Information on EC 3.5.1.2 - glutaminase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.5.1.2
-
RECOMMENDED NAME
GeneOntology No.
glutaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-glutamine + H2O = L-glutamate + NH3
show the reaction diagram
mechanism
-
L-glutamine + H2O = L-glutamate + NH3
show the reaction diagram
active site structure, the enzyme contains a catalytic dyad formed by S64 and K67
-
L-glutamine + H2O = L-glutamate + NH3
show the reaction diagram
structure-function relationship and catalytic mechanism, detailed overview
-
L-glutamine + H2O = L-glutamate + NH3
show the reaction diagram
active site structure, the enzyme contains a catalytic dyad formed by S64 and K67
Micrococcus luteus K-3
-
-
L-glutamine + H2O = L-glutamate + NH3
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
Arginine and proline metabolism
-
citrulline biosynthesis
-
D-Glutamine and D-glutamate metabolism
-
glutamine degradation I
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamine amidohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AoGls
Q66V97
-
GAC
O94925
splice variant of GLS1
GLNase
P13264
-
GLS
-
-
-
-
GLS
O94925
-
GLS1
-
-
GLS1
O94925
-
GlsA
Bacillus licheniformis DSM13
Q65NY1
-
-
glutaminase
Q8YMZ9, Q8YSZ5
-
glutaminase
O07637, O31465
-
glutaminase
Bacillus subtilis 168
O07637, O31465
-
-
glutaminase
P0A6W0, P77454
-
glutaminase
Escherichia coli W3110
P0A6W0, P77454
-
-
glutaminase
-
-
glutaminase
-
two isoforms: GAC, KGA
glutaminase
-
-
glutaminase
P13264
-
glutaminase
P73903
-
glutaminase 1
O94925
-
glutaminase 2
-
-
glutaminase A
-
-
glutaminase A
Micrococcus luteus K-3
-
-
-
glutaminase A
Q9I387
-
glutaminase A
-
-
glutaminase B
-
-
glutaminase C
-
-
glutaminase C
-
a splicing variant of the kidney-type glutaminase and has the enzyme activity of the phosphate-activated glutaminase
glutaminase I
-
-
-
-
glutaminase K
-
-
glutaminase K
-
-
glutaminase L
-
-
glutaminase L
O14907
-
glutaminase L
-
-
glutamine amidohydrolase
-
-
glutamine aminohydrolase
-
-
-
-
glutamine deamidating enzyme
-
-
K-glutaminase
-
-
-
-
K-glutaminase
O94925
-
KGA
O94925
-
kidney-type glutaminase
-
-
kidney-type glutaminase
O94925
-
kidney-type glutaminase
-
-
kidney-type glutaminase
Rattus norvegicus Sprague-Dawley
-
-
-
kidney-type-glutaminase
-
-
L-glutaminase
-
-
-
-
L-glutaminase
-
-
L-glutaminase
Bacillus sp. LKG-01
-
-
-
L-glutaminase
-
-
L-glutaminase
Streptomyces rimosus LG-10
-
-
-
L-glutamine amidohydrolase
-
-
-
-
L-glutamine amidohydrolase
-, Q9I387
-
L-glutamine amidohydrolase
-
-
liver-type glitaminase
-
-
liver-type glutaminase
-
-
liver-type glutaminase
-
-
Mglu
Q4U1A6
-
Micrococcus glutaminase Mglu
Q4U1A6
-
Micrococcus luteus K-3-type glutaminase
-
only from strain RIB40, not from strain MA-27-IM
Micrococcus luteus K-3-type glutaminase
Q66V97
-
mitochondrial glutaminase
-
-
N-PAG
-
-
neuroblastoma glutaminase
-
-
neuroblastoma PAG
-
-
Nit 2
-
-
nitrilase 2
-
-
omega-amidase
-
-
PAG
-
-
-
-
PAG
O14907
-
phosphate activated glutaminase
-
-
-
-
phosphate activated glutaminase
-
-
phosphate-activated glutaminase
-
-
phosphate-activated glutaminase
-
-
phosphate-activated glutaminase
O14907
-
phosphate-activated glutaminase
-
-
phosphate-activated L-glutamine amidohydrolase
-
-
salt-tolerant glutaminase
-
-
salt-tolerant glutaminase
Q4U1A6
-
salt-tolerant glutaminase
Micrococcus luteus K-3
-
;
-
salt-tolerant glutaminase
-
-
salt-tolerant glutaminase
Stenotrophomonas maltophilia NYW-81
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-47-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain PCC 7120
SwissProt
Manually annotated by BRENDA team
strain RIB40
SwissProt
Manually annotated by BRENDA team
strains RIB40 and MA-27-IM
-
-
Manually annotated by BRENDA team
ATCC 14580
UniProt
Manually annotated by BRENDA team
Bacillus licheniformis DSM13
ATCC 14580
UniProt
Manually annotated by BRENDA team
MTCC 10401, isolated from Gangotri region of Uttarakhand Himalaya
-
-
Manually annotated by BRENDA team
Bacillus sp. LKG-01
MTCC 10401, isolated from Gangotri region of Uttarakhand Himalaya
-
-
Manually annotated by BRENDA team
strain 168, ATCC 23857D-5
SwissProt
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168, ATCC 23857D-5
SwissProt
Manually annotated by BRENDA team
Clostridium welchii
-
-
-
Manually annotated by BRENDA team
gene CagahA
-
-
Manually annotated by BRENDA team
Cryptococcus albidus ATCC20293
gene CagahA
-
-
Manually annotated by BRENDA team
Cryptococcus flavescens NISL 3771
gene CngahA
-
-
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
production of significant amounts of enzyme only after the stage of rapid exponential growth
-
-
Manually annotated by BRENDA team
strain W3110
SwissProt
Manually annotated by BRENDA team
Escherichia coli W3110
strain W3110
SwissProt
Manually annotated by BRENDA team
male White Leghorn chicken
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GAC; GAC, a splice variant of isozyme GLS1; GLS1; isozyme GLS1
SwissProt
Manually annotated by BRENDA team
isozyme GLS2
-
-
Manually annotated by BRENDA team
kidney-type glutaminase isoform KGA
-
-
Manually annotated by BRENDA team
kidney-type glutaminase isozyme
SwissProt
Manually annotated by BRENDA team
kidney-type glutaminase, KGA or GLS1, glutaminase C, GAC, a splice variant of the gene gls encoding GLS1, and liver-type glutaminase GLS2
-
-
Manually annotated by BRENDA team
phosphate-activated isozyme, kidney type isozyme K-PAG and the hepatic type isozyme L-PAG
-
-
Manually annotated by BRENDA team
two isozymes, glutaminase K and L, i.e. LGA and KGA
-
-
Manually annotated by BRENDA team
two isozymes, glutaminase K and L, i.e. LGA and KGA, or liver-type isozyme and kidney-type isozyme
-
-
Manually annotated by BRENDA team
strain K-3, glutaminase I and II
-
-
Manually annotated by BRENDA team
Micrococcus luteus K-3
-
-
-
Manually annotated by BRENDA team
Micrococcus luteus K-3
strain K-3
-
-
Manually annotated by BRENDA team
Micrococcus luteus K-3
strain K-3, glutaminase I and II
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Gallus gallus
no liver-type isozyme, LGA, activity in the brain
-
-
Manually annotated by BRENDA team
IFO 3080
SwissProt
Manually annotated by BRENDA team
ATCC 21025
-
-
Manually annotated by BRENDA team
adult Wistar
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
male Wistar
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats, female
UniProt
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Stenotrophomonas maltophilia NYW-81
strain NYW-81
-
-
Manually annotated by BRENDA team
strain LG-10, isolated from the estuarine fish Chanos chanos, from gills, skin, and gut contents
-
-
Manually annotated by BRENDA team
Streptomyces rimosus LG-10
strain LG-10, isolated from the estuarine fish Chanos chanos, from gills, skin, and gut contents
-
-
Manually annotated by BRENDA team
gene trpG
-
-
Manually annotated by BRENDA team
Triticale sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to a distinct type of glutaminase with an amidase signature sequence forming a distinct family
evolution
Cryptococcus albidus ATCC20293, Cryptococcus flavescens NISL 3771
-
the enzyme belongs to a distinct type of glutaminase with an amidase signature sequence forming a distinct family
-
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
-
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
-, Q65NY1
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
Bacillus licheniformis DSM13
-
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
-
metabolism
-
glutaminase C is the first enzyme in glutaminolysis
additional information
-
Ile221-Leu533 is the catalytic domain of kidney-type glutaminase
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-glutaramate + H2O
?
show the reaction diagram
-
-
-
-
?
2-oxo-succinamate + H2O
?
show the reaction diagram
-
-
-
-
?
4-monomethyl-2-oxoglutarate + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-methyl-DL-Gln + H2O
?
show the reaction diagram
-
-
-
-
?
beta-cyanoalanine + H2O
?
show the reaction diagram
-
0.2% of the activity with L-Gln
-
-
?
D-Asn + H2O
D-Asp + NH3
show the reaction diagram
-
glutaminase A
-
-
?
D-Asn + H2O
D-Asp + NH3
show the reaction diagram
-
26% of the activity with L-Gln
-
-
?
D-Asn + H2O
D-aspartate + NH3
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia NYW-81
-
67% of the activity with L-glutamine
-
-
?
D-asparagine + H2O
D-aspartate
show the reaction diagram
-, Q9I387
44% activity
-
-
?
D-gamma-glutamyl-ethylester + H2O
D-Glu + ethanol
show the reaction diagram
-
-
-
-
?
D-gamma-glutamyl-ethylester + hydroxylamine
D-gamma-glutamyl hydroxamate + ethanol
show the reaction diagram
-
-
-
-
?
D-gamma-glutamyl-hydrazide + H2O
D-Glu + hydroxyhydrazine
show the reaction diagram
-
-
-
-
?
D-gamma-glutamyl-hydrazide + hydroxylamine
D-gamma-glutamyl hydroxamate + hydroxyhydrazine
show the reaction diagram
-
-
-
-
?
