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Information on EC 2.6.1.15 - glutamine-pyruvate transaminase
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EC Tree
2.6.1.15 glutamine-pyruvate transaminaseIUBMB Comments
A pyridoxal-phosphate protein. L-Methionine can act as donor; glyoxylate can act as acceptor.
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Word Map
- 2.6.1.15
-
transamination
- omega-amidase
-
beta-lyase
-
ketimine
- alpha-ketoglutaramate
- phenylpyruvate
-
kynurenic
-
s-conjugate
- alpha-keto-gamma-methiolbutyrate
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
glutamine transaminase, glutaminase ii, glutamine transaminase l, gamma-glutaminyltransferase, glutamine-oxo acid aminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminotransferase, glutamine-keto acid
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-
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gamma-glutaminyltransferase
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-
-
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glutaminase II
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-
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glutamine transaminase
glutamine transaminase L
glutamine-alpha-keto acid transamidase
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-
-
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glutamine-alpha-keto acid transaminase
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-
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glutamine-keto acid aminotransferase
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-
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glutamine-oxo acid aminotransferase
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-
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glutamine-oxo-acid transaminase
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-
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glutamine transaminase
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-
-
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glutamine transaminase L
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-glutamine:pyruvate aminotransferase
A pyridoxal-phosphate protein. L-Methionine can act as donor; glyoxylate can act as acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
9030-44-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutaramate + glycine
L-glutamine + glyoxylate
-
poor substrate
-
?
2-oxoglutaramate + L-alanine
L-glutamine + pyruvate
-
poor substrate
-
?
2-oxoglutaramate + L-asparagine
L-glutamine + 2-oxosuccinamate
-
poor substrate
-
?
2-oxoglutaramate + L-cysteine
L-glutamine + 3-mercapto-2-oxopropanoate
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poor substrate
-
?
2-oxoglutaramate + L-ethionine
L-glutamine + 4-ethylsulfanyl-2-oxobutanoate
-
-
-
?
2-oxoglutaramate + L-glutamic acid 4-benzylester
L-glutamine + 2-oxopentane-1,5-dioic acid benzyl ester
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poor substrate
-
?
2-oxoglutaramate + L-homoserine
L-glutamine + 4-hydroxy-2-oxobutanoate
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-
-
?
2-oxoglutaramate + L-methionine (SR)-sulfoxide
L-glutamine + 4-methylsulfinyl-2-oxobutanoate
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-
-
?
2-oxoglutaramate + L-methionine sulfone
L-glutamine + 4-methylsulfonyl-2-oxobutanoate
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-
-
?
2-oxoglutaramate + L-phenylalanine
L-glutamine + phenylpyruvate
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poor substrate
-
?
2-oxoglutaramate + L-serine
L-glutamine + 3-hydroxy-2-oxopropanoate
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poor substrate
-
?
gamma-glutamylhydrazones of 2-oxo acid
L-amino acid + 2-hydroxy-tetrahydro-6-pyridazinone-3-carboxylic acid
glyoxylate + DL-homocysteine
glycine + 2-oxo-4-thiobutanoate
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poor substrate
-
?
glyoxylate + L-2-amino-4-oxo-5-chloropentanoic acid
glycine + 5-chloro-2,4-dioxopentanoate
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poor substrate
-
?
glyoxylate + L-asparagine
glycine + 2-oxosuccinamate
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poor substrate
-
?
glyoxylate + L-serine
glycine + 3-hydroxy-2-oxopropanoate
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poor substrate
-
?
L-glutamine + 4-methylsulfanyl-2-oxobutanoate
2-oxoglutaramate + L-methionine
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-
-
?
L-phenylalanine + 4-methylthio-2-oxobutanoate
phenylpyruvate + 2-amino-4-methylthiobutanoate
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-
-
-
?
pyruvate + L-methionine
L-alanine + 4-methylsulfanyl-2-oxobutanoate
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poor substrate
-
?
pyruvate + L-methionine (SR)-sulfoxide
L-alanine + 4-methylsulfinyl-2-oxobutanoate
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poor substrate
-
?
pyruvate + L-methionine sulfone
L-alanine + 4-methylsulfonyl-2-oxobutanoate
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poor substrate
-
?
S-(3-aminopropyl)cysteine + pyruvate
S-(3-aminopropyl)thiopyruvic acid + amino acid
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-
-
?
selenium-(3-aminopropyl)selenocysteine + pyruvate
selenium-(3-aminopropyl)selenopyruvic acid + amino acid
-
-
-
?
selenomethionine + phenylpyruvate
2-oxo-gamma-methylselenobutyrate + L-phenylalanine
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-
-
?
2-oxoglutaramate + L-methionine
L-glutamine + 4-methylsulfanyl-2-oxobutanoate
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-
-
?
