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Information on EC 2.6.1.44 - alanine-glyoxylate transaminase
for references in articles please use BRENDA:EC2.6.1.44
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EC Tree 2 Transferases
2.6 Transferring nitrogenous groups
2.6.1 Transaminases
2.6.1.44 alanine-glyoxylate transaminase
IUBMB Comments
A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine—pyruvate transaminase.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 2.6.1.44
- hyperoxaluria
- peroxisomal
-
end-stage
- oxalosis
- nephrocalcinosis
-
transamination
- dimethylarginine
- stone
- urolithiasis
-
mistargeting
- pyridoxine
- nephrolithiasis
- medicine
-
liver-kidney
- hydroxypyruvate
- grhpr
- analysis
- diagnostics
- nutrition
showSynonyms
agxt2, alanine-glyoxylate aminotransferase, alanine glyoxylate aminotransferase, spt/agt, alanine-glyoxylate aminotransferase 2, alanine:glyoxylate aminotransferase 1, agt-mi, alanine:2-oxoglutarate aminotransferase, serine pyruvate aminotransferase, cytosolic alanine aminotransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AGT
AGT1
AGT2
AGXT
AGXT2
alanine glyoxalate transaminase 2
alanine glyoxylate aminotransferase
alanine-glyoxylate aminotransferase
alanine-glyoxylic aminotransferase
-
-
-
-
alanine:glyoxylate aminotransferase
alanine:glyoxylate aminotransferase 1
alanine:glyoxylate aminotransferase/beta-alanine:pyruvate aminotransferase
-
aminotransferase 3
AT3
At3g08860
EC 2.6.1.51
-
serine-pyruvate aminotransferase identical with liver isoenzyme 1
L-alanine-glycine transaminase
-
-
-
-
L-alanine-glyoxylate aminotransferase
-
-
-
-
serine:pyruvate/alanine:glyoxylate aminotransferase
additional information
AGT
-
-
-
-
alanine-glyoxylate aminotransferase
-
-
-
-
alanine:glyoxylate aminotransferase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-alanine + glyoxylate = pyruvate + glycine
A pyridoxal-phosphate protein
-
-
-
L-alanine + glyoxylate = pyruvate + glycine
A pyridoxal-phosphate protein.
-
-
-
L-alanine + glyoxylate = pyruvate + glycine
a pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine -pyruvate transaminase
-
-
-
L-alanine + glyoxylate = pyruvate + glycine
pyridoxamine 5'-phosphate remains bound to the enzyme during the catalytic cycle. The enzyme-pyridoxamine 5'-phosphate complex displays a reactivity towards oxo acids higher than that of the apo-enzyme in presence of pyridoxamine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
glycine biosynthesis III
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SYSTEMATIC NAME
IUBMB Comments
L-alanine:glyoxylate aminotransferase
A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine---pyruvate transaminase.
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CAS REGISTRY NUMBER
COMMENTARY
9015-67-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxykynurenine + glyoxylate
xanthurenic acid + glycine
Substrates: -
Products: -
Products: -
?
kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + 2-oxobutyrate
pyruvate + 2-aminobutanoate
-
Substrates: -
Products: -
Products: -
ir
L-alanine + 3-hydroxypyruvate
pyruvate + L-serine
Substrates: -
Products: -
Products: -
?
L-alanine + 4-methylthio-2-oxobutyrate
pyruvate + L-methionine
-
Substrates: poor amino acceptor
Products: -
Products: -
ir
L-aspartate + glyoxylate
2-oxosuccinate + glycine
-
Substrates: -
Products: -
Products: -
ir
L-glutamine + pyruvate
2-oxoglutaramate + L-alanine
-
Substrates: -
Products: -
Products: -
ir
L-histidine + pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
Substrates: -
Products: -
Products: -
ir
L-isoleucine + glyoxylate
3-methyl-2-oxopropanoate + glycine
-
Substrates: isoenzyme 1
Products: -
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L-tyrosine + pyruvate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-alanine
Substrates: -
Products: -
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L-valine + glyoxylate
3-methyl-2-oxobutanoate + glycine
-
Substrates: isoenzyme 1
Products: -
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Nomega,Nomega-dimethyl-L-arginine + pyruvate
5-(N,N-dimethylcarbamidamido)-2-oxopentanoate + alanine
Substrates: -
Products: -
Products: -
?
glycine + pyruvate
glyoxylate + L-alanine
Substrates: -
Products: -
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L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
-
Substrates: -
Products: -
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L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
Substrates: -
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L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
-
Substrates: -
Products: -
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L-alanine + glyoxylate
glycine + pyruvate
Substrates: transamination half-reaction kinetic parameters
Products: -
Products: -
r
L-alanine + glyoxylate
glycine + pyruvate
-
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
ir
L-alanine + glyoxylate
pyruvate + glycine
Substrates: photorespiratory enzyme
Products: -
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ir
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
r, ?
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: -
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ir
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
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L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: -
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L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: key role in the transamination/detoxification of glyoxylate
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L-alanine + glyoxylate
pyruvate + glycine
Substrates: the enzyme is highly specific for catalysing glyoxylate to glycine processing, thereby playing a key role in glyoxylate detoxification
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Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: the enzyme is highly specific for catalysing glyoxylate to glycine processing
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Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: high substrate specificity for Ala and glyoxylate
Products: -
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L-alanine + glyoxylate
pyruvate + glycine
Hydrogenobacter thermophilus TK-6 / IAM 12695
Substrates: high substrate specificity for Ala and glyoxylate
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L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: isoenzyme 1
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ir
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: isoenzyme 2 highly specific, little or no activity with other amino donors/acceptors
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L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: isoenzyme 1
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ir
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: isoenzyme 2 highly specific, little or no activity with other amino donors/acceptors
Products: -
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ir
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: -
Products: -
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ir
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates
Products: -
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L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: -
Products: -
Products: -
?
L-alanine + hydroxypyruvate
pyruvate + L-serine
-
Substrates: -
Products: -
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L-alanine + hydroxypyruvate
pyruvate + L-serine
-
Substrates: isoenzyme 1
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L-alanine + hydroxypyruvate
pyruvate + L-serine
-
Substrates: isoenzyme 1
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L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
-
Substrates: isoenzyme 1, less effectively acceptor
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L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
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Substrates: isoenzyme 1, less effectively acceptor
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L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
-
Substrates: isoenzyme 1
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ir
L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
-
Substrates: isoenzyme 1
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ir
L-alanine + pyruvate
pyruvate + L-alanine
Substrates: -
Products: -
Products: -
?
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
-
Substrates: -
Products: -
Products: -
ir
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
Substrates: -
Products: -
Products: -
ir
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
Substrates: -
Products: -
Products: -
?
