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Information on EC 3.5.1.2 - glutaminase and Organism(s) Escherichia coli and UniProt Accession P77454

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.2 glutaminase
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Select one or more organisms in this record:
This record set is specific for:
Escherichia coli
UNIPROT: P77454 not found.
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
phosphate-activated glutaminase, l-glutaminase, mitochondrial glutaminase, phosphate activated glutaminase, glutaminase 1, kidney-type glutaminase, glutaminase a, glnase, glutaminase c, glutaminase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GLS
-
-
-
-
glutaminase
288962, 288966
-
glutaminase I
-
-
-
-
glutamine aminohydrolase
-
-
-
-
K-glutaminase
-
-
-
-
L-glutaminase
-
-
-
-
L-glutamine amidohydrolase
-
-
-
-
PAG
-
-
-
-
phosphate activated glutaminase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamine + H2O = L-glutamate + NH3
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamine amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-47-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
?
gamma-ethyl glutamate + H2O
Glu + ethanol
show the reaction diagram
-
-
-
-
?
gamma-ethyl glutamate + hydroxylamine
gamma-glutamyl hydroxamate + ethanol
show the reaction diagram
-
-
-
-
?
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 + 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
-
-
-
-
?
Glu + hydroxylamine
gamma-glutamyl hydroxamate + H2O
show the reaction diagram
-
-
-
-
?
L-Gln + hydroxylamine
L-gamma-glutamyl hydroxamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamate-p-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-diazo-5-oxo-L-norleucine
-
6-diazo-5-oxo-L-norleucine
Hg2+
-
0.1 mM, complete inhibition
Ngamma,Ngamma-diethyl-L-glutamine
-
-
Ngamma,Ngamma-dimethyl-L-glutamine
-
-
Ngamma-ethyl-L-glutamine
-
-
Ngamma-methyl-L-glutamine
-
-
p-mercuribenzoate
-
0.1 mM, complete inhibition, presence of Gln prevents inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
slight activation
dithiothreitol
-
slight activation
EDTA
-
slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.3 - 23.7
L-glutamine
50
gamma-ethyl glutamate
-
-
12
gamma-glutamyl hydrazide
-
-
3.3
gamma-glutamyl methylamide
-
-
64
gamma-methyl glutamate
-
-
23
gamma-thioethyl glutamate
-
-
10
gamma-thiomethyl glutamate
-
-
0.42
Gln
-
-
2.9
Glu
-
-
30.6
L-glutamine
-
additional information
additional information
-
effect of pH on Km-value
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
49.9 - 91.4
L-glutamine
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
-
-
1270
Gln
-
-
5080
Glu
-
-
101
L-glutamine
-
additional information
additional information
-
effect of pH on turnover number
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5
ampicillin
competitive inhibitor
2.95
Ngamma,Ngamma-diethyl-L-glutamine
-
37°C, pH 7.5
2.64
Ngamma,Ngamma-dimethyl-L-glutamine
-
37°C, pH 7.5
1.58
Ngamma-ethyl-L-glutamine
-
37°C, pH 7.5
1.11
Ngamma-methyl-L-glutamine
-
37°C, pH 7.5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
Mg2+
Escherichia coli
P0A6W0, P77454
-
0.1
Mn2+
Escherichia coli
P0A6W0, P77454
-
17.2 - 17.4
PO43-
Escherichia coli
P0A6W0, P77454
-
1.7 - 5.5
Mg2+
Escherichia coli
P0A6W0, P77454
-
0.7 - 1.3
Mn2+
Escherichia coli
P0A6W0, P77454
-
39
Ngamma,Ngamma-diethyl-L-glutamine
Escherichia coli
-
37°C, pH 7.5
35
Ngamma,Ngamma-dimethyl-L-glutamine
Escherichia coli
-
37°C, pH 7.5
24
Ngamma-ethyl-L-glutamine
Escherichia coli
-
37°C, pH 7.5
20
Ngamma-methyl-L-glutamine
Escherichia coli
-
37°C, pH 7.5
17.2 - 17.4
PO43-
Escherichia coli
P0A6W0, P77454
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 9
-
hydrolysis of Gln, glutaminase B
8.3 - 9.2
-
formation of gamma-glutamyl hydroxamate from L-Gln and NH2OH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
-
pH 6.0: about 55% of maximal activity, pH 11.0: about 55% of maximal activity, hydrolysis of Gln
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32900
4 * 32900, SDS-PAGE
148800
gel filtration
33500
2 * 33500, SDS-PAGE
74900
gel filtration
90000
-
glutaminase B, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 32900, SDS-PAGE
homodimer
2 * 33500, SDS-PAGE
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G261A
54,7% wild-type activity, Km: 23.7 mM
Q162A
wild-type level of activity
S260A
16.5% of wild-type activity
S66A
very low activity
Y29A
32.5% of wild-type activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
low level of activity after partial purification at 4°C in absence of stabilizing ligands, warming at 24°C results in 2fold to 5fold increase in activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
significant loss of activity upon freezing at -20°C and -80°C in presence and absence of 20% glycerol
-
sodium borate is the most effective stabilizing agent against cold inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stable at -196°C (unstable at -80°C)
4°C, in presence of sodium borate, stable for 5 days
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
glutaminase B
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Prusiner, S.; Davis, J.N.; Stadtman, E.R.
Regulation of glutaminase B in Escherichia coli. I. Purification, properties, and cold lability
J. Biol. Chem.
251
3447-3456
1976
Escherichia coli
Manually annotated by BRENDA team
Hartman, S.C.
Glutaminases and gamma-glutamyltransferases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
79-100
1971
Escherichia coli
-
Manually annotated by BRENDA team
Roy, S.; Ghosh, S.; Mallick, P.; Maity, P.
Acivicin with glutaminase regulates proliferation and invasion of human MCF-7 and OAW-42 cells-an in vitro study
Indian J. Exp. Biol.
46
22-26
2008
Escherichia coli
Manually annotated by BRENDA team
Brown, G.; Singer, A.; Proudfoot, M.; Skarina, T.; Kim, Y.; Chang, C.; Dementieva, I.; Kuznetsova, E.; Gonzalez, C.F.; Joachimiak, A.; Savchenko, A.; Yakunin, A.F.
Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis
Biochemistry
47
5724-5735
2008
Bacillus subtilis 168 (O07637), Bacillus subtilis 168 (O31465), Bacillus subtilis, Bacillus subtilis (O07637), Bacillus subtilis (O31465), Escherichia coli, Escherichia coli (P0A6W0), Escherichia coli (P77454), Escherichia coli W3110 / ATCC 27325 (P0A6W0), Escherichia coli W3110 / ATCC 27325 (P77454)
Manually annotated by BRENDA team
Prokop, M.; Czarnecka, J.; Milewska, M.
Ngamma-alkyl derivatives of L-glutamine as inhibitors of glutamine-utilizing enzymes
Z. Naturforsch. C
64
631-636
2009
Escherichia coli
Manually annotated by BRENDA team
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