2-oxoglutaramate + L-methionine
L-glutamine + 4-methylsulfanyl-2-oxobutanoate
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best amino group donor
-
?
gamma-glutamylhydrazones of 2-oxo acid
L-amino acid + 2-hydroxy-tetrahydro-6-pyridazinone-3-carboxylic acid
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-
-
?
gamma-glutamylhydrazones of 2-oxo acid
L-amino acid + 2-hydroxy-tetrahydro-6-pyridazinone-3-carboxylic acid
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gamma-glutamylhydrazones of 4-ethylsulfanyl-2-oxobutanoate, glyoxylate, 2-oxoisovalerate, transfers the 2-amino group of the glutamyl moiety to the oxo acid moiety, the reaction rates are higher than those of the corresponding glutamine alpha-keto acid transaminations
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?
glyoxylate + glutamic acid 4-methyl ester
glycine + 2-oxoglutarate 4-methyl ester
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-
-
?
glyoxylate + glutamic acid 4-methyl ester
glycine + 2-oxoglutarate 4-methyl ester
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-
-
?
glyoxylate + L-cysteine
glycine + 3-mercapto-2-oxopropanoate
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-
-
?
glyoxylate + L-cysteine
glycine + 3-mercapto-2-oxopropanoate
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poor substrate
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?
glyoxylate + L-ethionine
glycine + 4-ethylsulfanyl-2-oxobutanoate
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-
-
?
glyoxylate + L-ethionine
glycine + 4-ethylsulfanyl-2-oxobutanoate
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-
-
?
glyoxylate + L-ethionine
glycine + 4-ethylsulfanyl-2-oxobutanoate
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-
-
?
glyoxylate + L-glutamine
glycine + 2-oxoglutaramate
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2-oxoglutaramate cyclizes spontaneously to form 2-pyrrolidone-5-hydroxy-5-carboxylate
?
glyoxylate + L-glutamine
glycine + 2-oxoglutaramate
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best substrate
-
?
glyoxylate + L-glutamine
glycine + 2-oxoglutaramate
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-
-
?
glyoxylate + L-homoserine
glycine + 4-hydroxy-2-oxobutanoate
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-
-
?
glyoxylate + L-homoserine
glycine + 4-hydroxy-2-oxobutanoate
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poor substrate
-
?
glyoxylate + L-methionine
glycine + 4-methylsulfanyl-2-oxobutanoate
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-
-
?
glyoxylate + L-methionine
glycine + 4-methylsulfanyl-2-oxobutanoate
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-
-
?
glyoxylate + L-methionine
glycine + 4-methylsulfanyl-2-oxobutanoate
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-
-
?
glyoxylate + L-methionine
glycine + 4-methylsulfanyl-2-oxobutanoate
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-
-
?
glyoxylate + L-methionine (SR)-sulfoxide
glycine + ?
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-
-
?
glyoxylate + L-methionine sulfone
glycine + 4-methylsulfonyl-2-oxobutanoate
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-
-
?
glyoxylate + L-methionine sulfone
glycine + 4-methylsulfonyl-2-oxobutanoate
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-
-
?
glyoxylate + L-phenylalanine
glycine + phenylpyruvate
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poor substrate
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?
glyoxylate + S-methyl-L-cysteine
glycine + 3-methylsulfanyl-2-oxopropanoate
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-
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?
glyoxylate + S-methyl-L-cysteine
glycine + 3-methylsulfanyl-2-oxopropanoate
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poor substrate
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?
L-albizziin + glyoxylate
glycine + 2-imidazolidone-5-hydroxy-5-carboxylic acid
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undergoes non-enzymatic dehydration to 2-imidazolinone-5-carboxylate
?
L-albizziin + glyoxylate
glycine + 2-imidazolidone-5-hydroxy-5-carboxylic acid
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S-carbamoyl-L-cysteine or O-carbamoyl-L-serine can replace albizziin
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?
L-glutamine + 2-oxoglutaramate
2-oxoglutaramate + L-glutamine
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-
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?
L-glutamine + 2-oxoglutaramate
2-oxoglutaramate + L-glutamine
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-
-
?
L-glutamine + 3-mercaptopyruvate
2-oxoglutaramate + L-cysteine
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-
-
?
L-glutamine + 3-mercaptopyruvate
2-oxoglutaramate + L-cysteine
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-
-
?
L-glutamine + alpha-keto acid
alpha-ketoglutarate + amino acid
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-
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?
L-glutamine + alpha-keto acid
alpha-ketoglutarate + amino acid
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-
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?
L-glutamine + alpha-keto acid
alpha-ketoglutarate + amino acid
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-
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?
L-glutamine + alpha-keto acid
alpha-ketoglutarate + amino acid
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-
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?
pyruvate + L-glutamine
L-alanine + 2-oxoglutaramate
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pyruvate cannot be replaced by its hydrazone, oxime or semicarbazone derivatives
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?
pyruvate + L-glutamine
L-alanine + 2-oxoglutaramate
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L-glutamine cannot be replaced by glycine
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?
additional information
?
-
recombinant mouse KAT3/GTL selectively metabolizes selenomethionine to 2-oxo-gamma-methylselenobutyrate, KAT3/GTLis more efficient in transamination of both than is KAT1/GTK
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additional information
?
