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Enzyme Nomenclature
Information on EC 3.5.1.2 - glutaminase
for references in articles please use BRENDA:EC3.5.1.2
Word Map on EC 3.5.1.2
- 3.5.1.2
- ammonia
- renal
-
phosphate-dependent
-
glutamatergic
- cortex
-
amidotransferase
-
neurotransmitter
- lactate
-
glutaminolysis
- cerebral
- asparaginase
- urea
-
ammoniagenesis
- astrocyte
-
excitatory
- alpha-ketoglutarate
- phosphoenolpyruvate
-
glutamine-dependent
- 6-diazo-5-oxo-l-norleucine
-
neurotransmission
-
gamma-glutamyl
- hexokinase
- l-glutamate
- bicarbonate
- l-asparagine
- nh3
-
transamination
-
transmitter
-
synaptosomes
-
tricarboxylic
-
gabaergic
-
acidotic
-
carboxykinase
-
deamidation
-
hyperammonemia
- enterocytes
-
carbamyl
- aminooxyacetate
- acivicin
-
glutamate-glutamine
-
warburg
-
ammoniagenic
- alkalosis
- nutrition
-
ph-responsive
- glucosamine-6-phosphate
- carbamoyl-phosphate
-
anaplerosis
- food industry
- chrysanthemi
-
ureagenesis
-
perivenous
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.5.1.2
-
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RECOMMENDED NAME
GeneOntology No.
glutaminase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamine + H2O = L-glutamate + NH3
active site structure, the enzyme contains a catalytic dyad formed by S64 and K67
-
L-glutamine + H2O = L-glutamate + NH3
structure-function relationship and catalytic mechanism, detailed overview
-
L-glutamine + H2O = L-glutamate + NH3
active site structure, the enzyme contains a catalytic dyad formed by S64 and K67
-
-
L-glutamine + H2O = L-glutamate + NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-glutamine amidohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-47-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MTCC 10401, isolated from Gangotri region of Uttarakhand Himalaya
-
-
Bacillus sp. (in: Bacteria) LKG-01
MTCC 10401, isolated from Gangotri region of Uttarakhand Himalaya
-
-
isolated from the estuarine fish Chanos chanos, from gills, skin, and gut contents
-
-
isolated from the estuarine fish Chanos chanos, from gills, skin, and gut contents
-
-
production of significant amounts of enzyme only after the stage of rapid exponential growth
-
-
-
209014, 209031, 656204, 669694, 687117, 688502, 688517, 699661, 700394, 713112, 713428, 713429, 713550, 734818, 735073
-
-
kidney-type glutaminase, KGA or GLS1, glutaminase C, GAC, a splice variant of the gene gls encoding GLS1, and liver-type glutaminase GLS2
-
-
phosphate-activated isozyme, kidney type isozyme K-PAG and the hepatic type isozyme L-PAG
-
-
two isozymes, glutaminase K and L, i.e. LGA and KGA, or liver-type isozyme and kidney-type isozyme
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
treating cells that coexpressed Mek2-K101A and kidney-type glutaminase with suboptimal level of BPTES leads to synergistic inhibition on cell proliferation
physiological function
additional information
-
Ile221-Leu533 is the catalytic domain of kidney-type glutaminase
evolution
-
the enzyme belongs to a distinct type of glutaminase with an amidase signature sequence forming a distinct family
evolution
-
the enzyme belongs to a distinct type of glutaminase with an amidase signature sequence forming a distinct family
evolution
-
the enzyme belongs to a distinct type of glutaminase with an amidase signature sequence forming a distinct family
-
evolution
-
the enzyme belongs to a distinct type of glutaminase with an amidase signature sequence forming a distinct family
-
physiological function
-
GLS2 identified as a previously uncharacterized p53 target gene to regulate cellular energy metabolism and antioxidant defense. GLS regulates cellular energy metabolism by increasing production of glutamate and 2-oxoglutarate, which in turn results in enhanced mitochondrial respiration and ATP generation. Furthemore GLS2 regulates antioxidant defense function in cells by increasing reduced glutathione levels and decreasing reactive oxygen spcies (ROS) levels, which in turn protects cells from oxidative stress
physiological function
-
GLS2 probably controls the intracellular reactive oxygen species (ROS) and the apoptotic response fascilitating the ability of p53 to protect cells from accumulation of genomic damage and allows cells to survive after mild and repairable genotoxic stress
physiological function
-
glutaminase C is important for tumor metabolism. Glutamate production by mitochondrial glutaminase C, the first enzyme in glutaminolysis, is a key process for body homeostasis, and a crucial carbon donor for amino acid and lipid synthesis in tumor cells
physiological function
-
kidney-type glutaminase activity in cells is stimulated by EGF, and kidney-type glutaminase associates with all three kinase components of the Raf-1/Mek2/Erk signaling module, interaction mode, the bound ligand makes several hydrogen-bonding contacts to Gln285, Ser286, Asn335, Glu381, Asn388, Tyr414, Tyr466, and Val484, overview. The kidney-type glutaminase active and inhibitory sites show a dynamic nature, cross-talk and regulation of kidney-type glutaminase activities by EGF-mediated Raf-Mek-Erk signaling. The enhanced activity is abrogated by kinase-dead, dominant negative mutants of Raf-1 (Raf-1-K375M) andMek2 (Mek2-K101A), protein phosphatase PP2A, and Mek-inhibitor U0126, indicative of phosphorylation-dependent regulation. kidney-type glutaminase can interact equally well with the wild-type or mutant forms of Raf-1 and Mek2. The activity of kidney-type glutaminase is directly regulated by Raf-Mek-Erk downstream of EGF receptor
physiological function
glutaminase functions in cellular metabolism of every organism by supplying nitrogen required for the biosynthesis of a variety of metabolic intermediates, while glutamic acid plays a role in both sensory and nutritional properties of food
physiological function
-
glutaminase functions in cellular metabolism of every organism by supplying nitrogen required for the biosynthesis of a variety of metabolic intermediates, while glutamic acid plays a role in both sensory and nutritional properties of food
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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
6-diazo-5-oxo-L-norleucine + H2O
?
