
glyoxylate
-
pH 7.0, 50°C, alanine as amino donor
2.5
glyoxylate
-
pH 8.0, 37°C, L-alanine as amino donor
64
glyoxylate
pH 7.0, 50°C, alanine as amino donor
0.24
L-alanine
-
pH 7.5, 37°C, mitochondrial isozyme, glyoxylate as amino acceptor
0.52
L-alanine
-
isoenzyme AGT 1
0.63
L-alanine
at pH 8.0 and 30°C
0.88
L-alanine
-
GPT 1, alanine:2-oxoglutarate aminotransferase AGT activity
1.11
L-alanine
-
pH 7.5, 37°C, cytosolic isozyme, glyoxylate as amino acceptor
1.4
L-alanine
-
pH 8.2, 37°C, isoenzyme 1, glyoxylate as amino acceptor
1.6
L-alanine
-
pH 7.0, 27°C, glyoxylate as amino acceptor
2.1
L-alanine
-
pH 8.2, 37°C, isoenzyme 1, glyoxylate as amino acceptor
2.1
L-alanine
-
pH 8.2, 37°C, glyoxylate as amino acceptor
2.26
L-alanine
pH 8.0, 37°C
2.6
L-alanine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
2.9
L-alanine
-
pH 8.0, 37°C, 2-oxobutyrate as amino acceptor
3
L-alanine
-
pH 8.2, 37°C, isoenzyme 1, glyoxylate as amino acceptor
3.3
L-alanine
-
isoenzyme AGT 2
3.56
L-alanine
pH 7.5, 25°C
3.9
L-alanine
-
pH 8.2, 37°C, isoenzyme 1, glyoxylate as amino acceptor
4.76
L-alanine
pH 7.5, 25°C
8.1
L-alanine
in 50 mM NaPO4 (pH 8.0), at 70°C
9.1
L-alanine
-
pH 8.0, 37°C, recombinant His-AGT, glyoxylate as amino acceptor
9.4
L-alanine
-
pH 8.0, 37°C, recombinant AGT-His, glyoxylate as amino acceptor
11
L-alanine
-
pH 8.0, 37°C, glyoxylate as amino acceptor
13.5
L-alanine
-
pH 8.0, 37°C, glyoxylate as amino acceptor
14.9
L-alanine
-
pH 7.4, 37°C, glyoxylate as amino acceptor
15
L-alanine
mutant G82E, 25°C
15
L-alanine
pH 7.4, 25°C, mutant enzyme G82E
15
L-alanine
-
G82E, pH not specified in the publication, temperature not specified in the publication
18
L-alanine
-
pH 7.0, 50°C, glyoxylate as amino acceptor
22
L-alanine
-
G41R, pH not specified in the publication, temperature not specified in the publication
25
L-alanine
-
pH 8.2, 37°C, isoenzyme 2, glyoxylate as amino acceptor
28
L-alanine
minor allele wild type enzyme
28
L-alanine
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
28
L-alanine
recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C
30
L-alanine
-
pH 8.2, 37°C, isoenzyme 2, glyoxylate as amino acceptor
30
L-alanine
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
31
L-alanine
pH 7.4, 25°C, wild-type enzyme
31
L-alanine
wild-type, 25°C
31
L-alanine
major allele wild type enzyme
31
L-alanine
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
31
L-alanine
recombinant wild-type enzyme AGT-Ma, pH 7.4, 25°C
34
L-alanine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
37
L-alanine
major allele mutant enzyme F152I
37
L-alanine
-
F152I, pH not specified in the publication, temperature not specified in the publication
37
L-alanine
recombinant mutant P11R-Ma, pH 7.4, 25°C
41
L-alanine
minor allele mutant enzyme F152I
41
L-alanine
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
42
L-alanine
-
G41V, pH not specified in the publication, temperature not specified in the publication
43
L-alanine
recombinant mutant I56N-Mi, pH 7.4, 25°C
46
L-alanine
major allele mutant enzyme F152A
46
L-alanine
recombinant mutant F238S, pH 7.4, 25°C
51
L-alanine
recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C
52
L-alanine
pH 7.4, 25°C
59
L-alanine
recombinant mutant I56N-Ma, pH 7.4, 25°C
77
L-alanine
recombinant mutant R118A, pH 7.4, 25°C
80
L-alanine
recombinant mutant P11R/I56N-Ma, pH 7.4, 25°C
84
L-alanine
recombinant mutant F240S, pH 7.4, 25°C
101.2
L-alanine
pH 7.0, 37°C, glyoxylate as amino acceptor
149
L-alanine
pH 7.0, 50°C, glyoxylate as amino acceptor
1.7
L-glutamate
-
pH 7.0, 27°C, glyoxylate as amino acceptor
1.97
L-glutamate
pH 7.5, 25°C
3.32
L-glutamate
pH 7.5, 25°C
0.39
L-serine
pH 7.0, 37°C, SGT activity, pyruvate as amino acceptor
1.52
L-serine
pH 7.0, 37°C, SGT activity, glyoxylate as amino acceptor
256
L-serine
pH 7.0, 50°C, glyoxylate as amino acceptor
0.21
pyruvate
pH 7.4, 25°C, wild-type enzyme
0.21
pyruvate
wild-type, 25°C
2.5
pyruvate
-
pH 8.0, 37°C, 2-aminobutyrate as amino donor
51
pyruvate
pH 7.0, 50°C, serine as amino donor
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes
-
additional information
additional information
steady-state Michaelis-Menten kinetics
-
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20
3-hydroxykynurenine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
12
kynurenine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
0.33
glycine
pH 7.4, 25°C, wild-type enzyme
0.33
glycine
wild-type, 25°C
0.068
glyoxylate
mutant G82E, 25°C
0.068
glyoxylate
pH 7.4, 25°C, mutant enzyme G82E
0.068
glyoxylate
-
G82E, pH not specified in the publication, temperature not specified in the publication
11.1
glyoxylate
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
16
glyoxylate
-
pH 7.0, 50°C, L-alanine as amino donor
18.3
glyoxylate
-
G41V, pH not specified in the publication, temperature not specified in the publication
19
glyoxylate
recombinant mutant R118A, pH 7.4, 25°C
20
glyoxylate