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recombinant mouse KAT3/GTL selectively metabolizes selenomethionine to 2-oxo-gamma-methylselenobutyrate, KAT3/GTLis more efficient in transamination of both than is KAT1/GTK
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
selenomethionine + phenylpyruvate
2-oxo-gamma-methylselenobutyrate + L-phenylalanine
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-
-
?
L-glutamine + alpha-keto acid
alpha-ketoglutarate + amino acid
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-
-
?
L-glutamine + alpha-keto acid
alpha-ketoglutarate + amino acid
-
-
-
?
L-glutamine + alpha-keto acid
alpha-ketoglutarate + amino acid
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glyoxylate
-
at high concentration, transamination between albizziin and glyoxylate
L-gamma-glutamylhydrazide
-
with gamma-glutamylhydrazone of glyoxylate as substrate, weak
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
Effect of chronic alkalosis and acidosis on glutaminase II path in the dog kidney in vivo.
Alkalosis
Effect of chronic alkalosis and acidosis on glutaminase II path in the dog kidney in vivo.
Astrocytoma
GLUTAMINE TRANSAMINASE IN BRAIN TISSUE PREPARATIONS AND IN CELLS OF A HUMAN STRAIN OF DEDIFFERENTIATED ASTROCYTOMA.
Astrocytoma
[Glutamine transaminase in brain preparations and in cells of a strain of differentiated human astrocytoma.]
Carcinogenesis
Upregulation of the Glutaminase II Pathway Contributes to Glutamate Production upon Glutaminase 1 Inhibition in Pancreatic Cancer.
Carcinoma
[Specificity of glutamine metabolism in pre-tumorous diseases and cancer of the human stomach]
Gastritis, Atrophic
[Specificity of glutamine metabolism in pre-tumorous diseases and cancer of the human stomach]
Hepatic Encephalopathy
[Analysis of prognostic factors and construction of a logistic regression model for patients with drug-induced liver failure].
Hepatorenal Syndrome
[Analysis of prognostic factors and construction of a logistic regression model for patients with drug-induced liver failure].
Liver Diseases
[Analysis of prognostic factors and construction of a logistic regression model for patients with drug-induced liver failure].
Neoplasms
High Levels of Glutaminase II Pathway Enzymes in Normal and Cancerous Prostate Suggest a Role in 'Glutamine Addiction'.
Neoplasms
The Metabolic Importance of the Glutaminase II Pathway in Normal and Cancerous Cells.
Neoplasms
Upregulation of the Glutaminase II Pathway Contributes to Glutamate Production upon Glutaminase 1 Inhibition in Pancreatic Cancer.
Nephrosis
Erythrocytic enzymes and amino acids related to glutamic acid metabolism in childhood hypoproteinemic states.
Pancreatic Neoplasms
Upregulation of the Glutaminase II Pathway Contributes to Glutamate Production upon Glutaminase 1 Inhibition in Pancreatic Cancer.
Prostatic Neoplasms
High Levels of Glutaminase II Pathway Enzymes in Normal and Cancerous Prostate Suggest a Role in 'Glutamine Addiction'.
Protein-Energy Malnutrition
Erythrocytic enzymes and amino acids related to glutamic acid metabolism in childhood hypoproteinemic states.
Renal Insufficiency, Chronic
[Activity of glutamine deaminating enzymes in the kidneys, liver and serum of dogs with renal failure and under normal conditions]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6 - 8.8
-
about half-maximum activity at pH 7.6 and about 90% of maximum activity at pH 8.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional kynurenine aminotransferase/glutamine transaminase, 4 isoforms, expression in COS1-cells
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
tissue localizations of KAT3/GTL/CCBL2, real-time RT-PCR enzyme expression analysis in tissues of female and male animals, overview. The enzyme is present in both liver and kidney of the mouse, but is much more abundant in the kidney than in the liver
brenda
additional information
-
tissue localizations of KAT3/GTL/CCBL2, real-time RT-PCR enzyme expression analysis in tissues of female and male animals, overview. The enzyme is present in both liver and kidney of the mouse, but is much more abundant in the kidney than in the liver
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
kynurenine aminotransferase 3 (KAT3, EC 2.6.1.7) catalyzes the transamination of kynurenine to kynurenic acid, and is identical to cysteine conjugate beta-lyase 2 (CCBL2, EC 4.4.1.13) and glutamine transaminase L (GTL, EC 2.6.1.64)
additional information
additional information
the enzyme is a key enzyme for studying the nephrotoxic mechanism of some xenobiotics and the formation of chemopreventive compounds in the mouse kidney
additional information
-
the enzyme is a key enzyme for studying the nephrotoxic mechanism of some xenobiotics and the formation of chemopreventive compounds in the mouse kidney
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A088SHX2_9TRYP
414
0
46414
TrEMBL
other Location (Reliability: 3)
A0A3Q8IGK8_LEIDO
414
0
46154
TrEMBL
Mitochondrion (Reliability: 5)
A0A1G4ICR0_TRYEQ
429
0
48334
TrEMBL
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM