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2-oxo-glutaramate + H2O
?
-
-
-
-
?
2-oxo-succinamate + H2O
?
-
-
-
-
?
5-methoxy-2,5-dioxopentanoic acid + H2O
methanol + 2-oxoglutaric acid
-
-
-
-
?
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
-
-
?
alpha-methyl-DL-Gln + H2O
?
-
-
-
-
?
beta-cyanoalanine + H2O
?
-
0.2% of the activity with L-Gln
-
-
?
Cbz-Gln-Gly + H2O
Cbz-Glu-Gly + NH3
-
-
-
-
?
Cbz-L-Gln + H2O
Cbz-L-Glu + NH3
-
-
-
-
?
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-asparagine + H2O
D-aspartate
44% activity
-
-
?
D-asparagine + H2O
D-aspartate + NH3
D-gamma-glutamyl-ethylester + H2O
D-Glu + ethanol
-
-
-
-
?
D-gamma-glutamyl-ethylester + hydroxylamine
D-gamma-glutamyl hydroxamate + ethanol
-
-
-
-
?
D-gamma-glutamyl-hydrazide + H2O
D-Glu + hydroxyhydrazine
-
-
-
-
?
D-gamma-glutamyl-hydrazide + hydroxylamine
D-gamma-glutamyl hydroxamate + hydroxyhydrazine
-
-
-
-
?
D-gamma-glutamyl-methylester + H2O
D-Glu + methanol
-
-
-
-
?
D-gamma-glutamyl-methylester + hydroxylamine
L-gamma-glutamyl hydroxamate + methanol
-
-
-
-
?
D-Gln + hydroxylamine
D-gamma-glutamyl hydroxamate + NH3
-
glutaminase A and B
-
?
D-glutamine + H2O
D-glutamate + NH3
D-theanine + H2O
D-glutamate + ethylamine
-
-
-
-
?
D-theanine + H2O
N-ethyl-D-glutamic acid
57% activity
-
-
?
gamma-ethyl glutamate + H2O
Glu + ethanol
-
-
-
-
?
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-hydrazide + H2O
Glu + hydroxyhydrazine
-
-
-
-
?
gamma-glutamyl-hydrazide + hydroxylamine
Glu + hydroxyhydrazine
-
-
-
-
?
gamma-glutamyl-hydroxamate + H2O
Glu + hydroxylamine
-
-
-
-
?
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 + H2O
Glu + N-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 + H2O
Glu + methanol
-
-
-
r
gamma-methyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + methanol
-
-
-
-
?
gamma-thioethyl glutamate + H2O
Glu + thioethanol
-
-
-
-
?
gamma-thioethyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + ?
-
-
-
-
?
gamma-thiomethyl glutamate + H2O
Glu + thiomethanol
-
-
-
-
?
gamma-thiomethyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + ?
-
-
-
-
?
Glu + hydroxylamine
gamma-glutamyl hydroxamate + H2O
-
-
-
-
?
glutaramate + H2O
?
-
-
-
-
?
Gly-Asn + H2O
Gly-Asp + NH3
-
-
-
-
?
Gly-Gln + H2O
Gly-Glu + NH3
-
-
-
-
?