-
the nucleophilic attack of Ser286 sidechain on 6-diazo-5-oxo-L-norleucine releases the diazo group (N2) from the inhibitor and results in the formation of an enzyme-inhibitor complex
-
-
?
beta-cyanoalanine + H2O
?
-
0.2% of the activity with L-Gln
-
-
?
D-Asn + H2O
D-aspartate + NH3
-
less 0.1% of the activity with L-glutamine and H2O as co-substrate
-
-
?
D-Asn + hydroxylamine
D-2-amino-4-(hydroxylamino)-4-oxobutanoic acid + NH3
-
-
-
-
?
D-gamma-glutamyl-ethylester + hydroxylamine
D-gamma-glutamyl hydroxamate + ethanol
-
-
-
-
?
D-gamma-glutamyl-hydrazide + hydroxylamine
D-gamma-glutamyl hydroxamate + hydroxyhydrazine
-
-
-
-
?
D-gamma-glutamyl-methylester + hydroxylamine
L-gamma-glutamyl hydroxamate + methanol
-
-
-
-
?
D-Gln + hydroxylamine
D-gamma-glutamyl hydroxamate + NH3
-
glutaminase A and B
-
?
gamma-ethyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + ethanol
-
-
-
-
?
gamma-glutamyl hydroxamate + NH2OH
?
-
36.3% of the activity with L-glutamine and H2O as co-substrate
-
-
?
gamma-glutamyl-hydroxamate + hydroxylamine
gamma-glutamyl hydroxamate + hydroxylamine
-
-
-
-
-
gamma-glutamyl-methoxyamide + H2O
Glu + N-hydroxy-O-methylhydroxylamine
-
-
-
-
?
gamma-glutamyl-methoxyamide + hydroxylamine
gamma-glutamyl hydroxamate + N-hydroxy-O-methylhydroxylamine
-
-
-
-
?
gamma-glutamyl-methylamide + hydroxylamine
gamma-glutamyl hydroxamate + N-methylhydroxylamine
-
-
-
-
?
gamma-L-glutamyl-4-nitroanilide + H2O
L-glutamate 4-nitroanilide + NH3
-
102% activity compared to L-glutamine
-
-
?
gamma-methyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + methanol
-
-
-
-
?
gamma-thioethyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + ?
-
-
-
-
?
gamma-thiomethyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + ?
-
-
-
-
?
L-Asn + H2O
L-aspartate + NH3
-
20.6% of the activity with L-glutamine and H2O as co-substrate
-
-
?
L-Asn + hydroxylamine
L-2-amino-4-(hydroxylamino)-4-oxobutanoic acid + NH3
-
-
-
-
?
L-gamma-glutamyl-anilide + hydroxylamine
L-gamma-glutamyl hydroxamate + aniline
-
-
-
-
?
L-gamma-glutamyl-hydrazide + hydroxylamine
L-gamma-glutamyl hydroxamate + hydroxyhydrazine
-
-
-
-
?
L-gamma-glutamyl-L-Ala + hydroxylamine
gamma-glutamyl hydroxamate + Ala
-
-
-
-
?
L-gamma-glutamyl-methylester + hydroxylamine
L-gamma-glutamyl hydroxamate + methanol
-
-
-
-
?
L-glutamic acid + NH2OH
gamma-glutamyl hydroxamate
-
0.9% of the activity with L-glutamine and H2O as co-substrate
-
-
?
L-glutamine + NH2OH
?
-
10.3% of the activity with L-glutamine and H2O as co-substrate
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
D-Asn + H2O
D-Asp + NH3
-
26% of the activity with L-Gln
-
-
?
D-asparagine + H2O
?
-
11% activity compared to L-glutamine
-
-
?
D-asparagine + H2O
D-aspartate + NH3
-
67% of the activity with L-glutamine
-
-
?