D-gamma-glutamyl-methylester + H2O
D-Glu + methanol
show the reaction diagram
-
-
-
-
?
D-gamma-glutamyl-methylester + hydroxylamine
L-gamma-glutamyl hydroxamate + methanol
show the reaction diagram
-
-
-
-
?
D-Gln + H2O
D-Glu + NH3
show the reaction diagram
-
glutaminase A
-
-
?
D-Gln + H2O
D-Glu + NH3
show the reaction diagram
-
35% of the activity with L-Gln
-
-
?
D-Gln + hydroxylamine
D-gamma-glutamyl hydroxamate + NH3
show the reaction diagram
-
glutaminase A and B
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
-
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
low activity
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
8.1% of the activity with L-glutamine and H2O as co-substrate
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-, Q9I387
65% activity
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-, Q9I387
92% activity
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
75% of the activity with L-glutamine
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
Bacillus sp. LKG-01
-
low activity
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
Stenotrophomonas maltophilia NYW-81
-
75% of the activity with L-glutamine
-
-
?
D-theanine + H2O
D-glutamate + ethylamine
show the reaction diagram
-
-
-
-
?
D-theanine + H2O
N-ethyl-D-glutamic acid
show the reaction diagram
-, Q9I387
57% activity
-
-
?
gamma-ethyl glutamate + H2O
Glu + ethanol
show the reaction diagram
-
-
-
-
?
gamma-ethyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + ethanol
show the reaction diagram
-
-
-
-
?
gamma-glutamyl hydroxamate + NH2OH
?
show the reaction diagram
-
36.3% of the activity with L-glutamine and H2O as co-substrate
-
-
?
gamma-glutamyl-hydrazide + H2O
Glu + hydroxyhydrazine
show the reaction diagram
-
-
-
-
?
gamma-glutamyl-hydrazide + hydroxylamine
Glu + hydroxyhydrazine
show the reaction diagram
-
-
-
-
?
gamma-glutamyl-hydroxamate + H2O
Glu + hydroxylamine
show the reaction diagram
-
-
-
-
?
gamma-glutamyl-hydroxamate + hydroxylamine
gamma-glutamyl hydroxamate + hydroxylamine
show the reaction diagram
-
-
-
-
-
gamma-glutamyl-methoxyamide + H2O
Glu + N-hydroxy-O-methylhydroxylamine
show the reaction diagram
-
-
-
-
?
gamma-glutamyl-methoxyamide + hydroxylamine
gamma-glutamyl hydroxamate + N-hydroxy-O-methylhydroxylamine
show the reaction diagram
-
-
-
-
?
gamma-glutamyl-methylamide + H2O
Glu + N-methylhydroxylamine
show the reaction diagram
-
-
-
-
?
gamma-glutamyl-methylamide + H2O
Glu + N-methylhydroxylamine
show the reaction diagram
-
no activity
-
-
-
gamma-glutamyl-methylamide + hydroxylamine
gamma-glutamyl hydroxamate + N-methylhydroxylamine
show the reaction diagram
-
-
-
-
?
gamma-methyl glutamate + H2O
Glu + methanol
show the reaction diagram
-
-
-
r
gamma-methyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + methanol
show the reaction diagram
-
-
-
-
?
gamma-thioethyl glutamate + H2O
Glu + thioethanol
show the reaction diagram
-
-
-
-
?
gamma-thioethyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + ?
show the reaction diagram
-
-
-
-
?
gamma-thiomethyl glutamate + H2O
Glu + thiomethanol
show the reaction diagram
-
-
-
-
?
gamma-thiomethyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + ?
show the reaction diagram
-
-
-
-
?
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
?
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
?
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
?
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
-
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
?
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
?
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
?
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
-
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
?
Gln + H2O
Glu + NH3
show the reaction diagram
Clostridium welchii
-
-
-
-
r
Gln + H2O
Glu + NH3
show the reaction diagram
-
-
-
-
?
Gln + H2O
Glu + NH3
show the reaction diagram
Micrococcus luteus K-3
-
-
-
-
?
Glu + hydroxylamine
gamma-glutamyl hydroxamate + H2O
show the reaction diagram
-
-
-
-
?
glutaramate + H2O
?
show the reaction diagram
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
show the reaction diagram
-
no activity
-
-
-
L-Asn + H2O
L-Asp + NH3
show the reaction diagram
-
glutaminase A
-
-
?
L-Asn + H2O
L-Asp + NH3
show the reaction diagram
-
77% of the activity with L-Gln
-
-
?
L-Asn + H2O
L-aspartate + NH3
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia NYW-81
-
74% of the activity with L-glutamine
-
-
?
L-asparagine + H2O
L-aspartate
show the reaction diagram
-, Q9I387
51% activity
-
-
?
L-gamma-glutamyl-anilide + H2O
L-Glu + aniline
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-anilide + hydroxylamine
L-gamma-glutamyl hydroxamate + aniline
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-ethylester + H2O
L-Glu + ethanol
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-hydrazide + H2O
L-Glu + hydroxyhydrazine
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-hydrazide + H2O
L-Glu + hydroxyhydrazine
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-hydrazide + hydroxylamine
L-gamma-glutamyl hydroxamate + hydroxyhydrazine
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-L-Ala + hydroxylamine
gamma-glutamyl hydroxamate + Ala
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-L-epsilon-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-L-epsilon-Lys + hydroxylamine
?
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-L-Glu + H2O
?
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-L-Glu + hydroxylamine
?
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-methylester + H2O
L-Glu + methanol
show the reaction diagram
-
-
-
-
-
L-gamma-glutamyl-methylester + H2O
L-Glu + methanol
show the reaction diagram
-
no activity
-
-
-
L-gamma-glutamyl-methylester + hydroxylamine
L-gamma-glutamyl hydroxamate + methanol
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-p-nitroanilide + H2O
?
show the reaction diagram
-, Q9I387
-
-
-
?
L-gamma-glutamylhydrazine + H2O
?
show the reaction diagram
-, Q9I387
-
-
-
?
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
-
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
-
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
glutaminase A and B
-
-
?
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
constitutive enzyme
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
contribution of the enzyme to elevated extracellular Glu at 24 h after onset of focal ischemia
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
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
show the reaction diagram
-
high glutaminase activity may be of importance for optimal insulin secretion elicited by amino acid secretagogues
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme produces myocardial Glu
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
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 + H2O
L-Glu + NH3
show the reaction diagram
Micrococcus luteus K-3
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
Micrococcus luteus K-3
-
constitutive enzyme
-
-
-
L-Gln + hydroxylamine
L-gamma-glutamyl hydroxamate + NH3
show the reaction diagram
-
-
-
-
?
L-Gln + hydroxylamine
L-gamma-glutamyl hydroxamate + NH3
show the reaction diagram
-
no activity
-
-
-
L-Gln + hydroxylamine
L-gamma-glutamyl hydroxamate + NH3
show the reaction diagram
-
glutaminase A and B
-
?
L-Gln + hydroxylamine
L-gamma-glutamyl hydroxamate + NH3
show the reaction diagram
Micrococcus luteus K-3
-
no activity
-
-
-
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
P0A6W0, P77454
-
-
-
?
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
O07637, O31465
-
-
-
?
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
Bacillus subtilis 168
O07637, O31465
-
-
-
?
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
Escherichia coli W3110
P0A6W0, P77454
-
-
-
?
L-glutamic acid + NH2OH
gamma-glutamyl hydroxamate
show the reaction diagram
-
0.9% of the activity with L-glutamine and H2O as co-substrate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
O94925
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-, Q9I387
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Q66V97
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
O94925
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-, Q65NY1
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
best substrate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
preferred substrate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
biosynthesis of pyridoxal-5-phosphate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
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
show the reaction diagram
-
glutamine catabolism
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Triticale sp.
-
glutamine catabolism
-
-
ir
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
glutamine metabolism
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
renal ammonia genesis and the utilization of glutamine as a metabolic fuel, neuronal synthesis of glutamate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
O14907
synthesis of neurotransmitter glutamate and regulates the concentrations of glutamine and glutamate, ammonia detoxification
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-, Q9I387
pH 7.2, 30C
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
O94925
glutamate is an important source for neurotransmitter
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme plays a key role in energy and nitrogen metabolism
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
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
show the reaction diagram
-
PDX2 is a glutaminase that is involved in vitamin B6 biosynthesis
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
P13264
assay at pH 8
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
specifc for L-glutamine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Q4U1A6
strictly specific to L-glutamine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-, O94925
the glutamate bindig pocket of the enzyme involves Glu381 and Tyr249, structure overview
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Bacillus sp. LKG-01
-
-, preferred substrate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Micrococcus luteus K-3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Stenotrophomonas maltophilia NYW-81
-
-, best substrate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Streptomyces rimosus LG-10
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Bacillus licheniformis DSM13
Q65NY1
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
Triticale sp.
-
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
Q8YMZ9, Q8YSZ5
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
P0A6W0, P77454
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
O07637, O31465
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
P73903
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
Bacillus subtilis 168
O07637, O31465
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
Micrococcus luteus K-3
-
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
Escherichia coli W3110
P0A6W0, P77454
-
-
-
?
L-glutamine + NH2OH
?
show the reaction diagram
-
10.3% of the activity with L-glutamine and H2O as co-substrate
-
-
?
L-glutaminyl-L-asparagine + H2O
?
show the reaction diagram
Bacillus sp., Bacillus sp. LKG-01
-
-
-
-
?
L-isoglutamine + H2O
?
show the reaction diagram
-
-
-
-
?
L-theanine + H2O
L-glutamate + ethylamine
show the reaction diagram
-
-
-
-
?
nitrocefin + H2O
?
show the reaction diagram
P0A6W0, P77454
-
-
-
?
nitrocefin + H2O
?
show the reaction diagram
Escherichia coli W3110
P0A6W0, P77454
-
-
-
?
succinamate + H2O
?
show the reaction diagram
-
-
-
-
?