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
Substrates: -
Products: -
Products: -
?
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
-
Substrates: isoenzyme 1
Products: -
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ir
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
-
Substrates: -
Products: -
Products: -
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
Substrates: -
Products: -
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L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
Substrates: -
Products: 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
Products: 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
Substrates: -
Products: -
Products: -
?
L-glutamate + glyoxylate
2-oxoglutarate + glycine
Substrates: -
Products: -
Products: -
?
L-glutamate + glyoxylate
2-oxoglutarate + glycine
-
Substrates: -
Products: -
Products: -
ir
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
-
Substrates: -
Products: -
Products: -
ir
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
-
Substrates: -
Products: -
Products: -
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
Substrates: -
Products: -
Products: -
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-leucine + glyoxylate
4-methyl-2-oxopentanoate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-leucine + glyoxylate
4-methyl-2-oxopentanoate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
-
Substrates: -
Products: -
Products: -
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
Substrates: -
Products: -
Products: -
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
-
Substrates: -
Products: -
Products: -
ir
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
Substrates: -
Products: -
Products: -
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
-
Substrates: -
Products: -
Products: -
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L-phenylalanine + glyoxylate
phenylpyruvate + glycine
Substrates: -
Products: -
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L-phenylalanine + glyoxylate
phenylpyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
-
Substrates: isoenzyme 1
Products: -
Products: -
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
-
Substrates: isoenzyme 1
Products: -
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L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
-
Substrates: -
Products: -
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L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
Substrates: -
Products: -
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L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
Substrates: -
Products: -
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L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
Substrates: -
Products: -
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L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
Substrates: -
Products: -
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ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
Substrates: -
Products: -
Products: -
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
Substrates: -
Products: -
Products: -
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
Substrates: -
Products: -
Products: -
?
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
Substrates: isoenzyme 1
Products: -
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ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
Substrates: -
Products: -
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L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
Substrates: isoenzyme 1
Products: -
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L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
-
Substrates: -
Products: -
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L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
Substrates: -
Products: -
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L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
Substrates: -
Products: -
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L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
Substrates: isoenzyme 1
Products: -
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ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
Substrates: -
Products: -
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L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
Substrates: isoenzyme 1
Products: -
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L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
Substrates: isoenzyme 1
Products: -
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L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
Substrates: isoenzyme 1
Products: -
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L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
-
Substrates: -
Products: -
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L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
-
Substrates: -
Products: -
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L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
Substrates: -
Products: -
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L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
-
Substrates: -
Products: -
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L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
Substrates: -
Products: -
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L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
Substrates: -
Products: -
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L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
-
Substrates: isoenzyme 1
Products: -
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L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
-
Substrates: isoenzyme 1
Products: -
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ir
additional information
?
-
-
Substrates: aminoadipate, asparagine, aspartate, glutamate, isoleucine, lysine, threonine and valine are no substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzymatic activity is not detected using beta-alanine as the amino donor with either pyruvate or glyoxylate as amino acceptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzymatic activity is not detected using beta-alanine as the amino donor with either pyruvate or glyoxylate as amino acceptors
Products: -
Products: -
?
additional information
?
-
Arabidopsis thaliana Col7
Substrates: enzymatic activity is not detected using beta-alanine as the amino donor with either pyruvate or glyoxylate as amino acceptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: aminoadipate, asparagine, aspartate, glutamate, isoleucine, lysine, threonine and valine are no substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: aminoadipate, asparagine, aspartate, glutamate, isoleucine, lysine, threonine and valine are no substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: mitochondrially localized human AGXT2 is able to effectively metabolize asymmetric dimethylarginine in vivo
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is also active as serine-pyruvate aminotransferase, EC 2.6.1.51
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: strict specificity for L-alanine and glyoxylate as substrates
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-alanine + 3-hydroxypyruvate
pyruvate + L-serine
Substrates: -
Products: -
Products: -
?
L-alanine + pyruvate
pyruvate + L-alanine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: photorespiratory enzyme
Products: -
Products: -
ir
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
r, ?
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: -
Products: -
Products: -
ir
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
ir
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: -
Products: -
Products: -
ir
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: key role in the transamination/detoxification of glyoxylate
Products: -
Products: -
ir
L-alanine + glyoxylate
pyruvate + glycine
Substrates: the enzyme is highly specific for catalysing glyoxylate to glycine processing, thereby playing a key role in glyoxylate detoxification
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
Substrates: -
Products: -
Products: -
?
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: -
Products: -
Products: -
ir
L-alanine + glyoxylate
pyruvate + glycine
-