D-asparagine + H2O
D-aspartate + NH3
-
67% of the activity with L-glutamine
-
-
?
D-Gln + H2O
D-Glu + NH3
-
35% of the activity with L-Gln
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
24% activity compared to L-glutamine
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
24% activity compared to L-glutamine
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
48.5% activity compared to L-glutamine
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
48.5% activity compared to L-glutamine
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
8.1% of the activity with L-glutamine and H2O as co-substrate
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
75% of the activity with L-glutamine
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
75% of the activity with L-glutamine
-
-
?
gamma-glutamyl-methylamide + H2O
Glu + N-methylhydroxylamine
-
no activity
-
-
-
Gln + H2O
Glu + NH3
-
-
209009, 209010, 209012, 209013, 209015, 209016, 209017, 209018, 209019, 209028, 209029, 209030, 209031, 209033, 209034
-
-
?
L-Asn + H2O
L-Asp + NH3
-
77% of the activity with L-Gln
-
-
?
L-asparagine + H2O
?
-
93% activity compared to L-glutamine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
74% of the activity with L-glutamine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
74% of the activity with L-glutamine
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
L-glutamate 4-nitroanilide + NH3
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
L-glutamate 4-nitroanilide + NH3
-
-
-
?
L-gamma-glutamyl-methylester + H2O
L-Glu + methanol
-
no activity
-
-
-
L-Gln + H2O
L-Glu + NH3
-
enzyme plays a key role in urea synthesis by regulating provision of glutamate for synthesis of N-acetylglutamate, the obligatory cofactor of carbamoylphosphate synthetase
-
-
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-Gln + hydroxylamine
L-gamma-glutamyl hydroxamate + NH3
-
no activity
-
-
-
L-Gln + hydroxylamine
L-gamma-glutamyl hydroxamate + NH3
-
no activity
-
-
-
L-Gln + hydroxylamine
L-gamma-glutamyl hydroxamate + NH3
-
glutaminase A and B
-
?
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
-
-
-
?
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
-
-
-
?
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
-
-
-
?
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
Escherichia coli W3110 / ATCC 27325
-
-
-
?
L-glutamic acid + H2O
?
-
13.5% activity compared to L-glutamine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
PDX2 is a glutaminase that is involved in vitamin B6 biosynthesis
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
biosynthesis of pyridoxal-5’-phosphate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
synthesis of neurotransmitter glutamate and regulates the concentrations of glutamine and glutamate, ammonia detoxification
-
-
?
L-glutamine + H2O
L-glutamate + NH3
glutamate is an important source for neurotransmitter
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
glutamine synthesis pathway, overview, the intestinal and brain phosphate-activated glutaminase plays a role in the pathogenesis of hepatic encephalopathy, overview, PAG is increased in cirrhotics showing minimal hepatic encephalopathy and, therefore, could be implicated in the production of systemic hyperammonemia in these patients, PAG localized into the astrocytes is responsible for ammonia and free-radical production, PAG regulation mechanism, overview
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
intestinal glutaminase activity is increased in liver cirrhosis and correlates with minimal hepatic encephalopathy, relationship between enzyme activity, liver function, and porto-systemic shunts, overview
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
the enzyme plays a key role in energy and nitrogen metabolism, glutamate is a major excitatory neurotransmitter in neurons, especially in the cerebral cortex
-
-
?
L-glutamine + H2O
L-glutamate + NH3
the glutamate bindig pocket of the enzyme involves Glu381 and Tyr249, structure overview
-
-
?
L-glutamine + H2O
L-glutamate + NH3
strictly specific to L-glutamine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
neurotransmitter glutamate has been thought to derive mainly from glutamine via the action of glutaminase type 1, the GLS1 pathway is essential for maintaining the function of active synapses, knockout mice lacking brain/kidney phosphate-activated glutaminase have impaired glutamatergic synaptic transmission, altered breathing, disorganized goal-directed behavior and die shortly after birth
-
-
?
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
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
enzyme participates in an ATP-consuming cycle, plays a catabolic role in the degradation of glutamine to carbon skeletons, maintaining the optimal balance between glutamine and glutamate
-
-
ir
L-glutamine + H2O
L-glutamate + NH3
-
best substrate
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
Escherichia coli W3110 / ATCC 27325
-
-
-
?
additional information
?
-
-
no activity with glutamine and hydroxylamine as substrates, no formation of L-glutamate-gamma-monohydroxamate
-
-
-
additional information
?
-
-
the enzyme prefers free L-glutamine to free L-asparagine, C-terminal glutaminyl, and asparaginyl residues in peptides
-
-
-
additional information
?
-
-
the enzyme does not show any activity against L-Glu, D-Asn, L-Gln-Gly, gamma-glutamyl hydrazide, glutathione, and L-gamma-Glu-4-nitroanilide
-
-
-
additional information
?