L-Ala-Gln + H2O
L-Ala-L-Glu + NH3
-
-
-
-
?
L-albizziin + H2O
? + NH3
-
-
-
-
?
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-asparagine + H2O
L-aspartate
51% activity
-
-
?
L-asparagine + H2O
L-aspartate + NH3
L-gamma-Gln-methyl ester + H2O
L-Gln + methanol
-
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
L-glutamate 4-nitroanilide + NH3
L-gamma-glutamyl-anilide + H2O
L-Glu + aniline
-
-
-
-
?
L-gamma-glutamyl-anilide + hydroxylamine
L-gamma-glutamyl hydroxamate + aniline
-
-
-
-
?
L-gamma-glutamyl-ethylester + H2O
L-Glu + ethanol
-
-
-
-
?
L-gamma-glutamyl-hydrazide + H2O
L-Glu + hydroxyhydrazine
L-gamma-glutamyl-hydrazide + hydroxylamine
L-gamma-glutamyl hydroxamate + hydroxyhydrazine
-
-
-
-
?
L-gamma-glutamyl-L-Ala + H2O
?
-
-
-
-
?
L-gamma-glutamyl-L-Ala + hydroxylamine
gamma-glutamyl hydroxamate + Ala
-
-
-
-
?
L-gamma-glutamyl-L-epsilon-Lys + H2O
?
-
-
-
-
?
L-gamma-glutamyl-L-epsilon-Lys + hydroxylamine
?
-
-
-
-
?
L-gamma-glutamyl-L-Glu + H2O
?
-
-
-
-
?
L-gamma-glutamyl-L-Glu + hydroxylamine
?
-
-
-
-
?
L-gamma-glutamyl-methylester + H2O
L-Glu + methanol
L-gamma-glutamyl-methylester + hydroxylamine
L-gamma-glutamyl hydroxamate + methanol
-
-
-
-
?
L-gamma-glutamyl-p-nitroanilide + H2O
?
-
-
-
?
L-gamma-glutamylhydrazine + H2O
?
-
-
-
?
L-Gln + hydroxylamine
L-gamma-glutamyl hydroxamate + NH3
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
L-glutamic acid + NH2OH
gamma-glutamyl hydroxamate
-
0.9% of the activity with L-glutamine and H2O as co-substrate
-
-
?
L-glutamine + ethylamine
theanine + NH3
L-glutamine + H2O
L-glutamate + NH3
L-glutamine + H2O
L-glutamic acid + NH3
L-glutamine + NH2OH
?
-
10.3% of the activity with L-glutamine and H2O as co-substrate
-
-
?
L-glutaminyl-L-asparagine + H2O
?
L-isoglutamine + H2O
?
-
-
-
-
?
L-Leu-Ala-Asn + H2O
L-Leu-Ala-Asp + NH3
-
-
-
-
?
L-Leu-Gln-Gly + H2O
L-Leu-Glu-Gly + NH3
-
-
-
-
?
L-Leu-Gly-Asn + H2O
L-Leu-Gly-Asp + NH3
-
-
-
-
?
L-Pro-Leu-Gly-Asn + H2O
L-Pro-Leu-Gly-Asp + NH3
-
-
-
-
?
L-Pro-Leu-Gly-Gln + H2O
L-Pro-Leu-Gly-Glu + NH3
-
-
-
-
?
L-theanine + H2O
L-glutamate + ethylamine
-
-
-
-
?
L-theanine + H2O
N-ethyl-L-glutamic acid
71% activity
-
-
?
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
succinamate + H2O
?
-
-
-
-
?
additional information
?
-
D-Asn + H2O