Substrates: regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates
Products: -
Products: -
ir
additional information
?
-
-
Substrates: enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
activated by heat treatment with pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
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
pyridoxal 5'-phosphate
-
for some mutants, sensitivity to trypsin can be ameliorated by addition of pyridoxal 5'-phosphate or aminooxyacetic acid
pyridoxal 5'-phosphate
PLP, is bound at the active site but is not held in place by covalent interactions
pyridoxal 5'-phosphate
binding analysis with monomeric and dimeric enzyme, overview
pyridoxal 5'-phosphate
cofactor binding and kinetics of wild-type and mutant enzymes, overview. Stabilizing effect of PLP binding is mediated by the loop Gly252-Val266, which faces the active site and could be maintained by the coenzyme in the correct conformation. Pyridoxal 5'-phosphate (PLP) exerts a chaperone role by promoting dimerization
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-alanine
competitive inhibitor with L-alanine as varied substrate and glyoxylate as fixed substrate. Uncompetitive inhibitor with glyoxylate as varied substrate and L-alanine as fixed substrate; competitive with L-alanine, uncompetitive with glyoxylate
D-cycloserine
DCS, commercialized as Seromycin, a reversible inhibitor of AGT. DCS displays a time-dependent binding mainly generating an oxime intermediate, inhibition mechanism, overview
L-Cycloserine
LCS, a reversible inhibitor of AGT. LCS undergoes half-transamination generating a ketimine intermediate and behaves as a classical competitive inhibitor, inhibition mechanism, overview
pyruvate
mixed type inhibition with L-alanine, competitive with glyoxylate; mixed type inhibitor with L-alanine as varied substrate and glyoxylate as fixed substrate. Competitive inhibitor with glyoxylate as varied substrate and L-alanine as fixed substrate
additional information
the cycloserine enantiomers are reversible inhibitors of human alanine:glyoxylate aminotransferase. DCS, but not LCS, is able to promote the correct folding of the G41R variant, as revealed by its increased specific activity and expression as a soluble protein. This effect also translates into an increased glyoxylate detoxification ability of cells expressing the variant upon treatment with DCS. DCS might play a role as pharmacological chaperone. Inhibitor docking study and mass spectrometric analysis, identification of the wild-type and mutant AGT-cycloserine reaction products. Inhibitor effects on recombinant wild-type AGT and the G41R variant in CHO-GO cells, that overexpress glycolate oxidase, overview. Cell survival of CHO-GO-AGT-wild-type cells is much higher than that of CHO-GO-AGT-G41R mutant cells
-
additional information
-
not inhibitory: 10 mM EDTA, 10 mM p-chloromercuribenzoate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aminooxyacetic acid
-
for some enzyme mutants, sensitivity to trypsin can be ameliorated by addition of pyridoxal 5'-phosphate or aminooxyacetic acid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.13
glyoxylate
-
G41V, pH not specified in the publication, temperature not specified in the publication
0.15
glyoxylate
-
G82E, pH not specified in the publication, temperature not specified in the publication
0.22
glyoxylate
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
0.23
glyoxylate
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
0.25
glyoxylate
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
0.28
glyoxylate
-
F152I, pH not specified in the publication, temperature not specified in the publication
0.32
glyoxylate
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
0.41
glyoxylate
-
G41R, pH not specified in the publication, temperature not specified in the publication
0.24
L-alanine
-
pH 7.5, 37°C, mitochondrial isozyme, glyoxylate as amino acceptor
1.11
L-alanine
-
pH 7.5, 37°C, cytosolic isozyme, glyoxylate as amino acceptor
2.6
L-alanine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
3.9
L-alanine
-
pH 8.2, 37°C, isoenzyme 1, glyoxylate as amino acceptor
15
L-alanine
-
G82E, pH not specified in the publication, temperature not specified in the publication
22
L-alanine
-
G41R, pH not specified in the publication, temperature not specified in the publication
28
L-alanine
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
30
L-alanine
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
31
L-alanine
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
34
L-alanine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
37
L-alanine
-
F152I, pH not specified in the publication, temperature not specified in the publication
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
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
additional information
additional information
steady-state Michaelis-Menten kinetics
-
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.068
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
18.3
glyoxylate
-
G41V, pH not specified in the publication, temperature not specified in the publication
20.5
glyoxylate
-
G41R, pH not specified in the publication, temperature not specified in the publication
37
glyoxylate
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
39
glyoxylate
-
F152I, pH not specified in the publication, temperature not specified in the publication
40
glyoxylate
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
45
glyoxylate
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
0.07
L-alanine
-
G82E, pH not specified in the publication, temperature not specified in the publication
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
19.8
L-alanine
-
G41R, pH not specified in the publication, temperature not specified in the publication
33
L-alanine
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
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
-
F152I, pH not specified in the publication, temperature not specified in the publication
45
L-alanine
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
117
L-alanine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
glyoxylate
-
G82E, pH not specified in the publication, temperature not specified in the publication
35
glyoxylate
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
50
glyoxylate
-
G41R, pH not specified in the publication, temperature not specified in the publication
139
glyoxylate
-
F152I, pH not specified in the publication, temperature not specified in the publication
143
glyoxylate
-
G41V, pH not specified in the publication, temperature not specified in the publication
160
glyoxylate
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
168
glyoxylate
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
196
glyoxylate
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
0.005
L-alanine
-
G82E, pH not specified in the publication, temperature not specified in the publication
0.35
L-alanine
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
0.41
L-alanine
-
G41V, pH not specified in the publication, temperature not specified in the publication
0.82
L-alanine
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
0.9
L-alanine
-
G41R, pH not specified in the publication, temperature not specified in the publication
0.95
L-alanine
-
F152I, pH not specified in the publication, temperature not specified in the publication
1.2
L-alanine
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
1.4
L-alanine
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14.3
D-alanine
with L-alanine as varied substrate and glyoxylate as fixed substrate, Kis
28.7
D-alanine
with glyoxylate as varied substrate and L-alanine as fixed substrate, Kii
2.3
pyruvate
glyoxylate as varied substrate and L-alanine as fixed substrate
15.8
pyruvate
with L-alanine as varied substrate and glyoxylate as fixed substrate, Kis
22.8
pyruvate
with L-alanine as varied substrate and glyoxylate as fixed substrate, Kii
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160
2.93
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
7.4
8.3 - 8.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
additional information
-
activity increases with temperature from 37°C to 90°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
isoelectric focusing of the crude extract on a pH 3.0-10 pharmalyte gradient, 3 activity peaks with pI 7.4, 7.8 and 8.3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