recombinant mutant F240S, pH 7.4, 25°C
20.5
glyoxylate
-
G41R, pH not specified in the publication, temperature not specified in the publication
22
glyoxylate
recombinant mutant I56N-Mi, pH 7.4, 25°C
22
glyoxylate
recombinant mutant P11R/I56N-Ma, pH 7.4, 25°C
22.6
glyoxylate
major allele wild mutant enzyme F152A
23
glyoxylate
recombinant mutant P11R-Ma, pH 7.4, 25°C
30
glyoxylate
recombinant mutant I56N-Ma, pH 7.4, 25°C
33
glyoxylate
recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C
35
glyoxylate
recombinant mutant F238S, pH 7.4, 25°C
37
glyoxylate
minor allele wild type enzyme
37
glyoxylate
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
39
glyoxylate
major allele wild mutant enzyme F152I
39
glyoxylate
-
F152I, pH not specified in the publication, temperature not specified in the publication
39
glyoxylate
recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C
40
glyoxylate
minor allele mutant enzyme F152I
40
glyoxylate
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
45
glyoxylate
pH 7.4, 25°C, wild-type enzyme
45
glyoxylate
wild-type, 25°C
45
glyoxylate
major allele wild type enzyme
45
glyoxylate
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
45
glyoxylate
recombinant wild-type enzyme AGT-Ma, pH 7.4, 25°C
113
glyoxylate
pH 7.0, 50°C, L-alanine as amino donor
0.07
L-alanine
mutant G82E, 25°C
0.07
L-alanine
pH 7.4, 25°C, mutant enzyme G82E
0.07
L-alanine
-
G82E, pH not specified in the publication, temperature not specified in the publication
0.147
L-alanine
pH 7.4, 25°C
3 - 6
L-alanine
recombinant mutant F238S, pH 7.4, 25°C
10.6
L-alanine
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
17.1
L-alanine
-
G41V, pH not specified in the publication, temperature not specified in the publication
18
L-alanine
recombinant mutant I56N-Mi, pH 7.4, 25°C
19
L-alanine
recombinant mutant P11R/I56N-Ma, pH 7.4, 25°C
19.8
L-alanine
-
G41R, pH not specified in the publication, temperature not specified in the publication
20
L-alanine
-
pH 7.0, 50°C, glyoxylate as amino acceptor
21
L-alanine
recombinant mutant R118A, pH 7.4, 25°C
21.2
L-alanine
major allele mutant enzyme F152A
22
L-alanine
recombinant mutant F240S, pH 7.4, 25°C
22
L-alanine
recombinant mutant P11R-Ma, pH 7.4, 25°C
29
L-alanine
recombinant mutant I56N-Ma, pH 7.4, 25°C
33
L-alanine
minor allele wild type enzyme
33
L-alanine
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
33.6
L-alanine
minor allele mutant enzyme F152I
33.6
L-alanine
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
34.2
L-alanine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
35
L-alanine
major allele mutant enzyme F152I
35
L-alanine
-
F152I, pH not specified in the publication, temperature not specified in the publication
35
L-alanine
recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C
37
L-alanine
recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C
45
L-alanine
pH 7.4, 25°C, wild-type enzyme
45
L-alanine
wild-type, 25°C
45
L-alanine
major allele wild type enzyme
45
L-alanine
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
45
L-alanine
recombinant wild-type enzyme AGT-Ma, pH 7.4, 25°C
117
L-alanine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
131
L-alanine
pH 7.0, 50°C, glyoxylate as amino acceptor
0.36
pyruvate
pH 7.4, 25°C, wild-type enzyme
0.36
pyruvate
wild-type, 25°C
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metabolism
the expression of At3g08860 is highly coordinated with the genes of the uracil degradation pathway leading to the non-proteinogenic amino acid beta-alanine
evolution
AGT is a homodimer and belongs to the fold type I family of PLP-dependent enzymes. Enzyme AGT is present in the human population in two allelic forms, the major allele encoding AGT-Ma and the minor allele encoding AGT-Mi, the latter characterized by the Pro11 to Leu and Ile340 to Met amino acid substitutions
evolution
AGT is homodimeric and belongs to the fold type I family of PLP-dependent enzymes
evolution
aminotransferase enzymes function via a bimolecular double displacement ping-pong mechanism where an amino acid usually serves as the amino donor and an alpha-keto acid serves as the amino acceptor. Aminotransferases are ubiquitous in the three domains of life and are involved in a variety of metabolic pathways including amino acid metabolism, nitrogen assimilation, gluconeogenesis, responses to a number of biotic/abiotic stresses, and among other pathways. The aminotransferase gene family in the model plant Arabidopsis thaliana consists of 44 genes, eight of which are suggested to be alanine aminotransferases. One of the putative alanine aminotransferases genes, At3g08860, is attributed the function of alanine:glyoxylate aminotransferase/beta-alanine:pyruvate aminotransferase based on the analysis of gene expression networks and homology to other beta-alanine aminotransferases in plants
evolution