-
-
the enzyme does not show any relative activity against L-asparagine, D-asparagine, and L-gamma-glutamyl-4-nitroanilide
-
-
-
additional information
?
-
-
the enzyme does not show any relative activity against L-asparagine, D-asparagine, and L-gamma-glutamyl-4-nitroanilide
-
-
-
additional information
?
-
the brain-specific BNIP-2-homology protein, BHIP-H is involved in enzyme regulation in neurons, loss of BNIP-H function could render glutamate excitotoxicity or/and deregulated glutamatergic activation, leading to ataxia, dystonia or other neurological disorders
-
-
-
additional information
?
-
-
multifunctional isozyme LGA interacts with PDZ domain proteins, e.g. alpha-1-syntrophin or glutaminase-interacting protein GIP, via specific short sequence motifs, interaction mechanism, overview
-
-
-
additional information
?
-
-
glutaminase as a potential component of the pathogenic process of human immunodeficiency virus associated dementia
-
-
-
additional information
?
-
-
involvement of essential Cys and His residues in the activity of isolated glutaminase from tumour cells
-
-
-
additional information
?
-
-
no hydrolysis of nicotinamide adenine dinucleotide, nicotinamide, and acetamide under the same experimental conditions as L-glutamine as substrate
-
-
-
additional information
?
-
-
no reaction with L-theanine, D-theanine, L-gamma-glutamylhydrazine, and L-gamma-glutamyl-p-nitroanilide
-
-
-
additional information
?
-
no reaction with L-theanine, D-theanine, L-gamma-glutamylhydrazine, and L-gamma-glutamyl-p-nitroanilide
-
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
L-Gln + H2O
L-Glu + NH3
-
enzyme plays a key role in urea synthesis by regulating provision of glutamate for synthesis of N-acetylglutamate, the obligatory cofactor of carbamoylphosphate synthetase
-
-
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
-
PDX2 is a glutaminase that is involved in vitamin B6 biosynthesis
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
biosynthesis of pyridoxal-5’-phosphate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
O14907
synthesis of neurotransmitter glutamate and regulates the concentrations of glutamine and glutamate, ammonia detoxification
-
-
?
L-glutamine + H2O
L-glutamate + NH3
O94925
glutamate is an important source for neurotransmitter
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
glutamine synthesis pathway, overview, the intestinal and brain phosphate-activated glutaminase plays a role in the pathogenesis of hepatic encephalopathy, overview, PAG is increased in cirrhotics showing minimal hepatic encephalopathy and, therefore, could be implicated in the production of systemic hyperammonemia in these patients, PAG localized into the astrocytes is responsible for ammonia and free-radical production, PAG regulation mechanism, overview
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
intestinal glutaminase activity is increased in liver cirrhosis and correlates with minimal hepatic encephalopathy, relationship between enzyme activity, liver function, and porto-systemic shunts, overview
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
the enzyme plays a key role in energy and nitrogen metabolism, glutamate is a major excitatory neurotransmitter in neurons, especially in the cerebral cortex
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
neurotransmitter glutamate has been thought to derive mainly from glutamine via the action of glutaminase type 1, the GLS1 pathway is essential for maintaining the function of active synapses, knockout mice lacking brain/kidney phosphate-activated glutaminase have impaired glutamatergic synaptic transmission, altered breathing, disorganized goal-directed behavior and die shortly after birth
-
-
?
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
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
enzyme participates in an ATP-consuming cycle, plays a catabolic role in the degradation of glutamine to carbon skeletons, maintaining the optimal balance between glutamine and glutamate
-
-
ir
additional information
?
-
-
the enzyme prefers free L-glutamine to free L-asparagine, C-terminal glutaminyl, and asparaginyl residues in peptides
-
-
-
additional information
?
-
O94925
the brain-specific BNIP-2-homology protein, BHIP-H is involved in enzyme regulation in neurons, loss of BNIP-H function could render glutamate excitotoxicity or/and deregulated glutamatergic activation, leading to ataxia, dystonia or other neurological disorders
-
-
-
additional information
?
