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Information on EC 3.5.1.2 - glutaminase and Organism(s) Rattus norvegicus and UniProt Accession P13264
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3.5.1.2 glutaminaseSpecify your search results
Word Map
- 3.5.1.2
- ammonia
-
phosphate-dependent
-
glutaminolysis
-
neurotransmitter
-
glutamatergic
- l-asparaginase
-
amidotransferase
- cerebral
- astrocyte
- asparagine
-
excitatory
-
ammoniagenesis
-
glutamine-dependent
- 6-diazo-5-oxo-l-norleucine
- hexokinase
-
tricarboxylic
- tca
- alpha-ketoglutarate
- lymphoblastic
- phosphoenolpyruvate
-
deamidation
-
gamma-glutamyl
-
carboxykinase
-
synaptosomes
- bicarbonate
-
neurotransmission
- enterocytes
-
addict
-
gabaergic
-
transamination
-
transmitter
- l-glutamate
-
acidotic
- hyperammonemia
- nh3
-
carbamyl
-
warburg
-
ammoniagenic
-
anaplerosis
- aminooxyacetate
- alkalosis
- nh4cl
- acivicin
-
glutamate-glutamine
-
perivenous
-
slc1a5
- chrysanthemi
- carbamoylphosphate
-
ureagenesis
- analysis
- medicine
- nutrition
- synthesis
- food industry
- glucosamine-6-phosphate
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glutaminase, l-glutaminase, phosphate-activated glutaminase, mitochondrial glutaminase, glutaminase 1, kidney-type glutaminase, phosphate activated glutaminase, glutaminase a, glnase, glutaminase c, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GLS
-
-
-
-
glutaminase I
-
-
-
-
glutamine aminohydrolase
-
-
-
-
K-glutaminase
-
-
-
-
L-glutaminase
-
-
-
-
L-glutamine amidohydrolase
-
-
-
-
PAG
-
-
-
-
phosphate activated glutaminase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-glutamine amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9001-47-2
-
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
Gln + H2O
Glu + NH3
-
-
209009, 209010, 209012, 209013, 209015, 209016, 209017, 209018, 209019, 209028, 209029, 209030, 209031, 209033, 209034
-
-
?
additional information
?
-
-
the spatial segregation of tissue-specific isozymes in pancreas alpha- and beta-cells may have important functional implications, facilitating a differential regulation of glutamate production in insulin- and glucagon-secreting cells, overview
-
-
?
L-Gln + H2O
L-Glu + NH3
-
contribution of the enzyme to elevated extracellular Glu at 24 h after onset of focal ischemia
-
-
?
L-Gln + H2O
L-Glu + NH3
-
kidney enzyme increases during acidosis, skeletal muscle enzyme does not. Under some conditions the enzyme from skeletal muscle is able to catabolize Gln to Glu and further to CO2
-
-
?
L-Gln + H2O
L-Glu + NH3
-
high glutaminase activity may be of importance for optimal insulin secretion elicited by amino acid secretagogues
-
-
?
L-Gln + H2O
L-Glu + NH3
-
enzyme is involved in deamination of Gln to Glu, which is utilized for energy production via the TCA cycle. Glutaminase mRNA increases around the 3rd week of life
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
renal ammonia genesis and the utilization of glutamine as a metabolic fuel, neuronal synthesis of glutamate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
the enzyme plays a key role in energy and nitrogen metabolism
-
-
?
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
additional information
?
-
-
the spatial segregation of tissue-specific isozymes in pancreas alpha- and beta-cells may have important functional implications, facilitating a differential regulation of glutamate production in insulin- and glucagon-secreting cells, overview
-
-
?
L-Gln + H2O
L-Glu + NH3
-
contribution of the enzyme to elevated extracellular Glu at 24 h after onset of focal ischemia
-
-
?
L-Gln + H2O
L-Glu + NH3
-
kidney enzyme increases during acidosis, skeletal muscle enzyme does not. Under some conditions the enzyme from skeletal muscle is able to catabolize Gln to Glu and further to CO2
-
-
?
L-Gln + H2O
L-Glu + NH3
-
high glutaminase activity may be of importance for optimal insulin secretion elicited by amino acid secretagogues
-
-
?