enzyme AGT is present in the human population in two allelic forms, the major allele encoding AGT-Ma and the minor allele encoding AGT-Mi, the latter characterized by the Pro11 to Leu and Ile340 to Met amino acid substitutions
malfunction
alanine:glyoxylate aminotransferase deficiency causes primary hyperoxaluria type 1
malfunction
-
causes the hereditary kidney stone disease primary hyperoxaluria type 1
malfunction
-
deficiency is responsible for Primary Hyperoxaluria Type 1, an autosomal recessive disorder
malfunction
mutation W251K involved in primary hyperoxaluria type 1
malfunction
-
primary hyperoxaluria type 1, a lethal inborn error of glyoxylate metabolism characterized by increased oxalate production, is caused by a deficiency of hepatic peroxisomal alanine:glyoxylate aminotransferase
malfunction
-
The hereditary kidney stone disease primary hyperoxaluria type 1 is caused by a deficiency of the peroxisomal enzyme alanine:glyoxylate aminotransferase
malfunction
critical role of AGXT deletion during HCC progression, loss of AGXT expression is correlated with a poor prognosis and differentiation of HCC. Loss of AGXT expression promotes the malignant phenotypes of HCC cell lines
malfunction
deficit of AGT causes primary hyperoxaluria type I (PH1) (OMIM 259900), a rare metabolic recessive disease due to inborn errors affecting the metabolism of glyoxylate in liver peroxisomes. Molecular dynamics simulations of F152I-Mi and I244T-Mi variants associated with PH1 and implications in their pathogenicity
malfunction
deficit of AGT leads to primary hyperoxaluria type I (PH1), a rare disease characterized by calcium oxalate stones deposition in the urinary tract as a consequence of glyoxylate accumulation. Most missense mutations cause AGT misfolding, as in the case of the G41R, which induces aggregation and proteolytic degradation
malfunction
possible inverse correlation between the degree of destabilization/misfolding induced by a mutation and the extent of vitamin B6 responsiveness in PH1. Among the 79 missense mutations known to be associated with PH1, 26 involve residues directly located at the monomer-monomer interface
malfunction
primary hyperoxaluria type I (PH1) is a rare disease caused by mutations in the AGXT gene encoding alanine:glyoxylate aminotransferase (AGT), a liver enzyme involved in the detoxification of glyoxylate, the failure of which results in accumulation of oxalate and kidney stones formation. The role of protein misfolding in the AGT deficit caused by most PH1-causing mutations. Analysis of the clinical, biochemical and cellular effects of the p.Ile56Asn mutation, recently described in a PH1 patient, as a function of the residue at position 11, a hot-spot for both polymorphic (p.Pro11Leu) and pathogenic (p.Pro11Arg) mutations, overview. As compared with the non-pathogenic forms, AGT variants display reduced expression and activity in mammalian cells. Vitamin B6, a currently approved treatment for PH1, can overcome the effects of the p.Ile56Asn mutation only when it is associated with Pro at position 11. Primary hyperoxaluria type I (PH1), the most severe form of primary hyperoxaluria, is an inherited condition characterized by an increased endogenous production of oxalate, a metabolic end-product excreted by urine, that leads to the formation and precipitation of calcium oxalate crystals, first in the kidneys and urinary tract and then in many tissues including skin, bones, heart and retina, a condition known as systemic oxalosis
physiological function
-
overexpression of human AGXT2 protects from asymmetric dimethylarginine-induced inhibition in nitric oxide production
physiological function
-
indispensable for appressorium function
physiological function
-
seems to be required for mobilization and utilization of triglycerides during infection process (to generate glycerol required for mechanical breaching of the host surface)
physiological function
alanine:glyoxylate aminotransferase (AGT) catalyzes the conversion of L-alanine and glyoxylate into pyruvate and glycine in liver peroxisomes, using pyridoxal 5'-phosphate (PLP) as coenzyme
physiological function
Arabidopsis thaliana alanine:glyoxylate aminotransferase 1 (AGT1) is a multifunctional class IV aminotransferase protein that catalyzes transamination reactions using L-serine, L-alanine, and L-asparagine as amino donors and glyoxylate, pyruvate, and hydroxypyruvate as amino acceptors. AGT1 is a peroxisomal aminotransferase with a central role in photorespiration. This enzyme catalyzes various aminotransferase reactions, including serine:glyoxylate, alanine:glyoxylate, and asparagine:glyoxylate transaminations
physiological function
primary hyperoxaluria type I (PH1) is a rare disease caused by the deficit of liver alanine-glyoxylate aminotransferase (AGT). AGT prevents oxalate formation by converting peroxisomal glyoxylate to glycine. When the enzyme is deficient, progressive calcium oxalate stones deposit first in the urinary tract and then at the systemic level. Pyridoxal 5'-phosphate (PLP), the AGT coenzyme, exerts a chaperone role by promoting dimerization