-
-
glutaminase as a potential component of the pathogenic process of human immunodeficiency virus associated dementia
-
-
-
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
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
chloride
-
competes with phosphate for binding to the catalytic Ser291, at high concentration (500 mM NaCl) it can dislodge phosphate from its site and shift the protein equilibrium to lower-order oligomers
K+
KCl
Na+
NaCl
phosphate
PO43-
additional information
NaCl
-
enhances activity at 1-20% w/v, but reduces activity by 30% at 25% w/v, optimal at 1%
NaCl
-
enzyme is salt-tolerant as the relative activity displays 110% in the condition of 5% NaCl and remains over 50% in the presence of 20% NaCl
NaCl
-
salt-tolerant, 110% relative activity under 5% NaCl, 50% activity at 15% (w/v) concentration, over 50% activity with presence of 20% NaCl
NaCl
-
8-16%, maximal activity of glutaminase I, no effect of glutaminase II
NaCl
-
the enzyme is salt-tolerant, over 86% of maximal activity at 16% NaCl, no effect at 1 mM
NaCl
-
enzyme retains 40% of its activity in the presence of 15% NaCl, which is about 2fold higher than the activity of glutaminase from Aspergillus oryzae
phosphate
no activity without phosphate, max. activity at 60 mM K3PO4
additional information
-
the enzyme from strain RIB40 is salt-tolerant, while the enzyme from strain MA-27-IM is salt-sensitive
additional information
-
equivalent activities in absence and the presence of 3 M NaCl
additional information
-
the enzyme is salt-tolerant, the C-terminally truncated enzyme shows higher salt tolerance than the full-length enzyme, the N-terminal domain has abundant glutamic acid residues on its surface, which may explain its salt-tolerant mechanism
additional information
-
the enzyme is salt-tolerant, the C-terminally serine protease-cleaved enzyme fragment shows higher salt tolerance than the full-length enzyme, the N-terminal domain has abundant glutamic acid residues on its surface, which may explain its salt-tolerant mechanism
additional information
-
no effect with NaCl, no significant alteration with KCl, MgCl2, MnCl2, CaCl2 and NH4Cl
additional information
-
the enzyme is not affected by NiCl2 at 1 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-1-(2-formyl-3,6-dihydroxy-5-methoxycyclohexa-1,4-dien-1-yl)tridecan-2-yl acetate
-
-
(2R)-1-(2-hydroxy-5-methoxy-3,6-dioxocyclohexa-1,4-dien-1-yl)pentadecan-2-yl acetate
-
-
(2R)-1-(2-hydroxy-5-methoxy-3,6-dioxocyclohexa-1,4-dien-1-yl)tridecan-2-yl acetate
-
-
(2R)-1-(3,6-dihydroxy-5-methoxycyclohexa-1,4-dien-1-yl)tridecan-2-yl acetate
-
-
(2R)-1-[3-(acetyloxy)-6-hydroxy-5-methoxycyclohexa-1,4-dien-1-yl]pentadecan-2-yl acetate
-
-
(2R)-1-[3-(acetyloxy)-6-hydroxy-5-methoxycyclohexa-1,4-dien-1-yl]tridecan-2-yl acetate
-
-
2,2-dimethyl-5-[4-(methylsulfanyl)phenyl]-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
97% inhibition at 0.05 mM
2,2-dimethyl-5-[4-(naphthalen-1-yl)phenyl]-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
97% inhibition at 0.05 mM
2,2-dimethyl-5-[4-(propan-2-yl)phenyl]-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
91% inhibition at 0.05 mM
2-bromo-4-(2,2-dimethyl-4-oxo-1,2,3,4,5,6-hexahydrobenzo[a]phenanthridin-5-yl)-6-methoxyphenyl acetate
-
84% inhibition at 0.05 mM
5-(3-bromo-4,5-dimethoxyphenyl)-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
complete inhibition at 0.05 mM
5-(3-bromo-4-(dimethylamino)phenyl)-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
-
5-(3-chloro-4,5-dimethoxyphenyl)-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
88% inhibition at 0.05 mM
5-(4-tert-butylphenyl)-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
99% inhibition at 0.05 mM
5-[(6Z)-13-(3,5-dihydroxy-4-methylcyclohexa-1,4-dien-1-yl)tridec-6-en-1-yl]-2-methylbenzene-1,3-diol
-
-
5-[(6Z)-13-(3,5-dihydroxy-4-methylcyclohexa-1,4-dien-1-yl)tridec-6-en-1-yl]benzene-1,3-diol
-
-
5-[(6Z)-13-(3-hydroxy-5-methoxycyclohexa-1,4-dien-1-yl)tridec-6-en-1-yl]benzene-1,3-diol
-
-
5-[(7Z)-13-(3-hydroxy-5-methoxyphenyl)tridec-7-en-1-yl]-2-methylcyclohexa-1,4-diene-1,3-diol
-
-
5-[(7Z)-15-(3-hydroxy-5-methoxyphenyl)pentadec-7-en-1-yl]-2-methylcyclohexa-1,4-diene-1,3-diol
-
-
5-[(8Z)-15-(3,5-dihydroxy-4-methylcyclohexa-1,4-dien-1-yl)pentadec-8-en-1-yl]-2-methylbenzene-1,3-diol
-
-
5-[(8Z)-15-(3,5-dihydroxy-4-methylcyclohexa-1,4-dien-1-yl)pentadec-8-en-1-yl]benzene-1,3-diol
-
-