L-Gln + H2O
L-Glu + NH3
-
enzyme is involved in deamination of Gln to Glu, which is utilized for energy production via the TCA cycle. Glutaminase mRNA increases around the 3rd week of life
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
renal ammonia genesis and the utilization of glutamine as a metabolic fuel, neuronal synthesis of glutamate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
the enzyme plays a key role in energy and nitrogen metabolism
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide
-
a potent inhibitor of kidney-type glutaminase, but not of the liver-type glutaminase, glutamate dehydrogenase or gamma-glutamyl transpeptidase. The potent inhibitor causes the formation of a stable, but inactive, tetramer
L-glutamate
-
strong product inhibition of isozyme KGA, no inhibition of isozyme LGA
diazo-5-oxo-L-norleucine
-
inactivates dimeric enzyme form in presence or absence of phosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Leu
-
activates enzyme from mesenteric lymph nodes, 50% activation at 0.6 mM
phosphoenolpyruvate
-
activates enzyme from mesenteric lymph nodes, 50% activation at 0.2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.3
L-glutamine
-
recombinant enzyme with N-terminal and C-terminal deletions, T-phosphate buffer, pH 8.0
3.6
L-glutamine
-
recombinant enzyme with N-terminal deletion, T-phosphate buffer, pH 8.0
6.4
L-glutamine
-
recombinant enzyme with N-terminal and C-terminal deletions, T-acetate buffer, pH 8.0
7.9
L-glutamine
-
recombinant enzyme with N-terminal deletion, T-acetate buffer, pH 8.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
0.9 micromol/mg protein, measured in tumor tissue after treatment with dietary glutamine
additional information
1 micromol/mg protein, measured in jejunal mucosa in DMBA-treated rats wiht tumor
additional information
1,75 micromol/mg protein, measured in jejunal mucosa in normal rats
additional information
1.6 micromol/mg protein, measured in tumor tissue
additional information
2 micromol/mg protein, measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats with tumor
additional information
2.25 micromol/mg protein, measured in jejunal mucosa in DMBA-treated rats without tumor
additional information
3 micromol/mg protein, measured in jejunal mucosa after treatment with dietary glutamine in normal rats
additional information
5.25 micromol/mg protein, measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats without tumor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of both isozymes, the isozyme KGA/LGA ratio is very high in brain
-
expression of both isozymes, but mainly of the liver-type isozyme, LGA, the isozyme KGA/LGA ratio is very low in liver
-
isozyme LGA is specific for liver, and isozyme KGA is expressed in fetal liver
-
expression of both isozymes, the kidney-type, KGA, and the liver-type, LGA, with a complementary cellular pattern of expression, KGA is mainly present in alpha-cells, LGA is very abundant in beta-cells
-
all the glutaminase activity detected in pancreatic islets is attributed to kidney-type glutaminase and is confined to the mantle of the islet
-
preferentially localized to the surface epithelium of the small inestine, some activity is also found in cells of the lamina propria
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
one of the forms of phosphate activated glutaminase is associated with the inner mitochondrial membrane. Transport of glutamine into mitochondrial matrix may be a prerequisite for deamidation by phosphate activated glutaminase
-
parallel-fiber terminals contain a glutaminase activity that could sustain the glutamate levels during synaptic activity given that the terminals are provided with glutamine. The nerve terminal aspartate and GABA could be produced from glutamine in a reaction dependent on glutaminase activity
-
-
-
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). GLSK_RAT
674
0
74024
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
260000
-
recombinant enzyme with N-terminal deletion dialyzed versus T-phosphate buffer, pH 8.0, gel filtration
48000
-
recombinant enzyme with N-terminal and C-terminal deletions, SDS-PAGE
49700
-
recombinant enzyme with N-terminal and C-terminal deletions, based on amino acid content
64000
-
4 * 64000, based on amino acid content, recombinant enzyme with N-terminal deletion
65000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
-
in absence of phosphate the enzyme exists as an inactive protomer, addition of phosphate results in activation and dimerization
tetramer
-
4 * 63200, SDS-PAGE, recombinant enzyme with N-terminal deletion
tetramer
-
4 * 64000, based on amino acid content, recombinant enzyme with N-terminal deletion
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
in mitochondria, the first 16 amino acids are removed
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
10 min, enzyme in whole kidney homogenate, phosphate-independent glutaminase is completly stable, phosphate-dependent glutaminase is completly denatured, preincubation with phosphate, phosphate-borate or bromothymol blue which induce aggregation of the enzyme molecules fully protects from heat inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme with N-terminal deletion and recombinant enzyme with N-terminal and C-terminal deletions, by nickel-affinity chromatography, 63fold and 113fold respectively
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heini, H.G.; Gebhardt, R.; Brecht, A.; Mecke, D.
Purification and characterization of rat liver glutaminase
Eur. J. Biochem.
162
541-546
1987
Rattus norvegicus
Kvamme, E.; Torgner, I.A.A.; Svenneby, G.
Glutaminase from mammalian tissues
Methods Enzymol.
113
241-256
1985
Rattus norvegicus, Sus scrofa
Haser, W.G.; Shaphiro, R.A.; Curthoys, N.P.
Comparison of the phosphate-dependent glutaminase obtained from rat brain and kidney
Biochem. J.
229
399-408
1985
Rattus norvegicus
Patel, M.; McGivan, J.D.
Partial purification and properties of rat liver glutaminase
Biochem. J.
220
583-590
1984
Rattus norvegicus
Ardawi, M.S.M.; Newsholme, E.A.
Intracellular localization and properties of phosphate-dependent glutaminase in rat mesenteric lymph nodes
Biochem. J.
217
289-296
1984
Rattus norvegicus
Morehouse, R.F.; Curthoys, N.P.
Properties of rat renal phosphate-dependent glutaminase coupled to Sepharose. Evidence that dimerization is essential for activation
Biochem. J.