common chimpanzee, sequence of 5' region of the AGT gene
SwissProt
brenda
human
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
distributed throughout the brain, with high expression in the retrosplenial cortex and in hippocampal neurons
brenda
distributed throughout the brain, with high expression in the retrosplenial cortex and in hippocampal neurons
brenda
additional information
convoluted tubule, strong AGXT2 expression is detected in proximal tubular epithelial cells
brenda
-
-
brenda
diffuse AGXT2 expression in hepatocytes, but no significant AGXT2 expression in the hepatic vasculature
brenda
additional information
enzyme differential quantitative expression analysis in liver and hepatocellular carcinoma (data from 327 livers and 385 HCC tissues), overview
brenda
additional information
AGXT2 RT-PCR expression analysis and immunohistochemic analysis in human tissues, expression of key metabolic enzyme alanine:glyoxylate aminotransferase 2 in humans mainly in kidney and liver. The other tissues do not show any detectable AGXT2 mRNA
brenda
additional information
-
AGXT2 RT-PCR expression analysis and immunohistochemic analysis in human tissues, expression of key metabolic enzyme alanine:glyoxylate aminotransferase 2 in humans mainly in kidney and liver. The other tissues do not show any detectable AGXT2 mRNA
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
the first 93 nucleotides of the full-length cDNA are predicted to encode the signal sequence that denote localization to the mitochondria
brenda
Arabidopsis thaliana Col7
-
the first 93 nucleotides of the full-length cDNA are predicted to encode the signal sequence that denote localization to the mitochondria
-
brenda
-
apoenzyme in the peroxisomes, holoenzyme in the mitochondrion
brenda
the C-terminal tripeptide Ser-Arg-Ile (residues 399-401) constitute a type 1 peroxisomal targeting sequence (PTS1)
brenda
-
apoenzyme in the peroxisomes, holoenzyme in the mitochondrion
brenda
-
-
brenda
-
sequence contains two sites of peroxisomal targeting sequences around amino acids 59-66 and 389-392
brenda
AGT is synthetized and folded in the cell cytosol before being imported into peroxisomes via the interaction with the Pex5p carrier
brenda
-
apoenzyme in the peroxisomes, holoenzyme in the mitochondrion
brenda
Uroloncha striata domestica
-
apoenzyme in the peroxisomes, holoenzyme in the mitochondrion
brenda
additional information
AGXT2 RT-PCR expression analysis and immunohistochemic analysis in human tissues
-
brenda
additional information
-
AGXT2 RT-PCR expression analysis and immunohistochemic analysis in human tissues
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
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
physiological function
additional information
evolution
AGT is homodimeric and belongs to the fold type I family of PLP-dependent enzymes
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
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
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
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
Arabidopsis thaliana Col7
-
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
-
malfunction
alanine:glyoxylate aminotransferase deficiency causes primary hyperoxaluria type 1
malfunction
-
The hereditary kidney stone disease primary hyperoxaluria type 1 is caused by a deficiency of the peroxisomal enzyme alanine:glyoxylate aminotransferase
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
-
deficiency is responsible for Primary Hyperoxaluria Type 1, an autosomal recessive disorder
malfunction
-
causes the hereditary kidney stone disease primary hyperoxaluria type 1
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 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
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
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
-
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
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
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
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
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
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
the enzyme produces beta-alanine, which is an osmoprotectant in plants
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
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
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
the overall transamination catalyzed by AGT follows a ping-pong mechanism
additional information
structural analysis and homology modeling of the At3g08860-encoded enzyme
additional information
-
structural analysis and homology modeling of the At3g08860-encoded enzyme
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
170000
175000
200000
220000
38000
43000
45000
50000
77000
80000
90000
80000
-
peroxisomal and mitochondrial alanine-glyoxylate aminotransferase 1
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information
dimer
crystal structure, enzyme in solution, catalytic enzyme form
homodimer
structure modeling with monomer-monomer interface and active site, overview
tetramer
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
additional information
-
the two allelic forms consist of a wild-type major allele, AGTma, and a minor allele, AGTmi. Wild-type minor allele displays about 46-50% of the activity of the major allele
additional information
-
analysis of wild-type and mutants after partial digestions using trypsin. Partial digestion by trypsin provides an indicator of proper folding of the enzyme, while for some mutants, sensitivity to trypsin can be ameliorated by addition of pyridoxal 5'-phosphate or aminooxyacetic acid
additional information
Arg118, Phe238 and Phe240 are interfacial residues not essential for transaminase activity but important for dimer-monomer dissociation. AGT dimer interface model, overview. A synergic role of the residues Arg118 and Phe240 exist on the formation of the dimer of AGT-Mi, and substitution of both Phe238 and Phe240 with Ser might be relevant in preventing monomer-monomer aggregation. Proposed folding and dimerization pathway of wild-type AGT-Mi and of mutant I244T-Mi and F152T-Mi variant, overviews
additional information
-
Arg118, Phe238 and Phe240 are interfacial residues not essential for transaminase activity but important for dimer-monomer dissociation. AGT dimer interface model, overview. A synergic role of the residues Arg118 and Phe240 exist on the formation of the dimer of AGT-Mi, and substitution of both Phe238 and Phe240 with Ser might be relevant in preventing monomer-monomer aggregation. Proposed folding and dimerization pathway of wild-type AGT-Mi and of mutant I244T-Mi and F152T-Mi variant, overviews
additional information
dimerization is considered a crucial event, because it is supposed to influence the overall stability of the protein as well as its intracellular fate, including, in particular, the correct peroxisomal localization. Rigid-body protein-protein docking simulations aiming at predicting and analyzing the quaternary structure of proteins using the structure of dimeric AGT in complex with the tetratricopeptide repeat (TPR) domain of human Pex5p (PDB ID 3R9A), overview
additional information
biochemical properties of Pro11 and Ile56 variants: secondary, tertiary, and quaternary structures, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 12% polyethylene glycol 8000, 0.13 M magnesium acetate, 4% butanol, and 0.1 M cacodylic acid at pH 6.5
-
enzyme in apoform and complexed with L-serine, large, greenish-yellow crystals grow from drops containing equal volumes of 11 mg/ml protein in 0.2 mM PLP, 10% glycerol, and 100 mM Tris-HCl, pH 8.5, and precipitant solution containing 4.1-4.2 M sodium formate, equilibration against the same precipitant, several days, at room temperature, X-ray diffraction structure determination and analysis at 2.2 A and 2.1 A resolution, respectively, modelling
crystals belong to space group P4(1)2(1)2 or its enantiomorph with uni-cell parameters a = b = 90.81, c = 142.62 A
-
mutant S187F, to a resolution of 2.9 A. The overall conformation of the variant is similar to that of normal AGTwith a displacement of the PLP-binding Lys209 and Val185, located on the re and si side of PLP, respectively, and slight conformational changes of other active site residues, in particular Trp108, the base stacking residue with the pyridine cofactor moiety. This results in a mispositioning of the AGT-pyridoxamine 5'-phosphate complex and of the external aldimine