physiological function
role of AGXT in hepatocellular carcinoma (HCC) progression with effects of AGXT on cell cycle and apoptosis in HCC cells. The proportions of both early apoptotic and late apoptotic/necrotic cells increase as the expression of AGXT decreases
physiological function
the endogenous inhibitor of nitric oxide synthases asymmetric dimethylarginine (ADMA) can be catabolized by dimethylarginine dimethylaminohydrolase (DDAH, EC 3.5.3.18) or metabolized through an alternative pathway by alanine:glyoxylate aminotransferase 2 (AGXT2) with the formation of 2-oxo-D-(N,N-dimethylguanidino)valeric acid (ADGV). AGXT2 can metabolize the cardiovascular risk factors N-monomethylarginine (NMMA), asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA)
physiological function
the enzyme produces beta-alanine, which is an osmoprotectant in plants
physiological function
-
the enzyme produces beta-alanine, which is an osmoprotectant in plants
-
additional information
Arg118, Phe238 and Phe240 are interfacial residues not essential for transaminase activity but important for dimer-monomer dissociation. Molceular dynamics simulations
additional information
-
Arg118, Phe238 and Phe240 are interfacial residues not essential for transaminase activity but important for dimer-monomer dissociation. Molceular dynamics simulations
additional information
in the enzyme crystal, another dimer related by noncrystallographic symmetry makes close interactions to form a tetramer mediated in part by an extra carboxyl-terminal helix conserved in plant homologues of AGT1. Residues Tyr35' and Arg36', entering the active site from the other subunits in the dimer, mediate interactions between AGT and L-serine when used as a substrate. Structural model of AGT1 and structure-function analysis, structure comparisons, detailed overview
additional information
-
in the enzyme crystal, another dimer related by noncrystallographic symmetry makes close interactions to form a tetramer mediated in part by an extra carboxyl-terminal helix conserved in plant homologues of AGT1. Residues Tyr35' and Arg36', entering the active site from the other subunits in the dimer, mediate interactions between AGT and L-serine when used as a substrate. Structural model of AGT1 and structure-function analysis, structure comparisons, detailed overview
additional information
structural analysis and homology modeling of the At3g08860-encoded enzyme
additional information
-
structural analysis and homology modeling of the At3g08860-encoded enzyme
additional information
the AGT catalytic mechanism is typical of PLP-dependent aminotransferases and comprises two half-reactions. In the first one, the alpha-amino group of the substrate L-alanine displaces the epsilon-amino group of Lys209 producing the external aldimine. Then, Lys209 acts as a general base for the 1,3-prototropic shift generating a ketimine intermediate, which hydrolyzes to pyruvate and pyridoxamine 5'-phosphate (PMP). In the second half-reaction, glyoxylate binds to AGT-PMP and, through the same steps of the first reaction but in a reverse order, is converted to glycine regenerating AGT-PLP
additional information
the overall transamination catalyzed by AGT follows a ping-pong mechanism
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P251L
the sat mutation likely affects the dimer interface near the catalytic site, phenotype overview. The point mutation renders the sat mutant plants lethally stunted when grown in normal atmospheric conditions
A112D
-
less than 5% of the specific activity of the wild type enzyme
A280V
natural mutant from patient with primary hyperoxaluria type 1, 92% of normal enzyme activity
C173Y
-
less than 5% of the specific activity of the wild type enzyme
D183N
-
less than 5% of the specific activity of the wild type enzyme
DELTA 1-21
-
purified protein does not show bound PLP (affinity is about 80fold lower than wild type protein), catalytic activity about 1000fold lower than wild type protein, expressed in Escherichia coli in an insoluble form, peroxisomal localization, expressed in CHO cells the mutant protein forms large stable but catalytically inactive aggregates in the peroxisomes
F152A
the mutant shows decreased activity compared to the wild type enzyme
F238S
site-directed mutagenesis
F240S
site-directed mutagenesis
G156R
-
less than 5% of the specific activity of the wild type enzyme
G161C
-
5% of wild-type expression level, reduced catalytic activity
G161S
-
12% of wild-type expression level, reduced catalytic activity
G216R
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure, it also shows a strongly reduced catalytic efficiency
G42E
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure
G63R
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure
I244T
-
natural mutation in enzyme minor allele, 8-26% of the activity of major allele, in vitro
I279T
natural mutant from patient with primary hyperoxaluria type 1, 98% of normal enzyme activity
I340M
-
polymorphism associated with enzyme from minor allele, significantly higher Km-value than that for major allele, 90% of activity of enzyme from major allele
K209R
-
less than 5% of the specific activity of the wild type enzyme
P10L/P11L
-
Kcat value 56% of wild type protein, aggregation occuring at a slower rate than that of DELTA 1-21 protein
P11L/F152I/I340M
-
naturally occuring mutations, mistargeted to the mitochondria, forms dimers, catlytically active
P11L/G170R/I340M
-
naturally occuring mutations, creates a hidden N-terminal mitochondrial targeting sequence, the unmasking of which occurs in the hereditary calcium oxalate kidney stone disease primary hyperoxaluria type 1; this unmasking is due to the additional presence of a common disease-specific G170R mutation, forms dimers, catalytically active
P11L/G41R/I340M
-
naturally occuring mutations, mistargeted to the mitochondria, catalytically inactive, aggregates
P11L/I244T/I340M
-
naturally occuring mutations, mistargeted to the mitochondria, forms dimers, catlytically active
P11L/I340M/F152I
-
naturally occuring mutation, possibly mistargeting into mitochondrial matrix
P11L/I340M/G170R
-
naturally occuring mutations, pathogenic variant
P11L/I340M/G41R
-
naturally occuring mutation, predicted to be responsible for the depletion of immunoreactive enzyme protein and formation of intraperoxisomal aggregates
P11L/I56N
site-directed mutagenesis, the Ile56Asn mutation induces a structural defect mostly related to the apo-form of enzyme AGT. The effects are more pronounced when the substitution of Ile56 is combined with the Pro11Leu and, at higher degree, the Pro11Arg mutation
P11R
naturally occuring pathogenic mutation
P11R/I56N
site-directed mutagenesis, the Ile56Asn mutation induces a structural defect mostly related to the apo-form of enzyme AGT. The effects are more pronounced when the substitution of Ile56 is combined with the Pro11Leu and, at higher degree, the Pro11Arg mutation
R118A
site-directed mutagenesis
R118A/F238S/F240S
site-directed mutagenesis, the apo and the holo forms of the triple mutant R118A-Mi/F238S-Mi/F240S-Mi display a dimer-monomer equilibrium dissociation constant value at least about 260 and 31fold larger, respectively, than the corresponding ones of wild-type AGT-Mi. In the presence of cofactor pyridoxala 5'-phosphate (PLP), the apo-monomer of the triple mutant undergoes a biphasic process: the fast phase represents the formation of an inactive PLP-bound monomer, while the slow phase depicts the monomer-monomer association that parallels the regain of transaminase activity. The latter events occur with a rate constant of about 20 nM/min. In the absence of PLP, the apomonomer is also able to dimerize but with a rate constant value about 2700fold lower. Kinetics of dimerization of triple variant, overview
R36H
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure
S158L
-
natural mutation in enzyme major allele, no in vitro enzymic activity
W108R
-
less than 5% of the specific activity of the wild type enzyme
W251K
naturally occuring mutation, mutant protein localized in peroxisome and cytosol
F152I
-
natural mutation in enzyme minor allele, decreased activity
F152I
the mutation is associated with primary hyperoxaluria type 1 in combination with the minor AGT allele and shows decreased activity compared to the wild type enzyme
F152I
-
soluble, catalytically active
F52I
-
natural mutation in enzyme major allele, 13% of the activity of major allele
F52I
-
natural mutation in enzyme minor allele, 14% of the activity of minor allele
G161R
natural mutant from patient with primary hyperoxaluria type 1, 6.2% of normal enzyme activity
G161R
-
less than 5% of the specific activity of the wild type enzyme
G161R
-
4% of wild-type expression level, reduced catalytic activity
G170R
-
mutation associated with primary hyperoxaluria type I, no effect on affinity for pyridoxal 5-phosphate
G170R
-
42% of the specific activity of the wild type enzyme
G170R
-
mainly localized in mitochondria compared to the peroxisomal wild type enzyme
G170R
-
natural mutation in enzyme minor allele, 40-57% of the activity of major allele, in vitro
G170R
the mutant shows decrease in protein stability
G41R
-
mutation associated with primary hyperoxaluria type I, enhanced activity after re-folding
G41R
-
24% of the specific activity of the wild type enzyme
G41R
-
natural mutation in enzyme major allele, 46.5% of the activity of major allele
G41R
-
natural mutation in enzyme minor allele, 23.7% of the activity of minor allele
G41R
-
the mutation on the minor and major alleles causes hyperoxaluria type 1, the variant under physiological conditions forms insoluble inactive high-order aggregates through intermolecular electrostatic interactions, the mutation decreases resistance to thermal denaturation and inactivation