L-theanine + H2O
N-ethyl-L-glutamic acid
show the reaction diagram
-, Q9I387
71% activity
-
-
?
additional information
?
-
-
involvement of essential Cys and His residues in the activity of isolated glutaminase from tumour cells
-
-
-
additional information
?
-
-, Q9I387
no reaction with L-theanine, D-theanine, L-gamma-glutamylhydrazine, and L-gamma-glutamyl-p-nitroanilide
-
-
-
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
?
-
-
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
-
-
-
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
?
-
-
no activity with glutamine and hydroxylamine as substrates, no formation of L-glutamate-gamma-monohydroxamate
-
-
-
additional information
?
-
-
glutaminase as a potential component of the pathogenic process of human immunodeficiency virus associated dementia
-
-
-
additional information
?
-
-
no hydrolysis of nicotinamide adenine dinucleotide, nicotinamide, and acetamide under the same experimental conditions as L-glutamine as substrate
-
-
-
additional information
?
-
Bacillus sp., Bacillus sp. LKG-01
-
no activity with D-asparagine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
-
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
-
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
constitutive enzyme
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
contribution of the enzyme to elevated extracellular Glu at 24 h after onset of focal ischemia
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
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
show the reaction diagram
-
high glutaminase activity may be of importance for optimal insulin secretion elicited by amino acid secretagogues
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme produces myocardial Glu
-
-
-
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
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 + H2O
L-Glu + NH3
show the reaction diagram
Micrococcus luteus K-3
-
constitutive enzyme
-
-
-
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
O94925
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-, Q9I387
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Q66V97
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-, Q65NY1
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
biosynthesis of pyridoxal-5-phosphate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
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
show the reaction diagram
-
glutamine catabolism
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Triticale sp.
-
glutamine catabolism
-
-
ir
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
glutamine metabolism
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
renal ammonia genesis and the utilization of glutamine as a metabolic fuel, neuronal synthesis of glutamate
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
O14907
synthesis of neurotransmitter glutamate and regulates the concentrations of glutamine and glutamate, ammonia detoxification
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
O94925
glutamate is an important source for neurotransmitter
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme plays a key role in energy and nitrogen metabolism
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
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
show the reaction diagram
-
PDX2 is a glutaminase that is involved in vitamin B6 biosynthesis
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Bacillus sp. LKG-01
-
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
Micrococcus luteus K-3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Micrococcus luteus K-3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Stenotrophomonas maltophilia NYW-81
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Streptomyces rimosus LG-10
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Bacillus licheniformis DSM13
Q65NY1
-
-
-
?
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
?
-
-
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
-
-
-
additional information
?
-
-
glutaminase as a potential component of the pathogenic process of human immunodeficiency virus associated dementia
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
arsenate
-
50 mM, 800% of the relative activity without addition
Ca2+
-
0.5-1.0 mM, 2fold activation of NEM-insensitive enzyme
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
Cl-
Triticale sp.
-
1 mM, markedly activates the enzyme
KCl
-
2 M, 1.4fold activation
Na+
P73903
1 mol/l: 2fold activity
NaBr
-
0.25 M, 1.2-1.3fold activation
NaCl
-
8-16%, maximal activity of glutaminase I, no effect of glutaminase II
NaCl
-
5%, increases activity almost 2fold
NaCl
-
the enzyme is salt-tolerant, over 86% of maximal activity at 16% NaCl, no effect at 1 mM
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
-
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
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
-
75% of the original activity in the presence of 15-30% NaCl
NaCl
-
enhances activity at 1-20% w/v, but reduces activity by 30% at 25% w/v, optimal at 1%
NaF
-
0.25 M, 1.2-1.3fold activation
NaI
-
0.25 M, 1.2-1.3fold activation
NH4+
-
Ka 1 mM
phosphate
-
50 mM, 900% of the relative activity without addition
phosphate
-
induces association to form active tetramers
phosphate
-
activates the enzyme in vivo in tumor cells at 100 mM
phosphate
-
phosphate-activated glutaminase isozyme
phosphate
Q8YMZ9, Q8YSZ5
no activity without phosphate, max. activity at 60 mM K3PO4
PO43-
Triticale sp.
-
activity increases with the increase of the concentration of the ion
sulfate
-
50 mM, 700% of the relative activity without addition
KCl
-
25% activation at 1 mM
additional information
-
equivalent activities in absence and the presence of 3 M NaCl
additional information
-
no effect with NaCl, no significant alteration with KCl, MgCl2, MnCl2, CaCl2 and NH4Cl
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
-
the enzyme from strain RIB40 is salt-tolerant, while the enzyme from strain MA-27-IM is salt-sensitive
additional information
-
the enzyme is not affected by NiCl2 at 1 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,2-naphthoquinone 4-sulfonate
-
-
1,4-Naphthoquinone
-
-
1-amino-8-naphthol-2,4-disulfonic acid
-
weak
2,4-dinitro-1-naphthol-7-sulfonic acid
-
i.e. flavianic acid
2-oxoglutarate
-
enzyme from mesenteric lymph nodes
2-oxoglutarate
-
competitive inhibition
6-diazo-5-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
-
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
-
-
6-diazo-5-oxo-L-norleucine
O07637, O31465
;
6-diazo-5-oxo-L-norleucine
P0A6W0, P77454
;
Ampicillin
P0A6W0, P77454
-
anthraquinone-1,8-disulfonate
-
-
arsenate
-
0.5 M, 74% inhibition
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
-
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
bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide
-, O94925
; 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
Bromocresol green
-
-
bromocresol purple
-
-
Ca2+
-
0.5-1.0 mM, NEM-sensitive enzyme
CaCl21
-
inhibition to a variable extent
-
citrate
-
enzyme from mesenteric lymph nodes
Cl-
-
0.5 M, complete inhibition
CN-
-
0.5 M, complete inhibition
CoCl2
-
14% inhibition at 1 mM
Cu2+
-
CuCl2, inhibition of glutaminase II
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
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
diethyl dicarbonate
-
-
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
EDTA
-
glutaminase I and II
EDTA
-
10% inhibition at 1 mM
FeCl3
-
glutaminase II
glutamate
-
no inhibition
glutamate
-
competitive with respect to Gln
glutamate
-
no inhibition
glutamate
-
inhibits the enzyme in vivo in tumor cells at 100 mM
Hg2+
-
0.1 mM, complete inhibition
HgCl2
-
inhibition to a variable extent
iodoacetate
-
50 mM, strongly inhibited, 80% inhibition, especially more strongly with a progress of purification steps
L-glutamate
-
strong product inhibition of isozyme KGA, no inhibition of isozyme LGA
L-glutamate
-
product inhibition, competitive
L-Glutamic acid
Triticale sp.
-
5 mM, about a 40% inhibition
L-glutamine
Triticale sp.
-
above 0.3 mM
L-glutamine
P13264
inhibition of enzyme activity in tumor tissue
L-glutamine
-
product inhibition, strongly inhibits the membrane-associated enzyme, while the soluble form is not or weakly inhibited
Mersalyl
-
enzyme from mesenteric lymph nodes
Mersalyl
-
0.5 mM, almost complete inhibition
methylene blue
-
0.005%, irreversible inactivation
Mg2+
O07637, O31465
;
Mg2+
P0A6W0, P77454
;
MgCl2
-
20% inhibition at 1 mM, 12% at 0.1 mM
Mn2+
O07637, O31465
;
Mn2+
P0A6W0, P77454
;
Na2SO4
-
glutaminase I and II
NaCIO4
-
0.3 M, 25% inhibition
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
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
-
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
NaF
-
inhibition to a variable extent
NaH2PO4
-
0.3 M, complete inhibition
NaI
-
above 0.3 M
NaNO3
-
0.3 M, 15% inhibition
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
Ngamma,Ngamma-diethyl-L-glutamine
-
-
-
Ngamma,Ngamma-dimethyl-L-glutamine
-
-
-
Ngamma-ethyl-L-glutamine
-
-
Ngamma-methyl-L-glutamine
-
-
-
NH3
-
product inhibition, 10 mM inhibits the enzyme activity about 30%
NH3
-
product inhibition
NH4+
-
enzyme from mesenteric lymph nodes
NH4+
Triticale sp.
-
0.01 M, 50% inhibition
nitrite
-
0.5 M, complete inhibition
p-chloromercuribenzoate
-, Q9I387
-
p-mercuribenzoate
-
0.1 mM, complete inhibition, presence of Gln prevents inhibition
p-mercuribenzoate
-
-
PCMB
-
inhibition of glutaminase I but not glutaminase II
Penicillin
P0A6W0, P77454
-
phenylarsonic acid
-
causes a decrease in GAC levels
phenylmethylarsinic acid
-
causes a decrease in GAC levels
-
PO43-
P0A6W0, P77454
;
protein BNIP-H
O94925
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
-
pyruvate
-
0.5 M, complete inhibition
pyruvate
-
mixed inhibition
Rose bengal
-
0.01%, irreversible inactivation
succinate
-
enzyme from mesenteric lymph nodes
Tris
-
0.5 M, complete inhibition
Triton X-100
-
-
ZnCl2
-
7% inhibition at 1 mM
MnCl2
-
22% inhibition at 1 mM, 13% at 0.1 mM
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
-
additional information
-, Q9I387
no inhibition by HgCl2; no inhibition by p-chloromercuribenzoate
-
additional information
-
no inhibition by 2-mercaptomethanol and iodoacetate
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
slight activation
angiotensin II
-
activates
ATP
-
activates enzyme from mesenteric lymph nodes
ATP
-
activates only in presence of NH4+ or HCO3-
ATP
-
enhances activity
citrate
-
enhances activity
CTP
-
activates enzyme from mesenteric lymph nodes
D-fructose 6-phosphate
-
activates enzyme from mesenteric lymph nodes
D-glucose 6-phosphate
-
activates enzyme from mesenteric lymph nodes
dithiothreitol
-
slight activation
EDTA
-
slight activation
Epidermal growth factor
-
kidney-type glutaminase activity in cells is stimulated by EGF
Glucagon
-
activates
glyoxylate
-
50 mM, increasing enzyme activity by 30%
GTP
-
activates enzyme from mesenteric lymph nodes
HCO3-
-
activates
ITP
-
activates enzyme from mesenteric lymph nodes
L-glutamine
P13264
enhanced enzyme activity in jejunal mucosa
Lactate
-
enhances activity
Leu
-
activates enzyme from mesenteric lymph nodes, 50% activation at 0.6 mM
NH4+
-
required as an obligatory activator
NH4+
-
activates
NH4+
-
enzyme from mesenteric lymph nodes, 50% activation at 5 mM
NH4+
-
addition of phosphate results in dimerization and activation
NH4+
-
activates
NH4+
-
no effect
oxaloacetate
-
50 mM, increasing enzyme activity by 30%
phosphate
-
activates
phosphate
-
100 mM, maximal activation and dimerization of the enzyme; dependent on
phosphate
-
activates
phosphate
-
activates
phosphate
-
-
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
phosphoenolpyruvate
-
activates enzyme from mesenteric lymph nodes, 50% activation at 0.2 mM
sulfate
-
activates enzyme from mesenteric lymph nodes
sulfate
-
activates
Tris
Q4U1A6
activates Mglu by approximately 6fold at pH 7.5
malate
-
enhances activity
additional information
-
strong stimulation of glutaminase subunit TrpG activity by the associated synthase subunit TrpE within the glutamine amidotransferase, GATase, enzyme complex
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.195
-
2-oxo-glutaramate
-
pH 8.5, 30C
0.003
-
2-oxo-succinamate
-
pH 7.2, 30C
0.017
-
2-oxo-succinamate
-
pH 8.5, 30C
0.012
-
4-monomethyl-2-oxoglutarate
-
pH 7.2, 30C
-
6.7
-
D-gamma-Gln-methylester
-
glutaminase B
83
-
D-glutamine
-
pH 9.0, at 37C, 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 37C, NH2OH as co-substrate
3.3
-
gamma-glutamyl methylamide
-
-
64
-
gamma-methyl glutamate
-
-
23
-
gamma-thioethyl glutamate
-
-
10
-
gamma-thiomethyl glutamate
-
-
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 50C, pH 7.0
19.5
-
glutamine
Q8YMZ9, Q8YSZ5
Km apparent, no Michaelis-Menten kinetics
109.5
-
glutamine
Q8YMZ9, Q8YSZ5
Km apparent, no Michaelis-Menten kinetics
1.27
-
Glutaramate
-
pH 8.5, 30C
1.48
-
Glutaramate
-
pH 7.2, 30C
24
-
L-Asn
-
pH 9.0, at 37C, H2O as co-substrate
200
-
L-gamma-Gln-L-Ala
-
glutaminase B
-
2.1
-
L-gamma-Gln-methyl ester
-
glutaminase B
4.4
-
L-Gln
-
glutaminase I
500
-
L-Glutamic acid
-
pH 9.0, at 37C, NH2OH as co-substrate
0.11
-
L-glutamine
-, Q9I387
-
0.18
-
L-glutamine
-, Q9I387
-
0.24
-
L-glutamine
-
pH 11.0, 70C
0.4
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, GAC mutant Y394L
1.4
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, wild-type GAC
1.9
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, isozyme GLS1
2.3
-
L-glutamine
-
pH 7.5, 30C, full-length enzyme, in presence of 2.6 M NaCl
2.5
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, GAC mutant F322S/F318Y
3
-
L-glutamine
-
lower than, soluble and membrane-associated N-PAG, 37C, 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, 30C, protease-cleaved large enzyme fragment, in presence of 2.6 M NaCl
3.8
-
L-glutamine
-
pH 7.5, 30C, protease-cleaved large enzyme fragment, in absence of NaCl
4
-
L-glutamine
-
brain, membrane-associated PAG, 37C, pH 8.6
4
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, isozyme GLS2
4.5
-
L-glutamine
-
pH 7.5, 37C
6.1
-
L-glutamine
-
pH 7.5, 30C, full-length enzyme, in absence of NaCl
6.2
-
L-glutamine
-
mutant enzyme E160D
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
7.3
-
L-glutamine
P0A6W0, P77454
-
7.6
-
L-glutamine
O07637, O31465
-
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
P0A6W0, P77454
mutant Q162A
9.5
-
L-glutamine
-
pH 9.0, at 37C, H2O as co-substrate
11
-
L-glutamine
-
mutant enzyme Y191F
12.2
-
L-glutamine
P73903
1 mol/l NaCl present
14
-
L-glutamine
-
native enzyme, T-acetate buffer, pH 8.0
17
-
L-glutamine
-
pH 9.0, at 37C, NH2OH as co-substrate
23.7
-
L-glutamine
P0A6W0, P77454
mutant G261A
26
-
L-glutamine
-
brain, soluble PAG, 37C, pH 8.6
26.6
-
L-glutamine
P73903
Km apparent, no Michaelis-Menten enzyme
27.6
-
L-glutamine
O07637, O31465
-
30.6
-
L-glutamine
P0A6W0, P77454
-
460
-
L-glutamine
-
mutant enzyme Y191T
0.14
-
succinamate
-
pH 8.5, 30C
0.23
-
succinamate
-
pH 7.2, 30C
6.5
-
L-Gln
-
glutaminase II
additional information
-
L-glutamate
-
7.5 mol/l, pH and temperature not specified in this publication
0.71
-
L-Theanine
-
glutaminase B
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
-
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
-
kinetics, overview
-
additional information
-
additional information
-, Q65NY1
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
17.5
-
2-oxo-glutaramate
-
pH 8.5, 30C
0.87
-
2-oxo-succinamate
-
pH 8.5, 30C
1.15
-
2-oxo-succinamate
-
pH 7.2, 30C
134.5
-
4-monomethyl-2-oxoglutarate
-
pH 7.2, 30C
-
36
-
gamma-ethyl glutamate
-
-
14
-
gamma-glutamyl hydrazide
-
-
296
-
gamma-glutamyl methoxyamide
-
-
8
-
gamma-glutamyl methylamide
-
-
212
-
gamma-glutamyl-hydroxamate
-
-
645
-
gamma-methyl glutamate
-
-
300
-
gamma-thioethyl glutamate
-
-
1260
-
gamma-thiomethyl glutamate
-
-
4.1
-
Glutaramate
-
pH 7.2, 30C
8.8
-
Glutaramate
-
pH 8.5, 30C
0.96
-
L-glutamine
-
mutant enzyme E160D
1.4
-
L-glutamine
-
mutant enzyme Y191T
2.5
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, isozyme GLS2
10
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, isozyme GLS1
20
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, GAC mutant Y394L
22
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, wild-type GAC
38.6
-
L-glutamine
O07637, O31465
-
40
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, GAC mutant F322S/F318Y
49.9
-
L-glutamine
P0A6W0, P77454
mutant Q161A
57
-
L-glutamine
-
mutant enzyme Y191F
67.7
-
L-glutamine
O07637, O31465
-
79.9
-
L-glutamine
P0A6W0, P77454
mutant Q162A
91.4
-
L-glutamine
P0A6W0, P77454
-
101
-
L-glutamine
P0A6W0, P77454
-
128
-
L-glutamine
-
pH 7.5, 30C, full-length enzyme, in presence of 2.6 M NaCl
403.3
-
L-glutamine
-
pH 7.5, 30C, full-length enzyme, in presence of 2.6 M NaCl
821.7
-
L-glutamine
-
pH 7.5, 30C, protease-cleaved large enzyme fragment, in presence of 2.6 M NaCl
873.3
-
L-glutamine
-
pH 7.5, 30C, protease-cleaved large enzyme fragment, in absence of NaCl
1373
-
L-glutamine
-
pH 7.5, 30C, full-length enzyme, in absence of NaCl
2
-
succinamate
-
pH 7.2, 30C
2.8
-
succinamate
-
pH 8.5, 30C
1400
-
L-glutamine
-
wild-type enzyme
additional information
-
additional information
-
effect of pH on turnover number
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
89.7
-
2-oxo-glutaramate
-
pH 8.5, 30C
324817
51.2
-
2-oxo-succinamate
-
pH 8.5, 30C
324815
385
-
2-oxo-succinamate
-
pH 7.2, 30C
324815
11200
-
4-monomethyl-2-oxoglutarate
-
pH 7.2, 30C
0
2.8
-
Glutaramate
-
pH 7.2, 30C
10951
6.9
-
Glutaramate
-
pH 8.5, 30C
10951
0.63
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, isozyme GLS2
12226
5.3
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, isozyme GLS1
12226
16
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, wild-type GAC and GAC mutant F322S/F318Y
12226
47
-
L-glutamine
-, O94925
pH 8.5, temperature not specified in the publication, GAC mutant Y394L
12226
8.7
-
succinamate
-
pH 7.2, 30C
16752
20
-
succinamate
-
pH 8.5, 30C
16752
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.7
-
2-oxoglutarate
-
pH 7.0, at 37C
3.5
-
Ampicillin
P0A6W0, P77454
competitive inhibitor
2.95
-
Ngamma,Ngamma-diethyl-L-glutamine
-
37C, pH 7.5
-
2.64
-
Ngamma,Ngamma-dimethyl-L-glutamine
-
37C, pH 7.5
-
1.58
-
Ngamma-ethyl-L-glutamine
-
37C, pH 7.5
1.11
-
Ngamma-methyl-L-glutamine
-
37C, pH 7.5
-
6.4
-
Penicillin
P0A6W0, P77454
-
0.7
-
pyruvate
-
pH 7.0, at 37C
0.003
-
bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide
-
-
additional information
-
L-glutamate
-
39.0 mol/l, pH and temperature not specified in this publication
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6e-05
-
bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide
-, O94925
pH 8.5, temperature not specified in the publication, isozyme GLS1
8e-05
-
bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide
-, O94925
pH 8.5, temperature not specified in the publication, wild-type GAC
0.088
-
bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide
-, O94925
pH 8.5, temperature not specified in the publication, isozyme GLS2
0.1
-
bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide
-, O94925
pH 8.5, temperature not specified in the publication, GAC mutant F322S/F318Y and GAC mutant Y394L
0.2
-
Mg2+
P0A6W0, P77454
-
1.7
5.5
Mg2+
O07637, O31465
;
1.7
5.5
Mg2+
P0A6W0, P77454
-
0.1
-
Mn2+
P0A6W0, P77454
-
0.7
1.3
Mn2+
O07637, O31465
;
0.7
1.3
Mn2+
P0A6W0, P77454
-
39
-
Ngamma,Ngamma-diethyl-L-glutamine
-
37C, pH 7.5
-
35
-
Ngamma,Ngamma-dimethyl-L-glutamine
-
37C, pH 7.5
-
24
-
Ngamma-ethyl-L-glutamine
-
37C, pH 7.5
20
-
Ngamma-methyl-L-glutamine
-
37C, pH 7.5
-
17.2
17.4
PO43-
P0A6W0, P77454
;
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.516
-
-
pH 7.5, 40C, Lactobacillus reuteri shows the highest activity compared to wild-type Lactobacillus plantarum and wild-type Lactobacillus paracasei which are transformed with the glutaminase gene Lactobacillus reuteri in this study. The wild-type Lactobacillus paracasei shows no glutaminase activity
0.68
-
-
PAG, healthy liver tissue
1.23
-
-
recombinant enzyme
2.4
-
-
PAG, cirrhotic disease patient liver tissue
11.1
-
Q66V97
recombinant enzyme in Escherichia coli strain JM109
16.4
-
-
pH 7.5, 37C
22.1
-
-, Q9I387
purified enzyme
25.71
-
Q8YMZ9, Q8YSZ5
Vmax apparent, no Michaelis-Menten kinetics
27.1
-
-, Q9I387
purified enzyme
29.7
-
P73903
1 mol/l NaCl present
102.3
-
Q8YMZ9, Q8YSZ5
Vmax apparent, no Michaelis-Menten kinetics
325
-
-
purified enzyme
325
-
-, Q65NY1
purified recombinant His10-tagged GlsA, pH 7.5, 30C
403
-
-
recombinant enzyme with N-terminal deletion
405
-
-
recombinant enzyme with N-terminal and C-terminal deletions
584.2
-
-
purified enzyme, pH 11.0, 70C
730
-
Q66V97
purified recombinant enzyme
1230
-
-
purified native enzyme
1246
-
-
purified recombinant enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
1230 U/mg, original strain; 1965 U/mg, recombinant protein
additional information
-
-
tissue-specific enzyme activity, concentrations of free amino acids in muscles and plasma, overview
additional information
-
-
tissue-specific enzyme activity, concentrations of free amino acids in muscles and plasma, overview, glutamine concentrations in plasma of fed and starved chicken do not differ
additional information
-
-
tissue-specific enzyme activity, concentrations of free amino acids in muscles and plasma, overview
additional information
-
Q66V97
activity of different enzyme constructs recombinantly expressed in different Escherichia coli strains, overview
additional information
-
P13264
0.9 micromol/mg protein, measured in tumor tissue after treatment with dietary glutamine; 1.6 micromol/mg protein, measured in tumor tissue; 1,75 micromol/mg protein, measured in jejunal mucosa in normal rats; 1 micromol/mg protein, measured in jejunal mucosa in DMBA-treated rats wiht tumor; 2.25 micromol/mg protein, measured in jejunal mucosa in DMBA-treated rats without tumor; 2 micromol/mg protein, measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats with tumor; 3 micromol/mg protein, measured in jejunal mucosa after treatment with dietary glutamine in normal rats; 5.25 micromol/mg protein, measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats without tumor
additional information
-
-
the recombinant enzymes from Lactobacillus plantarum and Lactobacillus paracasei show increased enzyme activity. The wild-type organisms do not amplify the glutaminase gene. The recombinant Lactobacillus plantarum displays ca. 4fold higher activity than its wild-type and 1.5fold higher activity the wild-type Lactobacillus reuteri. The recombinant Lactobacillus paracasei enzyme increases to half of the activity of Lactobacillus reuteri. The wild-type Lactobacillus paracasei shows no glutaminase activity
additional information
-
-
0.024 U/mg in static culture at 20C using modified MRS medium in which sucrose is substituted for glucose
additional information
-
-
the proliferation state of the cells influence the specific activity. It is maximal at the start of the exponential phase of growth and is gradually reduced to a lower but significant level when the cell culture ceases to divide
additional information
-
-
133 U/mg
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
Q8YMZ9, Q8YSZ5
-
7
-
-
hydrolysis of L-Asn and L-Gln
7.1
9
-
hydrolysis of Gln, glutaminase B
7.4
-
-
assay at
7.4
-
O94925
assay at
7.4
-
-
assay at
7.5
8
O07637, O31465
;
7.5
8
P0A6W0, P77454
;
7.5
8.5
-
purified enzyme
7.5
-
-
assay at
7.5
-
Q66V97
assay at
7.5
-
Q8YMZ9, Q8YSZ5
-
7.5
-
Q4U1A6
assay at
7.5
-
-, Q65NY1
assay at
7.6
7.8
Triticale sp.
-
-
8
9
-
enzyme from strain RIB40
8
-
-
glutaminase I
8
-
-
assay at
8
-
P13264
assay at
8
-
-
assay at
8.3
9.2
-
formation of gamma-glutamyl hydroxamate from L-Gln and NH2OH
8.5
-
-
glutaminase II
8.5
-
-
-
8.5
-
-, Q9I387
-
8.5
-
-
assay at
8.6
-
-
assay at
11
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
11
-
over 40% activity at pH 5 and over 70'% at pH 11
5
12
-
activity range
6
11
-
pH 6.0: about 55% of maximal activity, pH 11.0: about 55% of maximal activity, hydrolysis of Gln
7.5
9
-, Q9I387
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
Q8YMZ9, Q8YSZ5
-
25
-
-
assay at
30
-
-
assay at
30
-
-
enzyme from strain RIB40
30
-
Q66V97
assay at
30
-
-
assay at
30
-
Q4U1A6
assay at
30
-
-, Q65NY1
assay at
37
-
-
assay at
37
-
-
assay at
37
-
Q8YMZ9, Q8YSZ5
-
37
-
-
assay at
50
-
-
glutaminase I and II
60
-
-
purified enzyme
70
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
60
-
over 70% activity at 20C and ca. 90% at 60C
35
85
-
activity range
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
kidney-type glutaminase GLS1
Manually annotated by BRENDA team
-
phosphate-activated isozyme
Manually annotated by BRENDA team
-
isozymes LGA and KGA
Manually annotated by BRENDA team
-
of medullar blood of acute lymphoblastic leukaemia patients
Manually annotated by BRENDA team
-
expression of both isozymes, the isozyme KGA/LGA ratio is very high in brain
Manually annotated by BRENDA team
O94925
isozyme KGA
Manually annotated by BRENDA team
-
of newborn mice, and adult brain cortex and stem, GLS1
Manually annotated by BRENDA team
-
phosphate-activated isozyme, isozyme K-PAG
Manually annotated by BRENDA team
-
isozymes LGA and KGA, mainly astrocytes, cerebral cortex, and neurons
Manually annotated by BRENDA team
-
isozymes LGA and KGA
Manually annotated by BRENDA team
-
activity is enhanced following portacaval anastomosis
Manually annotated by BRENDA team
-
lymphoblastoid cell
Manually annotated by BRENDA team
-
isozymes LGA and KGA
Manually annotated by BRENDA team
-
splicing variant isozyme GAC
Manually annotated by BRENDA team
-
optimizing concentration of sucrose, yeast extract, glutamine, and sodium chloride for L-glutaminase production by response surface methodology
Manually annotated by BRENDA team
Micrococcus luteus K-3
-
-
-
Manually annotated by BRENDA team
-
kidney-type glutaminase GLS1
Manually annotated by BRENDA team
-
phosphate-activated isozyme, mucosa
Manually annotated by BRENDA team
-
phosphate-activated isozyme
Manually annotated by BRENDA team
-
phosphate-activated isozyme
Manually annotated by BRENDA team
-
phosphate-activated isozyme
Manually annotated by BRENDA team
-
hepatoblastoma cell line
Manually annotated by BRENDA team
-
activity is enhanced following portacaval anastomosis
Manually annotated by BRENDA team
-
kidney-type isozyme, KGA
Manually annotated by BRENDA team
-
isozyme K-PAG
Manually annotated by BRENDA team
-
isozyme KGA
Manually annotated by BRENDA team
-
isozyme KGA and splicing variant isozyme GAC
Manually annotated by BRENDA team
-
activity is enhanced following portacaval anastomosis
Manually annotated by BRENDA team
-
kidney-type glutaminase GLS1 and glutaminase C
Manually annotated by BRENDA team
-
kidney-type glutaminase isoform KGA
Manually annotated by BRENDA team
-
myeloid cell line
Manually annotated by BRENDA team
-
expression of both isozymes, but mainly of the liver-type isozyme, LGA, the isozyme KGA/LGA ratio is very low in liver
Manually annotated by BRENDA team
-
moderate enzyme activity
Manually annotated by BRENDA team
-
neonatal liver, all GLS1 activity is caused by GLS1, which is downregulated during development, and supplanted by the liver-specific glutaminase type 2, GLS2, in adulthood
Manually annotated by BRENDA team
-
phosphate-activated isozyme, isozyme L-PAG
Manually annotated by BRENDA team
-
isozymes LGA and KGA
Manually annotated by BRENDA team
-
isozyme LGA is specific for liver, and isozyme KGA is expressed in fetal liver
Manually annotated by BRENDA team
-
liver-type glutaminase GLS2
Manually annotated by BRENDA team
-
breast cancer cell line
Manually annotated by BRENDA team
-
kidney-type glutaminase GLS1
Manually annotated by BRENDA team
O94925
isozyme KGA
Manually annotated by BRENDA team
-
isozymes LGA and KGA
Manually annotated by BRENDA team
-
of lateral reticular nucleus. Glutaminase enrichment is synergistically coupled with glutamatergic innervation to supplement the glutamate pool for GABA synthesis and for metabolic utilization (via the GABA shunt/tricarboxylic acid cycle)
Manually annotated by BRENDA team
-
human polymorphonuclear neutrophil
Manually annotated by BRENDA team
-
isozyme LGA is secreted from the plasma membrane
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
isozymes LGA and KGA
Manually annotated by BRENDA team
-
all the glutaminase activity detected in pancreatic islets is attributed to kidney-type glutaminase and is confined to the mantle of the islet; glutaminase activity is confined to the mantle
Manually annotated by BRENDA team
-
kidney-type glutaminase GLS1
Manually annotated by BRENDA team
Triticale sp.