purified recombinant wild-type enzyme in complex with inhibitors L- and D-cycloserine (LCS and DCS), hanging drop vapor diffusion technique, mixing of 0.001 ml of protein/ligand solution containing 0.215 mM enzyme, 2 mM DCS, and 50 mM potassium phosphate, pH 7.4, with an equal volume of reservoir solution containing 10-12% PEG 6000, 5% 2-methyl-2,4-pentanediol (MPD), and 0.1 M MES, pH 6.5, single crystals are cryoprotected by fast soaking into a reservoir solution containing 2 mM DCS and 25% MPD, for the AGT-LCS complex, AGT native crystals grown in the described conditions, with the exception of DCS, are soaked into a solution containing the reservoir and 20 mM LCS and 20% MPD, X-ray diffraction structure determination and analysis at 2.7-3.0 A resolution, modelling
crystallization of the native and selenomethionyl alanine:glyoxylate aminotransferase is performed using the hanging-drop vapour-diffusion method. Crystal struture is determined at 2.3 A resolution
crystallization of the native and selenomethionyl enzyme is performed using the hanging-drop vapour-diffusion method. Crystal structure is determined at 2.3 A resolution
native enzyme and selenomethionine derivative, to 2.3 A and 2.55 A resolution, respectively. Enzyme is a tetramer. The monomer consists of an N-terminal arm of residues 117, a small domain from residues 1847 and 295405 and a large domain of residues 48294. The amino-acid residues involved in cofactor binding are Asn175, Tyr206, Lys234 and Arg242. The guanidino group of Arg361 forms a salt bridge with one carboxylate of the maleate, Thr108 forms a salt bridge with the side-chain carboxylate of the maleate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
A280V
natural mutant from patient with primary hyperoxaluria type 1, 92% of normal enzyme activity
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
F152I
F52I
G161R
G170R
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
G41R
G41V
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
G82E
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
I56N
P10L/P11L
-
Kcat value 56% of wild type protein, aggregation occuring at a slower rate than that of DELTA 1-21 protein
P11L
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
P11L/I340M/F152I
-
naturally occuring mutation, possibly mistargeting into mitochondrial matrix
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/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/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
R233C
R36H
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure
S187F
S205P
S218L
V336D
W251K
naturally occuring mutation, mutant protein localized in peroxisome and cytosol
additional information
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
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
G170R
-
mutation associated with primary hyperoxaluria type I, no effect on affinity for pyridoxal 5-phosphate
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
G41R
-
mutation associated with primary hyperoxaluria type I, enhanced activity after re-folding
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
-
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
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
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
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
P11L/I340M
-
naturally occuring mutations, encoded by the minor allele, up to 100% activity
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
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
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
S218L
natural mutant from patient with primary hyperoxaluria type 1, 10% of normal enzyme activity
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
-
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
-
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
after random mutagenesis the subcellular distribution of mutant proteins (GFP-fusion proteins) is analyzed
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
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
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
human AGT can substitute for function of yeast Agx1 (Yeast alanine:glyoxylate aminotransferase) and that mutations associated with disease in humans show reduced growth in yeast. The reduced growth of minor allele mutants reflects reduced protein levels, indicating that these proteins are less stable than wild-type AGT in yeast
-
major allele (P11/I340) is more stable against increasing urea concentrations than minor allele (P11L/I340M) or mutant protein P11L/I340M/G170R
-
partial digestion by trypsin provides an indicator of proper folding of the enzyme, while for some mutants, sensitivity to trypsin can be ameliorated by addition of pyridoxal 5'-phosphate or aminooxyacetic acid
-
partial trypsin digestion provides an indicator of proper folding of the mutant enzyme. For selected mutations the sensitivity to trypsin can be ameliorated by addition of pyridoxal phosphate or aminooxy acetic acid as specific pharmacological chaperones
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
is inhibited by hypoxia, resulting in a very low amount of glycine in hypoxic seedlings
-
675140
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM-potassium phosphate buffer, pH 7.5, containing 100 mM NaCl, 0.1 mM pyridoxal 5'-phosphate and 10% glycerol, my be stored for at least 3 months without loss of activity
-
-20°C, 50 mM potassium phosphate buffer, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 4 weeks without loss of either activity
-
-20C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 4 weeks without loss of either activity
-20°C, crude homogenate can be stored for 6-12 months with little loss of activity
-
-20°C, peroxisomal apoenzyme, may be stored for at least 4 weeks without loss of activity
-
-20°C, peroxisomal holoenzyme, may be stored for at least 4 weeks without loss of activity
-
-20°C, purified enzyme, 50% glycerol, can be stored for at least 3 months with little loss in activity
-
-20°C, purified enzyme, freezing results in formation of floculence and complete loss of activity
-
0-6C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 2 weeks with little loss of either activity
-20C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 4 weeks without loss of either activity
-
-20C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 4 weeks without loss of either activity
-
-20C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 4 weeks without loss of either activity
-
0-6C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 2 weeks with little loss of either activity
-
0-6C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 2 weeks with little loss of either activity
-
0-6C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 2 weeks with little loss of either activity
-
0-6C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 2 weeks with little loss of either activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
butyl-Toyopearl column chromatography, DEAE-Toyopearl column chromatography, hydroxyapatite column chromatography, MonoQ column chromatography, and phenyl Superose gel filtration
DEAE-Sepharose chromatography, phenyl-Sepharose chromatography, hydroxyapatite chromatography, and gel filtration
isoenzyme 1
isoenzyme 1 and 2
partially
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AGXT cDNA cloned, AGXT*LTM expressed as a GST-fusion protein in Escherichia coli BL21(RIL) and in Sf9 cells
-
expressed in COS-7 cells and human umbilical vein endothelial cells with a C-terminal FLAG epitope tag
-
expressed in Escherichia coli BL21-CodonPlus-RIPL mutants auxotrophic for the amino acids L-alanine and beta-alanine
expression in Escherichia coli
expression of of untagged alanine-glyoxylate aminotransferase in Escherichia coli
-
expression vectors of the enhanced green fluorescent protein-tagged alanine:glyoxylate aminotransferase and deletion mutants are introduced into HeLa cells to identify the peroxisomal targeting signal of the alanine:glyoxylate aminotransferase
-
for sequence determination, GFP-fusion proteins used in localization experiments
gene AGT, recombinant expression of wild-type and mutant G41R enzymes in Escherichia coli strain BL21, recombinant expression of wild-type AGT and the G41R variant in CHO-GO cells, that overexpress glycolate oxidase