D-Asp + NH3
-
26% of the activity with L-Gln
-
-
?
D-Asn + H2O
D-Asp + NH3
-
glutaminase A
-
-
?
D-asparagine + H2O

?
-
11% activity compared to L-glutamine
-
-
?
D-asparagine + H2O
?
-
11% activity compared to L-glutamine
-
-
?
D-asparagine + H2O

D-aspartate + NH3
-
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
-
-
-
-
?
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-Gln + H2O
D-Glu + NH3
-
glutaminase A
-
-
?
D-glutamine + H2O

D-glutamate + NH3
-
-
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
-
-
-
?
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
-
low activity
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
low activity
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
-
-
-
?
D-glutamine + H2O
D-glutamate + NH3
65% activity
-
-
?
D-glutamine + H2O
D-glutamate + NH3
92% activity
-
-
?
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
-
-
?
gamma-glutamyl-methylamide + H2O
Glu + N-methylhydroxylamine
-
-
-
-
?
Gln + H2O

Glu + NH3
-
-
-
-
?
Gln + H2O
Glu + NH3
-
-
-
-
?
Gln + H2O
Glu + NH3
Clostridium welchii
-
-
-
-
r
Gln + H2O
Glu + NH3
-
-
-
-
?
Gln + H2O
Glu + NH3
-
-
-
-
?
Gln + H2O
Glu + NH3
-
-
-
-
?
Gln + H2O
Glu + NH3
-
-
-
-
?
Gln + H2O
Glu + NH3
-
-
-
-
?
Gln + H2O
Glu + NH3
-
-
-
-
?
Gln + H2O
Glu + NH3
-
-
-
-
?
Gln + H2O
Glu + NH3
-
-
209009, 209010, 209012, 209013, 209015, 209016, 209017, 209018, 209019, 209028, 209029, 209030, 209031, 209033, 209034 -
-
?
Gln + H2O
Glu + NH3
-
-
-
-
?
L-Asn + H2O

L-Asp + NH3
-
77% of the activity with L-Gln
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
no activity
-
-
?
L-Asn + H2O
L-Asp + NH3
-
glutaminase A
-
-
?
L-asparagine + H2O

?
-
93% activity compared to L-glutamine
-
-
?
L-asparagine + H2O
?
-
93% activity compared to L-glutamine
-
-
?
L-asparagine + H2O

L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
reaction of EC 3.5.1.1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
reaction of EC 3.5.1.1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
reaction of EC 3.5.1.1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
reaction of EC 3.5.1.1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
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-hydrazide + H2O

L-Glu + hydroxyhydrazine
-
-
-
-
?
L-gamma-glutamyl-hydrazide + H2O
L-Glu + hydroxyhydrazine
-
-
-
-
?
L-gamma-glutamyl-methylester + H2O

L-Glu + methanol
-
no activity
-
-
?
L-gamma-glutamyl-methylester + H2O
L-Glu + methanol
-
-
-
-
?
L-Gln + H2O

L-Glu + NH3
-
-
-
-
?
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
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
constitutive enzyme
-
-
?
L-Gln + H2O
L-Glu + NH3
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
constitutive enzyme
-
-
?
L-Gln + H2O
L-Glu + NH3
-
glutaminase A and B
-
-
?
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
-
the enzyme produces myocardial Glu
-
-
?
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
-
-
-
-
?
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
-
-
-
?
L-glutamic acid + H2O

?
-
13.5% activity compared to L-glutamine
-
-
?
L-glutamic acid + H2O
?
-
13.5% activity compared to L-glutamine
-
-
?
L-glutamine + ethylamine

theanine + NH3
-
-
-
?
L-glutamine + ethylamine
theanine + NH3
-
-
-
?
L-glutamine + H2O

L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
PDX2 is a glutaminase that is involved in vitamin B6 biosynthesis
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
100% activity
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
100% activity
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
100% activity
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
100% activity
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
preferred substrate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
preferred substrate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
biosynthesis of pyridoxal-5â-phosphate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
glutamine metabolism
-
-
?
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
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
specifc for L-glutamine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
strictly specific to L-glutamine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
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
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
pH 7.2, 30°C
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
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
assay at pH 8
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
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
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
glutamine catabolism
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
best substrate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
best substrate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
Triticale sp.
-
glutamine catabolism
-
-
ir
L-glutamine + H2O

L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
Triticale sp.
-
-
-
-
?
L-glutaminyl-L-asparagine + H2O