-
-
Manually annotated by BRENDA team
-
neuroblastoma cells, N-PAG, the proliferation state of the cells influence the specific activity. It is maximal at the start of the exponential phase of growth and is gradually reduced to a lower but significant level when the cell culture ceases to divide
Manually annotated by BRENDA team
-
kidney-type glutaminase GLS1
Manually annotated by BRENDA team
-
moderate activity in breast muscle, very low activity in leg muscle
Manually annotated by BRENDA team
-
high activity in breast muscle, low activity in leg muscle
Manually annotated by BRENDA team
-
preferentially localized to the surface epithelium of the small inestine, some activity is also found in cells of the lamina propria
Manually annotated by BRENDA team
-
phosphate-activated isozyme
Manually annotated by BRENDA team
-
isozymes LGA and KGA
Manually annotated by BRENDA team
-
low expression level of isozymes LGA and KGA
Manually annotated by BRENDA team
-
isozyme K-PAG
Manually annotated by BRENDA team
-
breast cancer cell line
Manually annotated by BRENDA team
additional information
-
isozyme tissue distribution, co-expression of glutaminase K and L isoenzymes in human tumour cells, overview
Manually annotated by BRENDA team
additional information
-
optimal enzyme production at pH 9.0 and 27C after 96 h on glucose and malt extract as carbon and nitrogen sources
Manually annotated by BRENDA team
additional information
-
strain NYW-81, Koji medium, effects of carbon and nitrogen sources for cell growth on the production of enzyme, overview
Manually annotated by BRENDA team
additional information
-
isozyme tissue distribution, overview, isozyme K-PAG is located in kidney, brain, and villus enterocyte, while isozyme L-PAG is restricted to the liver
Manually annotated by BRENDA team
additional information
-
isozyme tissue-specific expression patterns, the enzyme is overexpressed in a variety of tumours and malignancies, overview
Manually annotated by BRENDA team
additional information
-
isozyme expression patterns
Manually annotated by BRENDA team
additional information
-
GLS2 expression is lost or greatly decreased in hepatocellular carcinomas and the overexpression of GLS2 greatly reduces tumor cell colony formation
Manually annotated by BRENDA team
additional information
-
KGA and GAC are enhanced in cancer, but only GAC is found in mitochondria
Manually annotated by BRENDA team
additional information
Stenotrophomonas maltophilia NYW-81
-
strain NYW-81, Koji medium, effects of carbon and nitrogen sources for cell growth on the production of enzyme, overview
-
Manually annotated by BRENDA team
additional information
Streptomyces rimosus LG-10
-
optimal enzyme production at pH 9.0 and 27C after 96 h on glucose and malt extract as carbon and nitrogen sources
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
bound to membrane, highest activity in the cell pellet in comparison to supernatant fraction
-
Manually annotated by BRENDA team
-
of neutrophils, isozyme LGA
Manually annotated by BRENDA team
Cryptococcus albidus ATCC20293, Cryptococcus flavescens NISL 3771
-
-
-
Manually annotated by BRENDA team
-
enzyme from strain MA-27-IM
-
Manually annotated by BRENDA team
-
isozyme LGA is secreted from the plasma membrane/cell surface of neutrophils
-
Manually annotated by BRENDA team
Streptomyces rimosus LG-10
-
-
-
-
Manually annotated by BRENDA team
-
enzyme from strain MA-27-IM
Manually annotated by BRENDA team
-
membrane associated
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
synaptosomal and non-synaptosomal
Manually annotated by BRENDA team
-
loosely bound to inner membrane
Manually annotated by BRENDA team
-
loosely bound to inner membrane
Manually annotated by BRENDA team
-
mitochondrial enzyme with a cytosolic precursor
Manually annotated by BRENDA team
O94925
isozyme KGA
Manually annotated by BRENDA team
-
phosphate-activated isozyme
Manually annotated by BRENDA team
-
mitochondrial glutaminase plays a role in HIV-infected monocyte-derived macrophage-mediated neuronal apoptosis
Manually annotated by BRENDA team
-
neuroblastomal PAG is mitochondrial, enriched in mitochondria by 606% compared to the cell homogenate
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
-
of neutrophils, isozyme LGA
Manually annotated by BRENDA team
-
GAC is mitochondrial, distinctly localized from kidney-type GLS isozymes
Manually annotated by BRENDA team
additional information
-
analysis of subcellular targeting sequences and motifs of isozyme LGA
-
Manually annotated by BRENDA team
additional information
-
KGA and GAC are enhanced in cancer, but only GAC is found in mitochondria
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Geobacillus kaustophilus (strain HTA426)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
13740
-
O14907
calculation from sequence of cDNA
37000
-
-, Q65NY1
gel filtration
38500
-
-
fragment enzyme, SDS-PAGE
38970
-
-
N-terminal large enzyme fragment comprising residues 1-368, MALDI-TOF mass spectrometry
41000
-
-
gel filtration
48000
-
-
recombinant enzyme with N-terminal and C-terminal deletions, SDS-PAGE
48000
-
Q4U1A6
-
48300
-
-
intact enzyme, SDS-PAGE
49700
-
-
recombinant enzyme with N-terminal and C-terminal deletions, based on amino acid content
50000
-
-
and 70000 Da, SDS-PAGE
58000
-
-
N-PAG, immunoblot analysis, C-terminal antibody reacts with the protein of 65000 Da, while the N-terminal antibody primarily labels a protein of 58000 Da and to a minor degree one of 65000 Da. This strongly suggests that neuroblastoma cells mainly contain an active isoform of PAG lacking the C-terminal end, probably the GAC form, a splicing variant
65000
-
-
SDS-PAGE
65000
-
-
N-PAG, immunoblot analysis, C-terminal antibody reacts with the protein of 65000 Da, while the N-terminal antibody primarily labels a protein of 58000 Da and to a minor degree one of 65000 Da. This strongly suggests that neuroblastoma cells mainly contain an active isoform of PAG lacking the C-terminal end, probably the GAC form, a splicing variant
67000
-
-, Q9I387
gel filtration
70000
-
-
and 50000 Da, SDS-PAGE
72600
-
O07637, O31465
gel filtration
74900
-
P0A6W0, P77454
gel filtration
86000
-
-
glutaminase I and II, gel filtration
86000
-
-
C-terminally truncated enzyme, gel filtration
88800
-
-
gel filtration
90000
-
-
glutaminase B, gel filtration
95000
-
-
sucrose density gradient centrifugation
96000
-
-
full-length enzyme, gel filtration
110000
-
-
PAGE under nondenaturing conditions
122000
-
-
gel filtration
126000
-
-
gel filtration
137000
-
-, Q9I387
sedimentation equilibrium mehod
138100
-
O07637, O31465
gel filtration
146000
-
-
equilibrium centrifugation
148800
-
P0A6W0, P77454
gel filtration
170500
-
-
sucrose density gradient centrifugation
249000
-
-
gel filtration after dimerization with phosphate
260000
-
-
recombinant enzyme with N-terminal deletion dialyzed versus T-phosphate buffer, pH 8.0, gel filtration
270000
-
-
recombinant enzyme, gel filtration
290000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 65000, kidney enzyme
?
-
x * 64000, kidney enzyme
?
-
x * 65000 + x * 68000, protein bands in the ratio 4:1, SDS-PAGE
?
-
x * 43000, SDS-PAGE
?
-
x * 64000, SDS-PAGE
?
Q66V97
x * 49883, amino acid sequence calculation
?
Q8YMZ9, Q8YSZ5
x * 33000, SDS-PAGE; x * 36000, SDS-PAGE
?
P73903
x * 35000, SDS-PAGE
?
-
x * 66000, SDS-PAGE
?