5-[(8Z)-15-(3-hydroxy-5-methoxycyclohexa-1,4-dien-1-yl)pentadec-8-en-1-yl]benzene-1,3-diol
-
-
5-[14-(3-hydroxy-5-methoxycyclohexa-1,4-dien-1-yl)tetradecyl]benzene-1,3-diol
-
-
5-[3-bromo-4-(dimethylamino)phenyl]-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
5-[4-(diethylamino)phenyl]-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
96% inhibition at 0.05 mM
5-[4-(dimethylamino)phenyl]-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
59% inhibition at 0.05 mM
5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]-N-[2-(4-phenylpiperidin-1-yl)ethyl]pentanamide
-
-
5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]-N-[2-(piperidin-1-yl)ethyl]pentanamide
-
-
5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]-N-[2-(pyrrolidin-1-yl)ethyl]pentanamide
-
-
5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]-N-[4-(trifluoromethyl)benzyl]pentanamide
-
-
8-[3-bromo-4-(diethylamino)phenyl]-11,11-dimethyl-8,10,11,12-tetrahydrobenzo[a][4,7]phenanthrolin-9(7H)-one
-
96% inhibition at 0.05 mM
8-[3-bromo-4-(dimethylamino)phenyl]-11,11-dimethyl-8,10,11,12-tetrahydrobenzo[a][4,7]phenanthrolin-9(7H)-one
-
91% inhibition at 0.05 mM
apomorphine
-
competitive inhibition, i.e. 5,6,6a,7-tetrahydro-6-methyl-4H-dibenzo[de,g]quinoline-10,11-diol
bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl) ethyl sulfide
-
i.e. BPTES, binds to an allosteric pocket at the dimer interface of kidney-type glutaminase, triggering a dramatic conformational change of the key loop (Glu312-Pro329) near the catalytic site and rendering it inactive, allosteric inhibition. Binding of BPTES stabilizes the inactive tetramers of the catalytic domain of kidney-type glutaminase. The binding mode of BPTES on the hydrophobic pocket determines its specificity to the kidney-type glutaminase isoform KGA
bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide
; inhibits specifically GLS1 and its splice variant GAC, two inhibitor molecules bind at an interface region of the GAC tetramer in a manner that appears to lock the GAC tetramer into a nonproductive conformation, binding structure and mechanism of glutaminase inhibition, overview; inhibits specifically GLS1 splice variant GAC, two inhibitor molecules bind at an interface region of the GAC tetramer in a manner that appears to lock the GAC tetramer into a nonproductive conformation, binding structure and mechanism of glutaminase inhibition, overview
bis-2-(5-phenylacetimido-1,2,4-thiadiazol-2-yl) ethyl sulfide
-
glutaminase-1-selective inhibitor
bis-2-(5-phenylacetimido-1,2,4-thiadiazol-2-yl)ethyl sulfide
-
uncompetitive inhibition
chelerythrine
-
competitive inhibition, i.e. 1,2-dimethoxy-N-methyl[1,3]benzodioxolo[5,6-c]phenanthridinium
dimethyl 2-[1-(4-tert-butylbenzoyl)-2,2,7-trimethyl-3-methylidene-2,3-dihydroquinolin-4(1H)-ylidene]-1,3-dithiole-4,5-dicarboxylate
-
97% inhibition at 0.05 mM
diphenylarsinic acid
-
the protein level of GAC significantly decrease in an concentration manner. The PAG activities are also decreased in parallel with the decrease in GAC
ebselen
-
mixed non-competitive inhibition, i.e. 2-phenyl-1,2-benzisoselenazol-3[2H]-one
iodoacetate
-
50 mM, strongly inhibited, 80% inhibition, especially more strongly with a progress of purification steps
N'-[(E)-[3-bromo-4-(dimethylamino)phenyl]methylidene]-2-(9-oxoacridin-10(9H)-yl)acetohydrazide
-
93% inhibition at 0.05 mM
N,N'-[sulfanediylbis(ethane-2,1-diyl-1,3,4-thiadiazole-5,2-diyl)]bis(2-phenylacetamide)
-
-
N-(2-aminoethyl)-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]pentanamide
-
-
N-(5-[2-[2-(5-amino-[1,3,4]thiadiazol-2-yl)-ethylsulfanyl]-ethyl]-[1,3,4]thiadiazol-2-yl)-2-phenyl-acetamide
-
-
N-methyl-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]-N-[2-(pyrrolidin-1-yl)ethyl]pentanamide
-
-
N-tert-butyl-N-methyl-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]pentanamide
-
-
N-[2-(1-methylpyrrolidin-2-yl)ethyl]-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]pentanamide
-
-
N-[2-(4-hydroxypiperidin-1-yl)ethyl]-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]pentanamide
-
-
N-[2-(diethylamino)ethyl]-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]pentanamide
-
-
N-[4-(dimethylamino)benzyl]-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]pentanamide
-
-
N-[4-[4-(5-amino-1,3,4-thiadiazol-2-yl)butyl]-1,3-thiazol-2-yl]-2-phenylacetamide
-
-
N-[5-(2-[[2-(5-amino-1,3,4-thiadiazol-2-yl)ethyl]sulfinyl]ethyl)-1,3,4-thiadiazol-2-yl]-2-phenylacetamide