?
-
-
-
-
?
L-glutaminyl-L-asparagine + H2O
?
-
-
-
-
?
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
-
-
-
?
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
?
-
-
no activity with D-asparagine
-
-
?
additional information
?
-
-
no activity with D-asparagine
-
-
?
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
?
-
-
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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(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-(5-methoxy-3,6-dioxocyclohexa-1,4-dien-1-yl)pentadecan-2-yl acetate
-
-
(2R)-1-(5-methoxy-3,6-dioxocyclohexa-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
-
-
(2S)-1-(5-methoxycyclohexa-1,4-dien-1-yl)heptan-2-ol
-
-
(2S)-2-amino-6-imino-5-oxohexanoic acid
-
1,2-naphthoquinone 4-sulfonate
-
-
1-amino-8-naphthol-2,4-disulfonic acid
-
weak
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
2,4-dinitro-1-naphthol-7-sulfonic acid
-
i.e. flavianic acid
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
2-hydroxy-5-methoxy-3-tridecylcyclohexa-2,5-diene-1,4-dione
-
-
2-methoxy-6-pentadecylcyclohexa-2,5-diene-1,4-dione
-
-
2-methoxy-6-tridecylcyclohexa-2,5-diene-1,4-dione
-
-
2-methyl-5-[(7Z)-pentadec-7-en-1-yl]cyclohexa-1,4-diene-1,3-diol
-
-
2-methyl-5-[(7Z)-tridec-7-en-1-yl]cyclohexa-1,4-diene-1,3-diol
-
-
2-phenyl isoindolin-1-one
-
-
2-phenylbenzo[d] isoxazol-3(2H)-one
-
-
2-phenylbenzo[d]isothiazol-3(2H)-one
-
-
3-[(2S)-2-hydroxypentadecyl]-5-methoxycyclohexa-2,5-dien-1-ol
-
-
4-hydroxy-2-methoxy-6-(2-oxopentadecyl)cyclohexa-2,5-dien-1-yl acetate
-
-
5,5'-(sulfanediyldiethane-2,1-diyl)bis(1,3,4-thiadiazol-2-amine)
-
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-[(7Z)-pentadec-7-en-1-yl]cyclohexa-1,4-diene-1,3-diol
-
-
5-[(7Z)-tridec-7-en-1-yl]cyclohexa-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
-
6-diazo-5-oxo-L-norleucine
6-diazo-5-oxo-Lnorleucine
-
time-dependent inhibition
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
Al3+
-
46% residual activity at 1 mM
anthraquinone-1,8-disulfonate
-
-
apomorphine
-
competitive inhibition, i.e. 5,6,6a,7-tetrahydro-6-methyl-4H-dibenzo[de,g]quinoline-10,11-diol
arsenate
-
0.5 M, 74% inhibition
azaserine
about 19% inhibition at about 1 mM
BaCl2
-
inhibition to a variable extent
bicarbonate
-
0.5 M, complete inhibition
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-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide
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
CaCl2
-
inhibition to a variable extent
CB-839
i.e. N-[5-[4-[6-[[2-[3-(trifluoromethoxy)phenyl]acetyl]amino]-3-pyridazinyl]butyl]-1,3,4-thiadiazol-2-yl]-2-pyridineacetamide, is the best inhibitor as designated by the binding free energy changes
Cd2+
-
complete inhibition at 50 mM
chelerythrine
-
competitive inhibition, i.e. 1,2-dimethoxy-N-methyl[1,3]benzodioxolo[5,6-c]phenanthridinium
citrate
-
enzyme from mesenteric lymph nodes
Cl-
-
0.5 M, complete inhibition
CN-
-
0.5 M, complete inhibition
CoCl2
-
14% inhibition at 1 mM
compound 968
-
i.e. 5-(3-bromo-4-(dimethylamino)phenyl)-2,2-dimethyl-2,3,5,6-tetrahydrobenzo[a]phenanthridin-4(1H)-one, combined with erlotinib down-regulates the glutamine and glycolysis metabolism in erlotinib-resistant non-small cell lung cancer cells
CuCl2
-
20% inhibition at 1 mM, 17% at 0.1 mM
CuSO4
-
inhibition to a variable extent
D-glucose
-
negative influence in media with glucose as carbon source
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
diphosphate
-
0.1 M, 98% inhibition
ebselen
-
mixed non-competitive inhibition, i.e. 2-phenyl-1,2-benzisoselenazol-3[2H]-one
glufosinate ammonium
about 23% inhibition at about 1 mM
L-Glutamic acid
Triticale sp.
-
5 mM, about a 40% inhibition
L-methionine sulfoximine
about 21% inhibition at about 1 mM
metformin
-
68% inhibition at 100 mM
methylene blue
-
0.005%, irreversible inactivation
MgCl2
-
20% inhibition at 1 mM, 12% at 0.1 mM
MnCl2
-
22% inhibition at 1 mM, 13% at 0.1 mM
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-benzyl-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]pentanamide
-
N-bromosuccinimide
-
5 mM, 19% of initial activity
N-methyl-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]-N-[2-(pyrrolidin-1-yl)ethyl]pentanamide
-
N-tert-butyl-5-[5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl]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
-
Na2SO4
-
glutaminase I and II
NaCIO4
-
0.3 M, 25% inhibition
NaF
-
inhibition to a variable extent
NaH2PO4
-
0.3 M, complete inhibition
NaN3
-
complete inhibition at 1 mM
NaNO3
-
0.3 M, 15% inhibition
Ngamma,Ngamma-diethyl-L-glutamine
-
-
Ngamma,Ngamma-dimethyl-L-glutamine
-
-
Ngamma-ethyl-L-glutamine
-
-
Ngamma-methyl-L-glutamine
-
-
nitrite
-
0.5 M, complete inhibition
O-(diazoacetyl)-L-serine
-
-
p-chloromercuribenzoate
-
p-chloromercuribenzoic acid
-
complete inhibition at 10 mM
Pb2+
-
69.27% residual activity at 100 mM
phenylarsonic acid
-
causes a decrease in GAC levels
phenylmethylarsinic acid
-
causes a decrease in GAC levels
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
-
R(-)-propylnorapomorphine
-
-
Rose bengal
-
0.01%, irreversible inactivation
succinate
-
enzyme from mesenteric lymph nodes
TLCK
-
5 mM, 12% of initial activity
Tris
-
0.5 M, complete inhibition
ZnCl2
-
7% inhibition at 1 mM
2-oxoglutarate