Bacillus sp. LKG-01
-
x * 66000, SDS-PAGE
-
dimer
-
2 * 43000, glutaminase I, SDS-PAGE
dimer
-
2 * 48000, full-length enzyme, SDS-PAGE, 2 * 42000, C-terminally truncated enzyme, SDS-PAGE
dimer
-
active kidney-type glutaminase
dimer
Micrococcus luteus K-3
-
2 * 43000, glutaminase I, SDS-PAGE; 2 * 48000, full-length enzyme, SDS-PAGE, 2 * 42000, C-terminally truncated enzyme, SDS-PAGE
-
homodimer
-
2 * 55000, SDS-PAGE
homodimer
O07637, O31465
2 * 34000, SDS-PAGE
homodimer
P0A6W0, P77454
2 * 33500, SDS-PAGE
homodimer
Bacillus subtilis 168
-
2 * 34000, SDS-PAGE
-
homodimer
Escherichia coli W3110
-
2 * 33500, SDS-PAGE
-
homotetramer
O07637, O31465
4 * 36200, SDS-PAGE, gelfiltration
homotetramer
P0A6W0, P77454
4 * 32900, SDS-PAGE
homotetramer
Bacillus subtilis 168
-
4 * 36200, SDS-PAGE, gelfiltration
-
homotetramer
Escherichia coli W3110
-
4 * 32900, SDS-PAGE
-
homotrimer or homotetramer
-
x * 78000 recombinant enzyme, SDS-PAGEm x * 73801, sequence calculation
homotrimer or homotetramer
Cryptococcus flavescens NISL 3771
-
x * 78000 recombinant enzyme, SDS-PAGEm x * 73801, sequence calculation
-
monomer
-
1 * 48300, full-length enzyme, SDS-PAGE, 1 * 38500, N-terminal large enzyme fragment, after C-terminal cleavage by serine protease, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE
monomer
-, Q65NY1
1 * 38500, about, sequence calculation, 1 * 39000, SDS-PAGE
monomer
Bacillus licheniformis DSM13
-
1 * 38500, about, sequence calculation, 1 * 39000, SDS-PAGE
-
monomer
Micrococcus luteus K-3
-
1 * 48300, full-length enzyme, SDS-PAGE, 1 * 38500, N-terminal large enzyme fragment, after C-terminal cleavage by serine protease, SDS-PAGE
-
tetramer
-
4 * 73500, SDS-PAGE
tetramer
-
4 * 35000, glutaminase A, SDS-PAGE; 4 * 67000, glutaminase B, SDS-PAGE
tetramer
-
4 * 36400, SDS-PAGE
tetramer
-
4 * 63200, SDS-PAGE, recombinant enzyme with N-terminal deletion; 4 * 64000, based on amino acid content, recombinant enzyme with N-terminal deletion
tetramer
-, O94925
GLS1 splice variant GAC
tetramer
-
the side chain of Phe327, which in all monomers, is part of a hydrophobic cluster located at the tetramer interface, formed by the complementary stacking of Phe327 itself, Ala395, Ile396, Tyr399, in chain A, with its equivalent residues in chain D
tetramer
-
inactive kidney-type glutaminase
trimer
-
3 * 57000, SDS-PAGE
monomer
Stenotrophomonas maltophilia NYW-81
-
1 * 36000, SDS-PAGE
-
additional information
-
in absence of phosphate the enzyme exists as an inactive protomer, addition of phosphate results in activation and dimerization
additional information
-
The glutaminase fragment is composed of N-terminal and C-terminal domains, and a putative catalytic dyad of S64 and K67 is located in a cleft of the N-terminal domain
additional information
-
the glutaminase subunit TrpG, which adopts the triad G-type amidotransferase fold, and the synthase subunit TrpE, which adopts a complicated alpha/beta folding pattern, assemble to heterotetrameric (TrpE/TrpG)2-complexes. The sequence stretch L126-V127-A128-T129-R130-Y131 is localized between the catalytic triad Cys83-His175-Glu177 and the associated TrpE subunit, homology modeling based on the structure of Sulfolobus solfataricus TrpG
additional information
-
structure of ligand-free GAC, molecular replacement, overview. Accompanying tetramer assembly, conformational changes involving Phe327 are triggered, lifting the gating loop and exposing the active site
additional information
Micrococcus luteus K-3
-
The glutaminase fragment is composed of N-terminal and C-terminal domains, and a putative catalytic dyad of S64 and K67 is located in a cleft of the N-terminal domain
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no modification
-
-
glycoprotein
-
recombinant enzyme
glycoprotein
Cryptococcus flavescens NISL 3771
-
recombinant enzyme
-
no modification
-
-
phosphoprotein
-
phosphorylation-dependent regulation of kidney-type glutaminase
no modification
-
-
no modification
-
-
no modification
-
-
no modification
Triticale sp.
-
-
no modification
Micrococcus luteus K-3
-
-
-
additional information
-
in mitochondria, the first 16 amino acids are removed
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
O07637, O31465
handing-drop vapor diffusion technique, at 18C
-
purified recombinant mature C-terminally His6-tagged wild-type enzyme, hanging drop vapor diffusion method, mixing 0.005 ml of 34 mg/ml protein in 20 mM NaHEPES, pH 7.0, with 0.005 ml of reservoir solution containing 1.2 M ammonium dihydrogen phosphate, and 0.1 M sodium citrate, pH 5.6, crystallization of wild-type pro-enzyme by sitting drop vapour diffusion, mixing 0.002 ml of 20 mg/ml pro-enyzme in 20mM NaHEPES, pH 6.5, with 0.002 ml of reservoir solution containing 0.2 M ammonium citrate, pH 5.1, and 20% w/v PEG-3350, crystallization of mutant A47Q-1 by hanging drop vapour diffusion method, by mixing of 0.005 ml of 20 mg/ml protein in 20 mM ammonium tartrate, pH 6.7, with 0.005 ml of reservoir solution containing 0.2 M ammonium tartrate, pH 6.7, and 20% PEG 3350, and of mutant A47Q-2 by mixing 0.005 ml of 20 mg/ml protein in 20 mM sodium phosphate, pH 6.0, with 0.005 ml reservoir solution containing 0.2 M sodium tartrate, pH 8.6, and 20% w/v PEG 3350, 20C, X-ray diffraction structure determination and analysis at 1.5-1.75 A resolution
-
-
P0A6W0, P77454
phosphate- and L-glutamate-bound GAC, X-ray diffraction structure determination and analysis at 2.85 A and 2.80 A resolution, respectively
-
purified recombinant GAC free and in complex with inhibitor bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide, hanging drop vapor diffusion, mixing of protein in 25 mM HEPES (pH 7.5), 200 mM NaCl, 5% glycerol, and 5 mM beta-ME, with reservoir solution containing 0.3 M magnesium chloride, 0.1 M Tris, pH 8.5, and 12% w/v PEG 4000, X-ray diffraction structure determination and analysis at 2.55 and 2.3 A resolution, respectively
-, O94925
C-terminally truncated enzyme, hanging-drop, vapor-diffusion method at 25C, X-ray diffraction structure determination and analysis at 2.4 resolution using multiple-wavelength anomalous dispersion, MAD
-
determination of the structures of the intact enzyme in the presence and in the absence of its product L-glutamate and its activator Tris, which activates the enzyme by 6fold, and in the presence of both
Q4U1A6
enzyme and its fragment containing about 80% of the protein, handing-drop vapour-diffusion method
-
by addition of ammonium sulfate
-, Q9I387
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
10
-
most stable at pH 8.0, 60-80% of maximal activity at pH 5.0-10.0, purified enzyme
7
11
-
stable at
7
-
-
37C, 93% loss of activity, stable in presence of 1 mM EDTA, 20% loss of activity in presence of 1 mM EGTA
7.5
8
-
30 min, 40C, enzyme from strain RIB40, most stbale at
7.5
9
-
stable
8
11
-
purified enzyme, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
low level of activity after partial purification at 4C in absence of stabilizing ligands, warming at 24C results in 2fold to 5fold increase in activity
30
-
-
pH 7.5, 10 min, stable in absence of NaCl
35
-
-
30 min, pH 7.5, the enzyme from strain RIB40 is stable
37
-
-
pH 7.0, 93% loss of activity, stable in presence of 1 mM EDTA, 20% loss of activity in presence of 1 mM EGTA
40
-
-
pH 7.5, 10 min, 10% NaCl, glutaminase I and II stable up to
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
50
-
-
in presence of 1.71 M NaCl, stable up to
50
-
-
purified enzyme, 3 h, 100% stable
60
-
-
10 min, 70% remaining activity, purified enzyme
60
-
-
78% activity remains after incubation at 60C for 30 min
60
-
-
78% activity remains after incubation for 10 min at 60C
60
-
-
30 min at 60C in the absence of the substrate has no effect on the activity of the partially purified enzyme
70
-
-
10 min, 50% remaining activity, purified enzyme
70
-
-
purified enzyme, 3 h, 50% activity remaining
80
-
-
purified enzyme, 3 h, 20% activity remaining
additional information
-
-
10% NaCl enhances thermal stability of glutaminase I
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing and thawing produces a substantial loss of activity
-
significant loss of activity upon freezing at -20C and -80C in presence and absence of 20% glycerol
-
sodium borate is the most effective stabilizing agent against cold inactivation
-
enzyme shows high instability especially during the gel filtration step. Addition of 10% ethylene glycol as stabilizer
-
stabilized by MgCl2 and glycerol in addition to NaCl
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5C, enzyme preparation as a lyophilized powder, indefinitely stable
-
30C, pH 7.5, purified recombinant enzyme, stable for up to 6 h
-, Q65NY1
stable at -80?C
O07637, O31465
stable at -80C
O07637, O31465
4C, in presence of sodium borate, stable for 5 days
-
stable at -196C (unstable at -80C)
P0A6W0, P77454
stable at -80C
P0A6W0, P77454
0-5C, pH 7.2, 10 mM Tris-HCl, 10% glycerol, 10 mM MgCl2, glutaminase I and II, stable for 1 month
-
0-5C, 0.01 M potassium phosphate buffer, pH 7.2, containing 12.5% glycerol, little lose of activity
-, Q9I387
0-5C, 0.01 M potassium phosphate buffer, pH 7.2, containing 12.5% glycerol, little loss of activity
-, Q9I387
4C, T-phosphate buffer, pH 8.0, 1 mM dithiothreitol, very stable
-
-20C, stable for at least 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
;
Q8YMZ9, Q8YSZ5
recombinant enzyme 5.9fold from Escherichia coli by anion exchange, glutamine affinity, and hydrophobic interaction chromatography to homogeneity
Q66V97
recombinant His10-tagged GlsA 2.7fold from Escherichia coli by nickel affinity chromatography to homogeneity
-, Q65NY1
native enzyme, 49fold from cell-free extract by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration, to homogeneity
-
;
O07637, O31465
by centrifugation, lysis, nickel affinity chromatography
-
recombinant C-terminally His6-tagged wild-type and mutant A47Q enzymes from Escherichia coli strain BL21(DE3) cytosol by nickel affinity chromatography
-
;
P0A6W0, P77454
glutaminase B
-
recombinnat GAC from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography
-, O94925
partially purified, 21fold, 0.2% yield, protamine sulfate treatment, anion exchange chromatography, and gel filtration
-
DEAE-Toyopearl column
-
native enzyme from strain K-3 to homogeneity, recombinant enzyme from Escherichia coli strain JM109 by anion exchange chromatography to homogeneity
-
purification of glutaminase I, partial purification of glutaminase II
-
recombinant enzyme
-
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109
-
using Ni-NTA chromatography
-
partially purified by heating and Sephadex G-100 gel filtration, 25% yield
-
partially from rat pancreas by preparation of islets of Langerhans
-
recombinant enzyme with N-terminal deletion and recombinant enzyme with N-terminal and C-terminal deletions, by nickel-affinity chromatography, 63fold and 113fold respectively
-
recombinant enzyme, by metal affinity chromatography
-
by two-step ammonium sulfate precipitation, hydrophobic interaction chromatography on phenyl-Sepharose, anion exchange chromatography on DEAE-cellulose, hydrophobic interaction chromatography on phenyl-Superose and anion exchange chromatography using Mono Q, 762fold
-
native enzyme 250fold from strain NYW-81 to homogeneity by two steps of anion exchange chromatography, hydrophobic interaction and hydroxylapatite chromatography, and gel filtration
-
recombinant His-tagged TrpG, and mutant TrpG variants T129F and T129A from Escherichia coli strain BL21(DE3)Rosetta by heat treatment for 20 min at 60C, nickel affinity chromatography, and anion exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
;
Q8YMZ9, Q8YSZ5
expression in Escherichia coli
-
gene AoglsA, from strain RIB40, DNA and amino acid sequence determination and analysis, functional overexpression in Saccharomyces cerevisiae cell wall and in Escherichia coli as soluble protein
Q66V97
gene glsA, expression of His10-tagged GlsA in Escherichia coli under the control of a ptac promoter
-, Q65NY1
;
O07637, O31465
expression in Escherichia coli
-
gene prgA, overexpression of C-terminally His6-tagged wild-type and mutant A47Q enzymes in Escherichia coli strain BL21(DE3) cytosol
-
gene CagahA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Saccharomyces cerevisiae strain INVSc
-
gene CngahA, a single copy gene in the chromosomal DNA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Saccharomyces cerevisiae strain INVSc
-
;
P0A6W0, P77454
expression analysis of glutaminase isoenzymes in tumor cells by competitive RT-PCR, overview
-
expression in yeast strain EGY48
O14907
expression of FLAG-tagged KGA in 293T cells
O94925
expression of GAC in Spodoptera frugiperda Sf9 cells
-, O94925
expression of HA-tagged or FLAG-tagged wild-type and mutant kidney-type glutaminase in 293T cells
-
human L-type isoform expressed in baculovirus yields functional recombinant enzyme in Sf9 insect cells. Recombinant human glutaminase is targeted to both mitochondria and nucleus, and in both locations the protein is catalytically active
-
overexpression of GLS2 reduces the growth of tumor cells and colony formation
-
the L gene, encoding the liver-type isozyme, is cloned from a brain library and is located on chromosome 12, while the kidney-type isozy
-
heterologously expressed in Lactobacillus plantarum KLB213 which exhibits a high salt-tolerance and Lactobacillus paracasei KLB58 which produces high amount of exopolysaccharide
-
expression in Escherichia coli
-
expression in Escherichia coli strain JM109
-
expression of wild-type and mutant enzymes in Escherichia coli strain JM109
-
high-expression in Escherichia coli
-
overexpression in Escherichia coli
-
GLS1 gene, cloning from genomic library, quantitative expression analysis
-
mouse nitrilase 2 is expressed as a His-tagged fusion protein in Escherichia coli and in HEK-293T cells
-
expression in Escherichia coli
-
expressed in Escherichia coli
-
gene trpG, expression of His-tagged wild-type TrpG and mutant TrpG variants T129F and T129A in Escherichia coli strain BL21(DE3)Rosetta
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GLS2 expression is reduced in liver tumors
-
GLS2 expression is lost or greatly decreased in hepatocellular carcinomas and the overexpression of GLS2 greatly reduces tumor cell colony formation
-
p53 increases the GLS2 expression under both nonstressed and stressed conditions
-
is induced in response to DNA damage or oxidative stress in a p53-dependent manner, and p53 associates with the GLS promotor
-
wild-type TrpG shows no constitutive activity and needs to be induced by TrpE
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A47Q
-
site-directed mutagenesis, structure analysis, mutant crystal foms A47Q-1 and A47Q-2 at pH 6.7 and pH 8.6, respectively, overview
G261A
P0A6W0, P77454
54,7% wild-type activity, Km: 23.7 mM
Q162A
P0A6W0, P77454
wild-type level of activity
S260A
P0A6W0, P77454
16.5% of wild-type activity
S66A
P0A6W0, P77454
very low activity
Y29A
P0A6W0, P77454
32.5% of wild-type activity
G261A
Escherichia coli W3110
-
54,7% wild-type activity, Km: 23.7 mM
-
Q162A
Escherichia coli W3110
-
wild-type level of activity
-
S260A
Escherichia coli W3110
-
16.5% of wild-type activity
-
S66A
Escherichia coli W3110
-
very low activity
-
Y29A
Escherichia coli W3110
-
32.5% of wild-type activity
-
E599A
-
site-directed mutagenesis
F322S/F318Y
-, O94925
site-directed mutagenesis, mutant of GLS1 splice variant GAC, the mutant is not inhibited by bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide in comtrast to the wild-type enzyme
F327S
-
the gain-of-function GAC mutant shows a Km as low as 8.2 mM, even in the absence of phosphate and at only 5 nM protein concentration
L321A/F322A/L323
-
site-directed mutagenesis
M601A
-
site-directed mutagenesis
S600A
-
site-directed mutagenesis
V602A
-
site-directed mutagenesis
Y394L
-, O94925
site-directed mutagenesis, mutant of GLS1 splice variant GAC, the mutant is not inhibited by bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide in comtrast to the wild-type enzyme
E160D
-
inactive mutant enzyme; mutant enzyme with largely decreased catalytic activity, kcat/Km is 1167fold lower than wild-type value
K67E
-
site-directed mutagenesis, catalytic residue mutant, inactiv
K67E
-
inactive mutant enzyme
S64A
-
site-directed mutagenesis, catalytic residue mutant, inactiv
S64A
-
inactive mutant enzyme
Y191F
-
kcat/Km is 39fold lower than wild-type value
Y191T
-
kcat/Km is 67742fold lower than wild-type value
E160D
Micrococcus luteus K-3
-
inactive mutant enzyme; mutant enzyme with largely decreased catalytic activity, kcat/Km is 1167fold lower than wild-type value
-
K67E
Micrococcus luteus K-3
-
inactive mutant enzyme; site-directed mutagenesis, catalytic residue mutant, inactiv
-
S64A
Micrococcus luteus K-3
-
inactive mutant enzyme; site-directed mutagenesis, catalytic residue mutant, inactiv
-
L126G
-
site-directed mutagenesis, the mutant shows constitutive activity unlike the wild-type enzyme and does not require presence of TrpE
L126G/V127Y/T129Y/Y131V
-
site-directed mutagenesis, the mutant shows constitutive activity unlike the wild-type enzyme and does not require presence of TrpE
T129Y
-
site-directed mutagenesis, the mutant shows constitutive activity unlike the wild-type enzyme and does not require presence of TrpE
V127Y
-
site-directed mutagenesis, the mutant shows no constitutive activity like the wild-type enzyme and requires presence of TrpE
Y131V
-
site-directed mutagenesis, the mutant shows no constitutive activity like the wild-type enzyme and requires presence of TrpE
Y191T
Micrococcus luteus K-3
-
kcat/Km is 67742fold lower than wild-type value
-
additional information
-
construction of GLS1-knockout mice using W9.5 embryonic stem ES cells and C57BL6/J blastocysts, mice lacking brain/kidney phosphate-activated glutaminase have impaired glutamatergic synaptic transmission, altered breathing, disorganized goal-directed behavior and die shortly after birth, the amplitude of inspirations is decreased in vivo, chemosensitivity to CO2 is severely altered, and the frequency of pacemaker activity recorded in the respiratory generator in the in vitro isolated pre-Boetzinger complex, a glutamatergic brainstem network, is increased, phenotypic characterization of GLS1 neonate mutant mice, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
the enzyme from Aspergillus oryzae is important in soy sauce fermentation
food industry
-, Q65NY1
microbial glutaminases are enzymes with emerging potential in both the food and the pharmaceutical industries, potential application for bioconversion of glutamine to flavor-enhancing glutamic acid
food industry
Bacillus licheniformis DSM13
-
microbial glutaminases are enzymes with emerging potential in both the food and the pharmaceutical industries, potential application for bioconversion of glutamine to flavor-enhancing glutamic acid
-
medicine
-
acivicin along with Escherichia coli glutaminase synergistically reduces in vitro proliferation and matrigel invasion of human MCF-7 and OAW-42 cells. Combination of acivicin with glutaminase may provide a better therapeutic option than either of them separately for treating human breast and ovarian cancer
medicine
-
enzyme therapy at the dose of 10 unit/mouse in ascites tumor bearing mice, elicits a reduction in tumor growth. At day 5, 10 and 15 it is reduced by 60%, 95% and 89% respectively. The life span of the enzyme treated mice increases significantly with respect to control mice
nutrition
-
the enzyme is applicated in Japanese soy sauce fermentation
medicine
-
depresses some pro-inflammatory factors that occur during prolonged, exhaustive exercise
additional information
-
production of enzymically hydrolyzed plant proteins to reach high glutamic acid yields
additional information
-
food-processing industry, increases the amount of the savory flavoring L-glutamic acid
additional information
Micrococcus luteus K-3
-
food-processing industry, increases the amount of the savory flavoring L-glutamic acid
-
nutrition
Stenotrophomonas maltophilia NYW-81
-
the enzyme is applicated in Japanese soy sauce fermentation
-
additional information
-
Streptomyces rimosus strain LG-10 is a candidate for industrial production of extracellular L-glutaminase
additional information
Streptomyces rimosus LG-10
-
Streptomyces rimosus strain LG-10 is a candidate for industrial production of extracellular L-glutaminase
-