-
-
N-[5-[2-(5-amino-1,3,4-thiadiazol-2-yl)ethyl]-1,3,4-thiadiazol-2-yl]-2-phenylacetamide
-
-
N-[5-[4-(5-amino-1,3,4-thiadiazol-2-yl)butyl]-1,3,4-thiadiazol-2-yl]-2-(4-fluorophenyl)acetamide
-
-
N-[5-[4-(5-amino-1,3,4-thiadiazol-2-yl)butyl]-1,3,4-thiadiazol-2-yl]-2-(4-methylphenyl)acetamide
-
-
N-[5-[4-(5-amino-1,3,4-thiadiazol-2-yl)butyl]-1,3,4-thiadiazol-2-yl]-2-cyclohexylacetamide
-
-
N-[5-[4-(5-amino-1,3,4-thiadiazol-2-yl)butyl]-1,3,4-thiadiazol-2-yl]-2-phenylacetamide
-
-
N-[5-[4-(5-amino-1,3,4-thiadiazol-2-yl)butyl]-1,3,4-thiadiazol-2-yl]-2-phenylpropanamide
-
-
N-[5-[4-(5-amino-1,3,4-thiadiazol-2-yl)butyl]-1,3,4-thiadiazol-2-yl]-3-phenylpropanamide
-
-
N-[5-[4-(5-amino-1,3,4-thiadiazol-2-yl)butyl]-1,3,4-thiadiazol-2-yl]benzamide
-
-
N-[5-[4-(5-amino-1,3,4-thiadiazol-2-yl)butyl]-1,3-thiazol-2-yl]-2-phenylacetamide
-
-
protein BNIP-H
i.e. Caytaxin or brain-specific BNIP-2-homology protein, encoded by gene ATCAY, important in neuromal function, inhibits the enzyme and alters its steady-state kinetics, relocalises glutaminase to neurite terminals and reduces glutamate levels in vivo, effects on glutamate levels in overexpressing cell lines, e.g. murine Neuro2A cells or rat PC-12 cells, or in female rat brain, detailed overview
-
5-[3-bromo-4-(dimethylamino)phenyl]-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
-
5-[3-bromo-4-(dimethylamino)phenyl]-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one
-
95% inhibition at 0.05 mM
6-diazo-5-oxo-L-norleucine
-
blockade of PAG, avoids the toxic effects of Gln accumulation in the brain
6-diazo-5-oxo-L-norleucine
-
active site inhibitor, about 53% inhibition at about 1 mM
6-diazo-5-oxo-L-norleucine
-
10 mM, strongly inhibited, 80% inhibition, especially more strongly with a progress of purification steps
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
diazo-5-oxo-L-norleucine
-
inactivates dimeric enzyme form in presence or absence of phosphate
L-glutamate
-
strong product inhibition of isozyme KGA, no inhibition of isozyme LGA
L-glutamine
-
product inhibition, strongly inhibits the membrane-associated enzyme, while the soluble form is not or weakly inhibited
NaCl
-
40% inhibition of the enzyme from strain RIB40 and 90% of the enzyme from strain MA-27-IM at 2.9 M, reduces the temperature stability of the enzyme
NaCl
-
the enzyme activity is inhibited by approximately 95% in the presence of 18% (w/v) NaCl
NaCl
-
enhances activity at 1-20% w/v, but reduces activity by 30% at 25% w/v, at 25% NaCl concentration, the enzyme retains 60% of its activity after 4 h
NaCl
-
inhibits the enzyme slightly at 2.6 M, the enzyme is salt-tolerant, the C-terminally serine protease-cleaved enzyme fragment shows higher salt tolerance than the full-length enzyme, the N-terminal domain has abundant glutamic acid residues on its surface, which may explain its salt-tolerant mechanism
p-mercuribenzoate
-
0.1 mM, complete inhibition, presence of Gln prevents inhibition
additional information
-
bis(diphenylarsine)oxide causes no siginficant changes in GAC levels and PAG activities. Methylated inorganic arsenics dimethylarsinic acid, dimethylarsinous acid, and phenyldimethylarsine oxide show no effects on GAC levels and PAG activities. And both glutathione-conjugated diphenylarsinic acid and triphenylarsine had no significant suppressive effects on the GAC levels and PAG activity
-
additional information
-
no inhibition by 2-mercaptomethanol and iodoacetate
-
additional information
-
no inhibition by HgCl2; no inhibition by p-chloromercuribenzoate
-
additional information
no inhibition by HgCl2; no inhibition by p-chloromercuribenzoate
-
additional information
-
activity is not significantly impaired with 2-oxoglutarate, pyruvate, succinate and citrate, no inhibition with L-glutamate, NH4+ and L-aspartate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Epidermal growth factor
-
kidney-type glutaminase activity in cells is stimulated by EGF
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
additional information
-
strong stimulation of glutaminase subunit TrpG activity by the associated synthase subunit TrpE within the glutamine amidotransferase, GATase, enzyme complex
-
phosphate
-