-
enzyme from mesenteric lymph nodes
2-oxoglutarate
-
competitive inhibition
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

-
-
6-diazo-5-oxo-L-norleucine
-
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
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
-
-
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
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
-
bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide

-
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
Ca2+

-
10 mM, 80% of initial activity
Ca2+
-
72.59% residual activity at 100 mM
Ca2+
-
0.5-1.0 mM, NEM-sensitive enzyme
Co2+

-
90% residual activity at 1 mM
Co2+
-
70.53% residual activity at 100 mM
Co2+
-
5 mM, 81% of initial activity
Cu2+

-
10 mM, 44% of initial activity
Cu2+
-
complete inhibition at 50 mM
Cu2+
-
5 mM, 86% of initial activity
Cu2+
-
CuCl2, inhibition of glutaminase II
diazo-5-oxo-L-norleucine

-
enzyme from mesenteric lymph nodes
diazo-5-oxo-L-norleucine
-
inactivates dimeric enzyme form in presence or absence of phosphate
dithiothreitol

-
complete inhibition at 1 mM
dithiothreitol
-
5 mM, 82% of initial activity
EDTA

-
80% residual activity at 1 mM
EDTA
-
glutaminase I and II
EDTA
-
10% inhibition at 1 mM
Fe2+

-
0.1 mM, 55% of initial activity
Fe2+
-
92% residual activity at 1 mM
Fe2+
-
5 mM, 83% of initial activity
Fe3+

-
0.1 mM, 45% of initial activity
Fe3+
-
5 mM, 84% of initial activity
glutamate

-
no inhibition
glutamate
-
no inhibition
glutamate
-
inhibits the enzyme in vivo in tumor cells at 100 mM
glutamate
-
competitive with respect to Gln
Hg2+