gene AGXT, quantitative real-time reverse transcription-PCR enzyme expression analysis
gene AGXT, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
gene AGXT, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
His-tagged protein expressed in Escherichia coli JM109, expressed in CHO cells
-
human AGT can substitute for function of yeast Agx1 (yeast alanine:glyoxylate aminotransferase) and that mutations associated with disease in humans show reduced growth in yeast. The reduced growth of minor allele mutants reflects reduced protein levels, indicating that these proteins are less stable than wild-type AGT in yeast
-
locus At3g08860, DNA and amino acid sequence determination, analysis, and comparisons, recombinant expression of the enzyme lacking the N-terminal signal sequence and functional complementation of two Escherichia coli mutants (panD and HYE032) auxotrophic for the amino acids, L-alanine (proteinogenic) and beta-alanine (non-proteinogenic). The enzyme is not able to complement the Escherichia coli mutant DL39, that harbors a mutation in the tyrosine aminotransferase (tyrB) gene which leads to auxotrophy for L-tyrosine and L-phenylalanine. Recombinant expression of His-tagged enzyme in Escherichia coli
mitochondrial and peroxisomal isozymes generated from a single gene by alternative transcription initiation, cloned and expressed in Escherichia coli DH5 and ER1458
-
sequencing of the 5' region of the AGT gene
used in complementation experiments, AGT1-eGFP fusion protein used in localization experiments
-
used in knockout experiments
wild-type and G82E mutant His-tagged enzyme expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is specifically upregulated in response to osmotic stress, but not other stresses (beta-alanine is an osmoprotectant in plants)
the enzyme is specifically upregulated in response to osmotic stress, but not other stresses (beta-alanine is an osmoprotectant in plants)
the enzyme is specifically upregulated in response to osmotic stress, but not other stresses (beta-alanine is an osmoprotectant in plants)
Arabidopsis thaliana Col7
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation of enzyme with guanidine-HCl and re-folding, complete renaturation. Mutations G41V and G41R, associated with primary hyperoxaluria type I, show enhanced activity after re-folding. Pyridoxal 5-phosphate is not required for proper re-folding
-
quick dilution (100fold) to an urea concentration that would be expected to support native enzyme, only about 20 and 5% of activity is recovered for major allele (P11/I340) and P11L/I340M (minor allele, respectively)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
development of an indirect glycolate cytotoxicity assay using CHO cells expressing glycolate oxidase and various normal and mutant forms of AGT
diagnostics
loss of AGXT expression is correlated with a poor prognosis and differentiation of hepatocellular carcinoma (HCC)
medicine
nutrition
-
overexpression of enzyme in Ashbya gossypii, use for production of riboflavin for human and animal feed supplement
medicine
-
hereditary disease primary hyperoxaluria type 1 is caused by a deficiency of the liver-specific peroxisomal enzyme alanine:glyoxylate aminotransferase, diagnosis with selective inhibitors and enzyme assays
medicine
-
after 4 weeks of vitamin B6-deficient diet, hepatic enzyme activity and mRNA level are significantly lower than in control animals. Urinary oxalate-to-creatinine and glycolate-to-creatinine ratios are higher than in controls, but urinary glycine-to-creatinine and citrate-to-creatinine ratios are significantly lower
medicine
-
primary hyperoxaluria type I is a severe kidney stone disease caused by mutations in the protein alanine:glyoxylate aminotransferase
medicine
-
mutations in conserved residue Gly161 to Arg, Cys or Ser are associated with Primary Hyperoxaluria Type I, a severe rare disorder of metabolism. Mutations of Gly161 strongly reduce the expression levels and the intracellular half-life of AGT, and make the protein in the apo-form prone to an electrostatically-driven aggregation in the cell cytosol. The coenzyme pyridoxal 5'-phospahte, by shifting the equilibrium from the apo- to the holo-form, is able to reduce the aggregation propensity of the variants, thus partly decreasing the effect of the mutations
medicine
-
the effectiveness of pharmacological doses of pyridoxine results froman improved metabolic effectiveness of AGT. In cells expressing glycolate oxidase the great majority of glycolate is converted to oxalate and glyoxylate, with the latter causing the greater decrease in cell survival. Co-expression of normal AGTs and some, but not all, mutant AGT variants partially counteracts this cytotoxicity and leads to decreased synthesis of oxalate and glyoxylate. Increasing the extracellular pyridoxine up to 0.3 microM leads to an increased metabolic effectiveness of normal AGTs and the G170R variant. The increased survival seen with G170R is paralleled by a 40% decrease in oxalate and glyoxylate levels
medicine
-
infusion of asymmetric dimethylarginines causes a 3- to 4fold increase in plasma and urine asymmetric dimethylarginine levels and a 2- to 3fold increase in plasma and urine levels of the asymmetric dimethylarginine-specific metabolite of AGXT2, alpha-keto-delTA-(N,N-dimethylguanidino)valeric acid. Plasma levels of alpha-keto-delTA-(N,N-dimethylguanidino)valeric acid are elevated 32fold in the mice, which underwent bilateral nephrectomy. Neither bilateral nephrectomy nor asymmetric dimethylarginine infusion causes upregulation of AGXT2 expression or activity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koide, Y.; Honma, M.; Shimomura, T.
L-alanine-alpha-keto acid aminotransferase of Pseudomonas sp.
Agric. Biol. Chem.
41
781-784
1977
Pseudomonas sp.
-
brenda
Rowsell, E.V.; Snell, K.; Carnie, J.A.; Rowsell, K.V.
The subcellular distribution of rat liver L-alanine-glyoxylate aminotransferase in relation to a pathway for glucose formation involving glyoxylate
Biochem. J.
127
155-156
1972
Rattus norvegicus
brenda
Noguchi, T.; Okuno, E.; Takada, Y.; Minatogawa, Y.; Okai, K.; Kido, R.
Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species
Biochem. J.
169
113-122
1978
Canis lupus familiaris, Felis catus, Mus musculus, Rattus norvegicus
brenda
Okuno, E.; Minatogawa, Y.; Kido, R.
Co-purification of alanine-glyoxylate aminotransferase with 2-aminobutyrate aminotransferase in rat kidney
Biochim. Biophys. Acta
715
97-104
1982
Rattus norvegicus
brenda
Nakamura, Y.; Tolbert, N.E.
Serine: glyoxylate, alanine:glyoxylate, and glutamate:glyoxylate aminotransferase reactions in peroxisomes from spinach leaves
J. Biol. Chem.
258
7631-7638
1983
Spinacia oleracea
brenda
Noguchi, T.; Fujiwara, S.; Takada, Y.; Mori, T.; Nagano, M.; Hanada, N.; Saeki, E.; Yasuo, O.
Enzymatic and immunological comparison of alanine: glyoxylate aminotransferases from different fish and mammalian livers
Comp. Biochem. Physiol. B
77
279-283
1984
Caranx chrysos, Sardinops sp., Scomberomorus sp., Sebastes carnatus
brenda
Takada, Y.; Noguchi, T.
Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates
Biochem. J.
231
157-163
1985
Saccharomyces cerevisiae
brenda
Okuno, E.; Ishikawa, T.; Kawai, J.; Kido, R.
Alanine:glyoxylate aminotransferase activities in liver of Suncus murinus (Insectivora)
Comp. Biochem. Physiol. B
90
773-778
1988
Suncus murinus
brenda
Kobayashi, S.; Hayashi, S.; Fujiwara, S.; Noguchi, T.
Identity of alanine:glyoxylate aminotransferase with alanine:2-oxoglutarate aminotransferase in rat liver cytosol
Biochimie
71
471-475
1989
Rattus norvegicus
brenda
Sakuraba, H.; Fujiwara, S.; Noguchi, T.
Purification and characterization of peroxisomal apo and holo alanine:glyoxylate aminotransferase from bird liver
Arch. Biochem. Biophys.
286
453-460
1991
Anas platyrhynchos domestica, Anser anser, Columba livia, Gallus gallus, Melopsittacus undulatus, Passer montanus saturatus, Phasianus versicolor, Lonchura oryzivora, Serinus canaria, Uroloncha striata domestica
brenda
Danpure, C.J.; Fryer, P.; Griffiths, S.; Guttridge, K.M.; Jennings, P.R.; Allsop, J.; Moser, A.B.; Naidu, S.; Moser, H.W.; et al.
Cytosolic compartmentalization of hepatic alanine:glyoxylate aminotransferase in patients with aberrant peroxisomal biogenesis and its effect on oxalate metabolism
J. Inherit. Metab. Dis.
17
27-40
1994
Homo sapiens
brenda
Horvath, V.A.P.; Wanders, R.J.A.