homogenate protein of SH-SY5Y cells: without phosphate about 12% L-glutamine hydrolysis at 150 mM 119 nmol/min, at 0 mM 14 nmol/min, soluble and membrane-associated enzyme forms are phosphate-activated, but without phosphate about 25% activity remains compared to the addition of 150 mM phosphate. In the brain protein fraction no L-glutamine hydrolysis is found without phosphate. N-PAG in whole cell homogenates in mitochondrial buffer is activated by high concentrations of phosphate, showing hyperbolic kinetics with a Ka of ca. 41 mM
phosphate
-
structure-based phosphate activation mechanism of GAC and GLS1/KGA, introducing the tetramerization-induced lifting of a gating loop essential for the phosphate-dependent activation process, overview. Phosphate binds inside the catalytic pocket rather than at the oligomerization interface. Phosphate also mediates substrate entry by competing with glutamate. GLS1/KGA is as effective as GLS2/LGA, but presents an eightfold gain in efficiency at 50 mM phosphate, with kcat-app/Km-app of 0.4 mM/s and 17.6 mM/s, respectively. One ion bound per monomer, buried inside the highly positive active site where it makes polar contacts with Ser291, Asn340 and Tyr471, and two water molecules
phosphate
-
100 mM, maximal activation and dimerization of the enzyme; dependent on
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
gamma-glutamyl hydroxamate
-
pH 9.0, at 37ºC, NH2OH as co-substrate
0.38
L-glutamine
-
polyacrylic acid-Cu2+-immobilized enzyme, at pH 8.0 and 50°C
0.4
L-glutamine
pH 8.5, temperature not specified in the publication, GAC mutant Y394L
1.4
L-glutamine
pH 8.5, temperature not specified in the publication, wild-type GAC
1.9
L-glutamine
pH 8.5, temperature not specified in the publication, isozyme GLS1
2.3
L-glutamine
-
pH 7.5, 30°C, full-length enzyme, in presence of 2.6 M NaCl
2.5
L-glutamine
pH 8.5, temperature not specified in the publication, GAC mutant F322S/F318Y
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
3.7
L-glutamine
-
pH 7.5, 30°C, protease-cleaved large enzyme fragment, in presence of 2.6 M NaCl
3.8
L-glutamine
-
pH 7.5, 30°C, protease-cleaved large enzyme fragment, in absence of NaCl
4
L-glutamine
pH 8.5, temperature not specified in the publication, isozyme GLS2
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
additional information
L-glutamate
-
7.5 mol/l, pH and temperature not specified in this publication
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
glutaminase activity steady-state enzyme kinetics of TrpG and the AS complex, generated by mixing the recombinant TrpE and TrpGD subunits
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
effect of pH on turnover number
-
2.5
L-glutamine
pH 8.5, temperature not specified in the publication, isozyme GLS2
10
L-glutamine
pH 8.5, temperature not specified in the publication, isozyme GLS1
20
L-glutamine
pH 8.5, temperature not specified in the publication, GAC mutant Y394L
22
L-glutamine
pH 8.5, temperature not specified in the publication, wild-type GAC
40
L-glutamine
pH 8.5, temperature not specified in the publication, GAC mutant F322S/F318Y
128
L-glutamine
-
pH 7.5, 30°C, full-length enzyme, in presence of 2.6 M NaCl
403.3
L-glutamine
-
pH 7.5, 30°C, full-length enzyme, in presence of 2.6 M NaCl
821.7
L-glutamine
-
pH 7.5, 30°C, protease-cleaved large enzyme fragment, in presence of 2.6 M NaCl
873.3
L-glutamine
-
pH 7.5, 30°C, protease-cleaved large enzyme fragment, in absence of NaCl
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.63
L-glutamine
pH 8.5, temperature not specified in the publication, isozyme GLS2
5.3
L-glutamine
pH 8.5, temperature not specified in the publication, isozyme GLS1
16
L-glutamine
pH 8.5, temperature not specified in the publication, wild-type GAC and GAC mutant F322S/F318Y
47
L-glutamine
pH 8.5, temperature not specified in the publication, GAC mutant Y394L
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000125
bis-2-(5-phenylacetimido-1,2,4-thiadiazol-2-yl)ethyl sulfide
-
pH and temperature not specified in the publication
additional information
L-glutamate
-
39.0 mol/l, pH and temperature not specified in this publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0231 - 0.05
(2R)-1-(2-formyl-3,6-dihydroxy-5-methoxycyclohexa-1,4-dien-1-yl)tridecan-2-yl acetate
0.0251 - 0.05
(2R)-1-(2-hydroxy-5-methoxy-3,6-dioxocyclohexa-1,4-dien-1-yl)pentadecan-2-yl acetate
0.05 - 0.5
(2R)-1-(2-hydroxy-5-methoxy-3,6-dioxocyclohexa-1,4-dien-1-yl)tridecan-2-yl acetate
0.00026 - 0.0029
(2R)-1-(3,6-dihydroxy-5-methoxycyclohexa-1,4-dien-1-yl)tridecan-2-yl acetate