-
10 mM, 35% of initial activity
Hg2+
-
complete inhibition at 50 mM
Hg2+
-
5 mM, 61% of initial activity
Hg2+
-
0.1 mM, complete inhibition
HgCl2

-
inhibition to a variable extent
iodoacetamide

-
complete inhibition at 50 mM
iodoacetamide
-
5 mM, 3% of initial activity
iodoacetate

-
10 mM, 23% of initial activity
iodoacetate
-
50 mM, strongly inhibited, 80% inhibition, especially more strongly with a progress of purification steps
L-glutamate

-
product inhibition, competitive
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
L-glutamine
inhibition of enzyme activity in tumor tissue
L-glutamine
Triticale sp.
-
above 0.3 mM
Mersalyl

-
enzyme from mesenteric lymph nodes
Mersalyl
-
0.5 mM, almost complete inhibition
Mersalyl
-
0.5 mM, almost complete inhibition
Mg2+

-
10 mM, 55% of initial activity
Mg2+
-
74.29% residual activity at 100 mM
Mn2+

-
0.1 mM, 75% of initial activity
Mn2+
-
80% residual activity at 1 mM
Mn2+
-
76.23% residual activity at 100 mM
N-ethylmaleimide

-
10 mM, 60% of initial activity
N-ethylmaleimide
-
5 mM, 8% of initial activity
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
-
15%, remains 90% of the initial activity
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
NEM

-
-
NEM
-
enzyme from mesenteric lymph nodes
NEM
-
enzyme exists as an NEM-sensitive form and an NEM-insensitive form
NEM
-
1 mM, almost completely blocks activity
NEM
-
enzyme exists as an NEM-sensitive form and an NEM-insensitive form
NH3

-
product inhibition, 10 mM inhibits the enzyme activity about 30%
NH4+

-
-
NH4+
-
enzyme from mesenteric lymph nodes
NH4+
Triticale sp.
-
0.01 M, 50% inhibition
p-mercuribenzoate

-
-
p-mercuribenzoate
-
0.1 mM, complete inhibition, presence of Gln prevents inhibition
PCMB

-
inhibition of glutaminase I but not glutaminase II
pyruvate

-
mixed inhibition
pyruvate
-
0.5 M, complete inhibition
Zn2+

-
10 mM, 30% of initial activity
Zn2+
-
82.12% residual activity at 100 mM
Zn2+
-
5 mM, 79% of initial activity
additional information

-
not inhibited by EDTA
-
additional information
-
phenylmethylsulfonyl fluoride, sodium azide, ethylenediaminetetraacetic acid and N-acetylimidazole have no effect on enzyme
-
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
-
no inhibited by glutamate
-
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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0.195
2-oxo-glutaramate
-
pH 8.5, 30°C
0.003 - 0.017
2-oxo-succinamate
0.012
5-methoxy-2,5-dioxopentanoic acid
-
pH 7.2, 30°C
6.7
D-gamma-Gln-methylester
-
glutaminase B
83
D-glutamine
-
pH 9.0, at 37ºC, H2O as co-substrate
0.92
D-theanine
-
glutaminase B
50
gamma-ethyl glutamate
-
-
12
gamma-glutamyl hydrazide
-
-
15
gamma-glutamyl hydroxamate
-
pH 9.0, at 37ºC, NH2OH as co-substrate
3.3
gamma-glutamyl methylamide
-
-
64
gamma-methyl glutamate
-
-
23
gamma-thioethyl glutamate
-
-
10
gamma-thiomethyl glutamate
-
-
2.1
L-gamma-Gln-methyl ester
-
glutaminase B
200
L-gamma-glutamyl-L-Ala
-
glutaminase B
2.8
L-glutamate
-
pH 7.0, 37°C
500
L-Glutamic acid
-
pH 9.0, at 37ºC, NH2OH as co-substrate
0.71
L-Theanine
-
glutaminase B
additional information
L-glutamate
0.003
2-oxo-succinamate

-
pH 7.2, 30°C
0.017
2-oxo-succinamate
-
pH 8.5, 30°C
0.42
Gln

-
-
2.07
Gln
-
in presence of 50 mM phosphate
2.42
Gln
-
without phosphate
2.6
Gln
-
in presence of 10 mM phosphate
2.63
Gln
-
in presence of 100 mM phosphate
4.1
Gln
-
in presence of 100 mM phosphate
5
Gln
-
in presence of 150 mM phosphate
6
Gln
-
membrane-bound enzyme form
14
Gln
-
in presence of 10 mM phosphate
21
Gln
-
soluble enzyme form
4.8
glutamine

-
at 50ºC, pH 7.0
19.5
glutamine
Km apparent, no Michaelis-Menten kinetics
109.5
glutamine
Km apparent, no Michaelis-Menten kinetics
1.27
Glutaramate

-
pH 8.5, 30°C
1.48
Glutaramate
-
pH 7.2, 30°C
4.8
L-Asn

-
-
24
L-Asn
-
pH 9.0, at 37ºC, H2O as co-substrate
0.1
L-asparagine

mutant Q63E, pH 7.5, 37°C
0.23
L-asparagine
mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C
0.25
L-asparagine
mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C
0.25
L-asparagine
mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C
0.29
L-asparagine
wild-type, pH 7.5, 37°C
2.6
L-Gln

-
-
4.4
L-Gln
-
glutaminase I
6.5
L-Gln
-
glutaminase II
0.0053
L-glutamine

-
-
0.104
L-glutamine
pH 9.0, 70°C
0.24
L-glutamine
-
pH 11.0, 70°C
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
0.49
L-glutamine
-
free enzyme, at pH 8.0 and 50°C
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
L-glutamine
-
lower than, soluble and membrane-associated N-PAG, 37°C, pH 8.6
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
-
brain, membrane-associated PAG, 37°C, pH 8.6
4
L-glutamine
pH 8.5, temperature not specified in the publication, isozyme GLS2
4.5
L-glutamine
-
pH 7.5, 37°C
4.5
L-glutamine
-
pH 7.0, 30°C
4.5
L-glutamine
-
pH 7.0, 37°C
5.74
L-glutamine
-
pH not specified in the publication, temperature not specified in the publication
6.1
L-glutamine
-
pH 7.5, 30°C, full-length enzyme, in absence of NaCl
6.2
L-glutamine
-
mutant enzyme E160D
6.25
L-glutamine
-
at pH 7.5 and 35°C
6.4
L-glutamine
-
recombinant enzyme with N-terminal and C-terminal deletions, T-acetate buffer, pH 8.0
6.6
L-glutamine
-
wild-type enzyme
7.9
L-glutamine
-
recombinant enzyme with N-terminal deletion, T-acetate buffer, pH 8.0
8.1
L-glutamine
-
native enzyme, T-phosphate buffer, pH 8.0
8.5
L-glutamine
mutant Q162A
9.5
L-glutamine
-
pH 9.0, at 37ºC, H2O as co-substrate
11
L-glutamine
-
mutant enzyme Y191F
12.2
L-glutamine
1 mol/l NaCl present
14
L-glutamine
-
native enzyme, T-acetate buffer, pH 8.0
17
L-glutamine
-
pH 9.0, at 37ºC, NH2OH as co-substrate
23.7
L-glutamine
mutant G261A
26
L-glutamine
-
brain, soluble PAG, 37°C, pH 8.6
26.6
L-glutamine
Km apparent, no Michaelis-Menten enzyme
46.4
L-glutamine
wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C
76.5
L-glutamine
mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C
460
L-glutamine
-
mutant enzyme Y191T
0.14
succinamate

-
pH 8.5, 30°C
0.23
succinamate
-
pH 7.2, 30°C
additional information
L-glutamate

-
7.5 mol/l, pH and temperature not specified in this publication
additional information
additional information
-
effect of pH on Km-value
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics, overview
-
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
-
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