193
709-716
1981
Rattus norvegicus
McGivan, J.D.; Lacey, J.H.; Joseph, S.K.
Localization and some properties of phosphate-dependent glutaminase in disrupted liver mitochondria
Biochem. J.
192
537-542
1980
Rattus norvegicus
Kvamme, E.; Olsen, B.E.
Evidence for two species of mammalian phosphate-activated glutaminase having different regulatory properties
FEBS Lett.
107
33-36
1979
Rattus norvegicus, Sus scrofa
Kovacevic, Z.; Breberina, M.; Pavlovic, M.; Bajin, K.
Molecular form and kinetic properties of phosphate-dependent glutaminase in the mitochondria isolated from the kidneys of normal and acidotic rats
Biochim. Biophys. Acta
567
216-224
1979
Rattus norvegicus
Nelson, D.; Rumsey, W.L.; Erecinska, M.
Glutamine catabolism by heart muscle. Properties of phosphate-activated glutaminase
Biochem. J.
282
559-564
1992
Rattus norvegicus
Shapiro, R.A.; Farrell, L.; Srinivasan, M.; Curthoys, N.P.
Isolation, characterization, and in vitro expression of a cDNA that encodes the kidney isoenzyme of the mitochondrial glutaminase
J. Biol. Chem.
266
18792-18796
1991
Rattus norvegicus
Newcomb, R.; Pierce, A.R.; Kano, T.; Meng, W.; Bosque-Hamilton, P.; Taylor, L.; Curthoys, N.; Lo, E.H.
Characterization of mitochondrial glutaminase and amino acids at prolonged times after experimental focal cerebral ischemia
Brain Res.
813
103-111
1998
Rattus norvegicus
Swierczynski, J.; Bereznowski, Z.; Makarewicz, W.
Phosphate-dependent glutaminase of rat skeletal muscle. Some properties and possible role in glutamine metabolism
Biochim. Biophys. Acta
1157
55-62
1993
Homo sapiens, Rattus norvegicus
Michalik, M.; Nelson, J.; Erecinska, M.
Glutamate production in islets of Langerhans: properties of phosphate-activated glutaminase
Metabolism
41
1319-1326
1992
Rattus norvegicus
Shenoy, V.; Roig, J.C.; Kubilis, P.; Neu, J.
Characterization of glutaminase in the developing rat small intestine
J. Nutr.
126
1121S-1130S
1996
Rattus norvegicus
Kenny, J.; Bao, Y.; Hamm, B.; Taylor, L.; Toth, A.; Wagers, B.; Curthoys, N.P.
Bacterial expression, purification, and characterization of rat kidney-type mitochondrial glutaminase
Protein Expr. Purif.
31
140-148
2003
Rattus norvegicus
Baglietto-Vargas, D.; Lopez-Tellez, J.F.; Moreno-Gonzalez, I.; Gutierrez, A.; Aledo, J.C.
Segregation of two glutaminase isoforms in islets of Langerhans
Biochem. J.
381
483-487
2004
Rattus norvegicus
Marquez, J.; de la Oliva, A.R.; Mates, J.M.; Segura, J.A.; Alonso, F.J.
Glutaminase: a multifaceted protein not only involved in generating glutamate
Neurochem. Int.
48
465-471
2006
Homo sapiens, no activity in Gallus gallus, Rattus norvegicus
Robinson, M.M.; McBryant, S.J.; Tsukamoto, T.; Rojas, C.; Ferraris, D.V.; Hamilton, S.K.; Hansen, J.C.; Curthoys, N.P.
Novel mechanism of inhibition of rat kidney-type glutaminase by bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide (BPTES)
Biochem. J.
406
407-414
2007
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Montero, F.; Baglietto-Vargas, D.; Moreno-Gonzalez, I.; Lopez-Tellez, J.F.; Cuesta-Munoz, A.L.; Gutierrez, A.; Aledo, J.C.
Glutaminase activity is confined to the mantle of the islets of Langerhans
Biochimie
89
1366-1371
2007
Rattus norvegicus
Holten, A.T.; Gundersen, V.
Glutamine as a precursor for transmitter glutamate, aspartate and GABA in the cerebellum: a role for phosphate-activated glutaminase
J. Neurochem.
104
1032-1042
2008
Rattus norvegicus
Bak, L.K.; Zieminska, E.; Waagepetersen, H.S.; Schousboe, A.; Albrecht, J.
Metabolism of [U-13C]glutamine and [U-13C]glutamate in isolated rat brain mitochondria suggests functional phosphate-activated glutaminase activity in matrix
Neurochem. Res.
33
273-278
2008
Rattus norvegicus
Romero-Gomez, M.; Jover, M.; Diaz-Gomez, D.; de Teran, L.C.; Rodrigo, R.; Camacho, I.; Echevarria, M.; Felipo, V.; Bautista, J.D.
Phosphate-activated glutaminase activity is enhanced in brain, intestine and kidneys of rats following portacaval anastomosis
World J. Gastroenterol.
12
2406-2411
2006
Rattus norvegicus
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