Aminooxy acetic acid: a selective inhibitor of alanine:glyoxylate aminotransferase and its use in the diagnosis of primary hyperoxaluria type I
Clin. Chim. Acta
243
105-114
1995
Homo sapiens
brenda
Ishikawa, K.; Kaneko, E.; Ichiyama, A.
Pyridoxal 5'-phosphate binding of a recombinant rat serine: pyruvate/alanine:glyoxylate aminotransferase
J. Biochem.
119
970-978
1996
Rattus norvegicus
brenda
Leiper, J.M.; Oatey, P.B.; Danpure, C.J.
Inhibition of alanine:glyoxylate aminotransferase 1 dimerization is a prerequisite for its peroxisome-to-mitochondrion mistargeting in primary hyperoxaluria type 1
J. Cell. Biol.
135
939-951
1996
Homo sapiens
brenda
Rumsby, G.; Weir, T.; Samuell, C.T.
A semiautomated alanine:glyoxylate aminotransferase assay for the tissue diagnosis of primary hyperoxaluria type 1
Ann. Clin. Biochem.
34
400-404
1997
Homo sapiens
-
brenda
Holbrook, J.D.; Birdsey, G.M.; Yang, Z.; Bruford, M.W.; Danpure, C.J.
Molecular adaptation of alanine: glyoxylate aminotransferase targeting in primates
Mol. Biol. Evol.
17
387-400
2000
Ateles paniscus (Q9TTS7), Callimico goeldii (Q9TTQ8), Mico argentatus, Callithrix jacchus, Cercopithecus diana (Q9TTR4), Cheirogaleus medius, Gorilla gorilla (Q9TTQ0), Homo sapiens, Hylobates lar (Q9TTP9), Eulemur fulvus, Leontopithecus rosalia (Q9TTP8), Loris tardigradus, Macaca fuscata, Macaca nigra (Q9TTP7), Xanthonycticebus pygmaeus, Pan troglodytes (Q9TTP2), Papio anubis (Q9TSP4), Pithecia pithecia (Q9TTP3), Pongo pygmaeus, Saimiri sciureus (Q9TTP0), Saguinus oedipus
brenda
Lumb, M.J.; Danpure, C.J.
Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations
J. Biol. Chem.
275
36415-36422
2000
Homo sapiens
brenda
Oda, T.; Uchida, C.; Miura, S.
Mitochondrial targeting signal-induced conformational change and repression of the peroxisomal targeting signal of the precursor for rat liver serine:pyruvate/alanine:glyoxylate aminotransferase
J. Biochem.
127
665-671
2000
Rattus norvegicus
brenda
Liepman, A.H.; Olsen, L.J.
Peroxisomal alanine: glyoxylate aminotransferase (AGT1) is a photorespiratory enzyme with multiple substrates in Arabidopsis thaliana
Plant J.
25
487-498
2001
Arabidopsis thaliana (Q56YA5), Arabidopsis thaliana
brenda
Zhang, X.; Roe, S.M.; Pearl, L.H.; Danpure, C.J.
Crystallization and preliminary crystallographic analysis of human alanine:glyoxylate aminotransferase and its polymorphic variants
Acta Crystallogr. Sect. D
57
1936-1937
2001
Homo sapiens
brenda
Han, Q.; Li, J.
Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase
FEBS Lett.
527
199-204
2002
Aedes aegypti, Drosophila melanogaster (Q9W3Z3), Drosophila melanogaster
brenda
Danpure, C.J.; Lumb, M.J.; Birdsey, G.M.; Zhang, X.
Alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting in human hereditary kidney stone disease
Biochim. Biophys. Acta
1647
70-75
2003
Homo sapiens
brenda
Santana, A.; Salido, E.; Torres, A.; Shapiro, L.J.
Primary hyperoxaluria type 1 in the Canary Islands: A conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase
Proc. Natl. Acad. Sci. USA
100
7277-7282
2003
Homo sapiens
brenda
Zhang, X.; Roe, S.M.; Hou, Y.; Bartlam, M.; Rao, Z.; Pearl, L.H.; Danpure, C.J.
Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1
J. Mol. Biol.
331
643-652
2003
Homo sapiens
brenda
Kato, T.; Park, E.Y.
Expression of alanine:glyoxylate aminotransferase gene from Saccharomyces cerevisiae in Ashbya gossypii
Appl. Microbiol. Biotechnol.
71
46-52
2005
Saccharomyces cerevisiae
brenda
Meyer, P.; Liger, D.; Leulliot, N.; Quevillon-Cheruel, S.; Zhou, C.Z.; Borel, F.; Ferrer, J.L.; Poupon, A.; Janin, J.; van Tilbeurgh, H.
Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein
Biochimie
87
1041-1047
2005
Saccharomyces cerevisiae (P43567), Saccharomyces cerevisiae
brenda
Sakuraba, H.; Kawakami, R.; Takahashi, H.; Ohshima, T.
Novel archaeal alanine:glyoxylate aminotransferase from Thermococcus litoralis
J. Bacteriol.
186
5513-5518
2004
Thermococcus litoralis
brenda
Nishijima, S.; Sugaya, K.; Morozumi, M.; Hatano, T.; Ogawa, Y.
Hepatic alanine-glyoxylate aminotransferase activity and oxalate metabolism in vitamin B6 deficient rats
J. Urol.
169
683-686
2003
Rattus norvegicus
brenda
Coulter-Mackie, M.B.; Lian, Q.; Applegarth, D.; Toone, J.
The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1
Mol. Genet. Metab.
86
172-178
2005
Homo sapiens (P21549), Homo sapiens
brenda
Liepman, A.H.; Olsen, L.J.
Alanine aminotransferase homologs catalyze the glutamate:glyoxylate aminotransferase reaction in peroxisomes of Arabidopsis
Plant Physiol.
131
215-227
2003
Arabidopsis thaliana, Arabidopsis thaliana (Q9S7E9)
brenda
Coulter-Mackie, M.B.; Lian, Q.; Wong, S.G.
Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor
Protein Expr. Purif.
41
18-26
2005
Homo sapiens
brenda
Han, G.W.; Schwarzenbacher, R.; Page, R.; Jaroszewski, L.; Abdubek, P.; Ambing, E.; Biorac, T.; Canaves, J.M.; Chiu, H.J.; Dai, X.; Deacon, A.M.et al.
Crystal structure of an alanine-glyoxylate aminotransferase from Anabaena sp. at 1.70 A resolution reveals a noncovalently linked PLP cofactor
Proteins Struct. Funct. Bioinform.
58
971-975
2005
Anabaena sp.
brenda
Schlosser, T.; Gatgens, C.; Weber, U.; Stahmann, K.P.
Alanine:glyoxylate aminotransferase of Saccharomyces cerevisiae-encoding gene AGX1 and metabolic significance
Yeast
21
63-73
2004
Saccharomyces cerevisiae (P43567), Saccharomyces cerevisiae
brenda
Koul, S.; Johnson, T.; Pramanik, S.; Koul, H.
Cellular transfection to deliver alanine-glyoxylate aminotransferase to hepatocytes: a rational gene therapy for primary hyperoxaluria-1 (PH-1)
Am. J. Nephrol.
25
176-182
2005
Homo sapiens
brenda
Han, Q.; Kim, S.R.; Ding, H.; Li, J.
Evolution of two alanine glyoxylate aminotransferases in mosquito
Biochem. J.
397
473-481
2006
Aedes aegypti (Q3LSM4)
brenda
Huber, P.A.; Birdsey, G.M.; Lumb, M.J.; Prowse, D.T.; Perkins, T.J.; Knight, D.R.; Danpure, C.J.
Peroxisomal import of human alanine:glyoxylate aminotransferase requires ancillary targeting information remote from its C terminus
J. Biol. Chem.
280
27111-27120
2005
Homo sapiens
brenda
Han, Q.; Robinson, H.; Gao, Y.G.; Vogelaar, N.; Wilson, S.R.; Rizzi, M.; Li, J.
Crystal structures of Aedes aegypti alanine glyoxylate aminotransferase
J. Biol. Chem.
281
37175-37182
2006
Aedes aegypti
brenda
Ricoult, C.; Echeverria, L.O.; Cliquet, J.B.; Limami, A.M.
Characterization of alanine aminotransferase (AlaAT) multigene family and hypoxic response in young seedlings of the model legume Medicago truncatula
J. Exp. Bot.
57
3079-3089
2006
Medicago truncatula
brenda
Coulter-Mackie, M.B.; Lian, Q.
Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations
Mol. Genet. Metab.
89
349-359
2006
Homo sapiens
brenda
Salido, E.C.; Li, X.M.; Lu, Y.; Wang, X.; Santana, A.; Roy-Chowdhury, N.; Torres, A.; Shapiro, L.J.; Roy-Chowdhury, J.
Alanine-glyoxylate aminotransferase-deficient mice, a model for primary hyperoxaluria that responds to adenoviral gene transfer
Proc. Natl. Acad. Sci. USA
103
18249-18254
2006
Homo sapiens
brenda
Sakuraba, H.; Yoneda, K.; Takeuchi, K.; Tsuge, H.; Katunuma, N.; Ohshima, T.
Structure of an archaeal alanine:glyoxylate aminotransferase
Acta Crystallogr. Sect. D
64
696-699
2008
Thermococcus litoralis (Q9C4M4)
brenda
Cellini, B.; Bertoldi, M.; Montioli, R.; Paiardini, A.; Borri Voltattorni, C.
Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications
Biochem. J.
408
39-50
2007
Homo sapiens, Homo sapiens (A2V838)
brenda
Bertoldi, M.; Cellini, B.; Paiardini, A.; Montioli, R.; Borri Voltattorni, C.
Reactions of human liver peroxisomal alanine:glyoxylate aminotransferase with beta -chloro-L-alanine and L-cysteine: Spectroscopic and kinetic analysis
Biochim. Biophys. Acta
1784
1356-1362
2008
Homo sapiens (P21549)
brenda
Ikeda, M.; Kanouchi, H.; Minatogawa, Y.
Characterization of peroxisomal targeting signals on alanine: glyoxylate aminotransferase
Biol. Pharm. Bull.
31
131-134
2008
Homo sapiens
brenda
Hopper, E.D.; Pittman, A.M.; Fitzgerald, M.C.; Tucker, C.L.
In vivo and in vitro examination of stability of primary hyperoxaluria-associated human alanine:glyoxylate aminotransferase
J. Biol. Chem.
283
30493-30502
2008
Homo sapiens
brenda
Coulter-Mackie, M.B.; Lian, Q.
Partial trypsin digestion as an indicator of mis-folding of mutant alanine:glyoxylate aminotransferase and chaperone effects of specific ligands. Study of a spectrum of missense mutants
Mol. Genet. Metab.
94
368-374
2008
Homo sapiens
brenda
Cellini, B.; Montioli, R.; Bianconi, S.; Lopez-Alonso, J.P.; Voltattorni, C.B.
Construction, purification and characterization of untagged human liver alanine-glyoxylate aminotransferase expressed in Escherichia coli
Protein Pept. Lett.
15
153-159
2008
Homo sapiens
brenda
Djordjevic, S.; Zhang, X.; Bartlam, M.; Ye, S.; Rao, Z.; Danpure, C.J.
Structural implications of a G170R mutation of alanine:glyoxylate aminotransferase that is associated with peroxisome-to-mitochondrion mistargeting
Acta Crystallogr. Sect. F
66
233-236
2010
Homo sapiens (P21549)
brenda
Kameya, M.; Arai, H.; Ishii, M.; Igarashi, Y.
Purification of three aminotransferases from Hydrogenobacter thermophilus TK-6 - novel types of alanine or glycine aminotransferase
FEBS J.
277
1876-1885
2010
Hydrogenobacter thermophilus (D2Z0I0), Hydrogenobacter thermophilus TK-6 / IAM 12695 (D2Z0I0)
brenda
Cellini, B.; Montioli, R.; Paiardini, A.; Lorenzetto, A.; Voltattorni, C.B.
Molecular insight into the synergism between the minor allele of human liver peroxisomal alanine:glyoxylate aminotransferase and the F152I mutation
J. Biol. Chem.
284
8349-8358
2009
Homo sapiens (P21549), Homo sapiens
brenda
Rodionov, R.N.; Murry, D.J.; Vaulman, S.F.; Stevens, J.W.; Lentz, S.R.
Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production
J. Biol. Chem.
285
5385-5391
2010
Homo sapiens
brenda
Cellini, B.; Montioli, R.; Paiardini, A.; Lorenzetto, A.; Maset, F.; Bellini, T.; Oppici, E.; Voltattorni, C.B.
Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I
Proc. Natl. Acad. Sci. USA
107
2896-2901
2010
Homo sapiens
brenda
Kawai, C.; Minatogawa, Y.; Akiyoshi, H.; Hirose, S.; Suehiro, T.; Tone, S.
A novel mutation of human liver alanine:glyoxylate aminotransferase causes primary hyperoxaluria type 1: immunohistochemical quantification and subcellular distribution
Acta Histochem. Cytochem.
45
121-129
2012
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
Homo sapiens (Q9BYV1), Mus musculus (Q3UEG6)
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
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