G41R
-
naturally occuring mutation, predicted to be responsible for the depletion of immunoreactive enzyme protein and formation of intraperoxisomal aggregates
G41R
the naturally occuring missense mutation causes AGT misfolding, which induces aggregation and proteolytic degradation. Enzyme inhibitor D-cycloserin significantly improves the glyoxylate detoxification ability of CHO-GO cells expressing the enzyme mutant G41R variant, because it increases cell viability upon glycolate treatment. These data confirm that the treatment increases the amount of intraperoxisomal functional AGT able to metabolize glyoxylate
G41V
-
mutation associated with primary hyperoxaluria type I, enhanced activity after re-folding
G41V
-
18% of the specific activity of the wild type enzyme
G41V
-
naturally occuring mutation
G41V
-
the mutation on the major alle causes hyperoxaluria type 1, the variant under physiological conditions forms insoluble inactive high-order aggregates through intermolecular electrostatic interactions, the mutation decreases resistance to thermal denaturation and inactivation
G82E
-
less than 5% of the specific activity of the wild type enzyme
G82E
natural enzyme variant. Significant reduction in affinty for pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate. Mutant displays an altered conformational state of the bound pyridoxal 5'-phosphate and a decrease in overall catlytic activity to 0.1% of wild-type
G82E
naturally occuring variant. Like the wild-type, the G82E variant is able to bind 2 mol pyridoxal 5'-phosphate/dimer, it exhibits a significant reduced affinity for pyridoxal 5'-phosphate and even more for pyridoxamine 5'-phosphate compared with wild-type, and an altered conformational state of the bound pyridoxal 5'-phosphate. Dramatic decrease of the overall catalytic activity (about 0.1% of that of normal alanine:glyoxylate aminotransferase), appears to be related to the inability to undergo an efficient transaldimination of the pyridoxal 5'-phosphate form of the enzyme with amino acids as well as an efficient conversion of AGT-pyridoxamine 5'-phosphate into AGT-pyridoxal 5'-phosphate
G82E
-
naturally occuring mutation, decreased catalytic activity
I56N
site-directed mutagenesis, the Ile56Asn mutation induces a structural defect mostly related to the apo-form of enzyme AGT. The effects are more pronounced when the substitution of Ile56 is combined with the Pro11Leu and, at higher degree, the Pro11Arg mutation
I56N
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure. The I56N mutation destabilizes the apo-WT-AGT quaternary structure, an effect possibly caused by the substitution of Ile56 to ASN interferes with interchain hydrophobic interactions between Ile56 and Leu18 and Ile20 of the other subunit
P11L
-
50% of activity of enzyme from major allele
P11L
-
one of the mutations of the minor allele
P11L
naturally occuring polymorphic mutation
P11L/I340M
-
minor allele, naturally occuring variant; mutant protein (minor allel) is about 95% peroxisomal and 5% mitochondrial; P11/I340 major allele is 100% peroxisomal, minor allele in both the holo and apo forms is more sensitive to thermal denaturation and to urea unfolding than major allele
P11L/I340M
-
naturally occuring mutations, encoded by the minor allele, up to 100% activity
P11L/I340M
-
naturally occuring mutations, minor allele
R233C
-
natural mutation in enzyme major allele, 14% of the activity of wild-type tmajor allele, in vitro
R233C
-
natural mutation in enzyme major allele, 21% of the activity of major allele
R233C
-
natural mutation in enzyme minor allele, below 5% of the activity of minor allele
R233C
-
natural mutation in enzyme minor allele, no in vitro enzymic activity
S187F
-
less than 5% of the specific activity of the wild type enzyme
S187F
mutation gives rise to a variant associated with primary hyperoxaluria type I. Mutation shows a 300- to 500fold decrease in both the rate constant of L-alanine half-transamination and the kcat of the overall transamination, a different pyridoxamine 5'-phosphate binding mode and affinity, and a different microenvironment of the external aldimine
S205P
-
less than 5% of the specific activity of the wild type enzyme
S205P
-
natural mutation in enzyme major allele, decreased activity
S218L
natural mutant from patient with primary hyperoxaluria type 1, 10% of normal enzyme activity
S218L
-
less than 5% of the specific activity of the wild type enzyme
V336D
-
natural mutation in enzyme major allele, 22.4% of the activity of major allele
V336D
-
natural mutation in enzyme minor allele, 5.2% of the activity of minor allele
additional information
analysis of additional mutations
additional information
-
analysis of additional mutations
additional information
-
expression of green fluorescent protein-tagged enzyme in HeLa cells. Identification of two sites of peroxisomal targeting sequences around amino acids 59-66 and 389-392. A truncated mutant missing the COOH-terminal amino acids, 1216 is not targeted into peroxisome. Deletion mutant lacking amino acids 221390 or amino acids 221389 are not targeted into peroxisome. Deltion mutants lacking 221388 or 221386 are targeted
additional information
-
human enzyme can substitute for function of yeast Agx1. Mutations associated with disease in humans show reduced growth in yeast, refecting reduced protein levels
additional information
after random mutagenesis the subcellular distribution of mutant proteins (GFP-fusion proteins) is analyzed
additional information
analysis of the effects of pathogenic interfacial mutations by combining bioinformatic predictions with molecular and cellular studies on selected variants (R36H, G42E, I56N, G63R, and G216R) in both their holo- (i.e. with bound PLP) and apo- (i.e. without bound PLP) form. All variants display structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure. Possible inverse correlation between the degree of destabilization/misfolding induced by a mutation and the extent of B6 responsiveness. More than 150 pathogenic mutations on the AGXT gene have been identified to date. Structure-function analysis of wild-type and mutant enzymes, overview
additional information
biochemical properties of Pro11 and Ile56 variants: secondary, tertiary, and quaternary structures, overview
additional information
molecular dynamics simulations of F152I-Mi and I244T-Mi variants associated with PH1 and implications in their pathogenicity
additional information
-
molecular dynamics simulations of F152I-Mi and I244T-Mi variants associated with PH1 and implications in their pathogenicity
additional information
siRNA enzyme knockdown in Huh-7 cells
additional information
enzyme knockout strain, 2% residual activity, no glycine auxotrophic phenotype. Glycine auxtrophy requires additional deletion of genes for threonine aldolase, and for mitochondrial and cytosolic serine hydroxymethyltransferase
additional information
-
enzyme knockout strain, 2% residual activity, no glycine auxotrophic phenotype. Glycine auxtrophy requires additional deletion of genes for threonine aldolase, and for mitochondrial and cytosolic serine hydroxymethyltransferase
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Homo sapiens (A2V838)
brenda
Caplin, B.; Wang, Z.; Slaviero, A.; Tomlinson, J.; Dowsett, L.; Delahaye, M.; Salama, A.; Salama, A.; Wheeler, D.C.; Leiper, J.
Alanine-glyoxylate aminotransferase-2 metabolizes endogenous methylarginines, regulates NO, and controls blood pressure
Arterioscler. Thromb. Vasc. Biol.
32
2892-2900
2012
Mus musculus (Q3UEG6)
brenda
Cellini, B.; Montioli, R.; Voltattorni, C.B.
Human liver peroxisomal alanine:glyoxylate aminotransferase: characterization of the two allelic forms and their pathogenic variants
Biochim. Biophys. Acta
1814
1577-1584
2011
Homo sapiens
brenda
Cellini, B.; Lorenzetto, A.; Montioli, R.; Oppici, E.; Voltattorni, C.B.
Human liver peroxisomal alanine:glyoxylate aminotransferase: Different stability under chemical stress of the major allele, the minor allele, and its pathogenic G170R variant
Biochimie
92
1801-1811
2010
Homo sapiens
brenda
Montioli, R.; Fargue, S.; Lewin, J.; Zamparelli, C.; Danpure, C.J.; Borri Voltattorni, C.; Cellini, B.
The N-terminal extension is essential for the formation of the active dimeric structure of liver peroxisomal alanine:glyoxylate aminotransferase
Int. J. Biochem. Cell Biol.
44
536-546
2012
Homo sapiens
brenda
Fargue, S.; Lewin, J.; Rumsby, G.; Danpure, C.J.
Four of the most common mutations in primary hyperoxaluria type 1 unmask the cryptic mitochondrial targeting sequence of alanine:glyoxylate aminotransferase encoded by the polymorphic minor allele
J. Biol. Chem.
288
2475-2484
2013
Homo sapiens
brenda
Bhadauria, V.; Banniza, S.; Vandenberg, A.; Selvaraj, G.; Wei, Y.
Alanine: Glyoxylate aminotransferase 1 is required for mobilization and utilization of triglycerides during infection process of the rice blast pathogen, Magnaporthe oryzae
Plant Signal. Behav.
7
1206-1208
2012
Pyricularia oryzae
brenda
Bhadauria, V.; Banniza, S.; Vandenberg, A.; Selvaraj, G.; Wei, Y.
Peroxisomal alanine: glyoxylate aminotransferase AGT1 is indispensable for appressorium function of the rice blast pathogen, Magnaporthe oryzae
PLoS ONE
7
e36266
2012
Pyricularia oryzae
brenda
Ichiyama, A.
Studies on a unique organelle localization of a liver enzyme, serine:pyruvate (or alanine:glyoxylate) aminotransferase
Proc. Jpn. Acad. Ser. B Phys. Biol. Sci.
87
274-286
2011
Homo sapiens
brenda
Oppici, E.; Roncador, A.; Montioli, R.; Bianconi, S.; Cellini, B.
Gly161 mutations associated with Primary Hyperoxaluria Type I induce the cytosolic aggregation and the intracellular degradation of the apo-form of alanine:glyoxylate aminotransferase
Biochim. Biophys. Acta
1832
2277-2288
2013
Homo sapiens
brenda
Fargue, S.; Knight, J.; Holmes, R.P.; Rumsby, G.; Danpure, C.J.
Effects of alanine:glyoxylate aminotransferase variants and pyridoxine sensitivity on oxalate metabolism in a cell-based cytotoxicity assay
Biochim. Biophys. Acta
1862
1055-1062
2016
Homo sapiens
brenda
Abe, M.; Ochi, S.; Mori, Y.; Yamazaki, K.; Ishimaru, T.; Yoshino, Y.; Fukuhara, R.; Tanimukai, S.; Matsuda, S.; Ueno, S.
Distribution of D-3-aminoisobutyrate-pyruvate aminotransferase in the rat brain
BMC Neurosci.
15
53
2014
Rattus norvegicus (Q64565)
brenda
Rodionov, R.N.; Martens-Lobenhoffer, J.; Brilloff, S.; Hohenstein, B.; Jarzebska, N.; Jabs, N.; Kittel, A.; Maas, R.; Weiss, N.; Bode-Bger, S.M.
Role of alanine:glyoxylate aminotransferase 2 in metabolism of asymmetric dimethylarginine in the settings of asymmetric dimethylarginine overload and bilateral nephrectomy
Nephrol. Dial. Transplant.
29
2035-2042
2014
Mus musculus
brenda
Oppici, E.; Fodor, K.; Paiardini, A.; Williams, C.; Voltattorni, C.B.; Wilmanns, M.; Cellini, B.
Crystal structure of the S187F variant of human liver alanine: glyoxylate [corrected] aminotransferase associated with primary hyperoxaluria type I and its functional implications
Proteins
81
1457-1465
2013
Homo sapiens (P21549)
brenda
Jarzebska, N.; Georgi, S.; Jabs, N.; Brilloff, S.; Maas, R.; Rodionov, R.N.; Zietz, C.; Montresor, S.; Hohenstein, B.; Weiss, N.
Kidney and liver are the main organs of expression of a key metabolic enzyme alanine glyoxylate aminotransferase 2 in humans
Atheroscler. Suppl.
40
106-112
2019
Homo sapiens (Q9BYV1), Homo sapiens
brenda
Dindo, M.; Grottelli, S.; Annunziato, G.; Giardina, G.; Pieroni, M.; Pampalone, G.; Faccini, A.; Cutruzzola, F.; Laurino, P.; Costantino, G.; Cellini, B.
Cycloserine enantiomers are reversible inhibitors of human alanine glyoxylate aminotransferase implications for primary hyperoxaluria type 1
Biochem. J.
476
3751-3768
2019
Homo sapiens (P21549)
brenda
Dindo, M.; Montioli, R.; Busato, M.; Giorgetti, A.; Cellini, B.; Borri Voltattorni, C.
Effects of interface mutations on the dimerization of alanine glyoxylate aminotransferase and implications in the mistargeting of the pathogenic variants F152I and I244T
Biochimie
131
137-148
2016
Homo sapiens (P21549), Homo sapiens
brenda
Han, Q.; Yang, C.; Lu, J.; Zhang, Y.; Li, J.
Metabolism of oxalate in humans a potential role kynurenine aminotransferase/glutamine transaminase/cysteine conjugate beta-lyase plays in hyperoxaluria
Curr. Med. Chem.
26
4944-4963
2019
Mus musculus (Q3UEG6), Homo sapiens (Q9BYV1)
brenda
Liepman, A.H.; Vijayalakshmi, J.; Peisach, D.; Hulsebus, B.; Olsen, L.J.; Saper, M.A.
Crystal structure Of photorespiratory alanine glyoxylate aminotransferase 1 (AGT1) from Arabidopsis thaliana
Front. Plant Sci.
10
1229
2019
Arabidopsis thaliana (Q56YA5), Arabidopsis thaliana
brenda
Dindo, M.; Oppici, E.; DellOrco, D.; Montone, R.; Cellini, B.
Correlation between the molecular effects of mutations at the dimer interface of alanine-glyoxylate aminotransferase leading to primary hyperoxaluria type I and the cellular response to vitamin B6
J. Inherit. Metab. Dis.
41
263-275
2018
Homo sapiens (P21549)
brenda
Sun, Y.; Li, W.; Shen, S.; Yang, X.; Lu, B.; Zhang, X.; Lu, P.; Shen, Y.; Ji, J.
Loss of alanine-glyoxylate and serine-pyruvate aminotransferase expression accelerated the progression of hepatocellular carcinoma and predicted poor prognosis
J. Transl. Med.
17
390
2019
Homo sapiens (P21549)
brenda
Dindo, M.; Mandrile, G.; Conter, C.; Montone, R.; Giachino, D.; Pelle, A.; Costantini, C.; Cellini, B.
The ILE56 mutation on different genetic backgrounds of alanine glyoxylate aminotransferase clinical features and biochemical characterization
Mol. Genet. Metab.
131
171-180
2020
Homo sapiens (P21549)
-
brenda
Parthasarathy, A.; Adams, L.E.; Savka, F.C.; Hudson, A.O.
The Arabidopsis thaliana gene annotated by the locus tag At3g08860 encodes alanine aminotransferase
Plant Direct
3
e00171
2019
Arabidopsis thaliana (Q9SR86), Arabidopsis thaliana, Arabidopsis thaliana Col7 (Q9SR86)
brenda