Information on EC 3.5.1.44 - protein-glutamine glutaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.44
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RECOMMENDED NAME
GeneOntology No.
protein-glutamine glutaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protein L-glutamine + H2O = protein L-glutamate + NH3
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amide bond
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-
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SYSTEMATIC NAME
IUBMB Comments
protein-L-glutamine amidohydrolase
Specific for the hydrolysis of the gamma-amide of glutamine substituted at the carboxyl position or both the alpha-amino and carboxyl positions, e.g., L-glutaminylglycine and L-phenylalanyl-L-glutaminylglycine.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-11-0
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
effect of the enzymatic deamidation by protein-glutaminase on flavor-binding properties of soy protein isolate under aqueous conditions, overview. The partial deamidation of soybean protein by the enzyme decreases the overall flavor-binding affinity at 25°C for both vanillin and maltol by approximately 9 and 4fold, respectively. Deamidation of soy protein causes a change in the mechanism of binding from hydrophobic interactions or covalent bonding (Schiff base formation) to weaker van der Waals forces or hydrogen bonding, thermodynamics, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-casein + H2O
? + NH3
show the reaction diagram
-
protein-glutaminase deamidation induces the dissociation of casein micelle resulting in an increase of the oil/water surface area
-
-
?
alpha-lactalbumin + H2O
? + NH3
show the reaction diagram
alpha-zein + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gln-Gly + H2O
benzyloxycarbonyl-Glu-Gly + NH3
show the reaction diagram
benzyloxycarbonyl-L-Gln + H2O
benzyloxycarbonyl-L-Glu + NH3
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Gln-Gly + H2O
benzyloxycarbonyl-L-Glu-Gly + NH3
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Gln-Gly methyl ester + H2O
benzyloxycarbonyl-L-Glu-Gly methyl ester + NH3
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Gln-L-Pro + H2O
benzyloxycarbonyl-L-Glu-L-Pro + NH3
show the reaction diagram
-
-
-
-
?
beta-casein + H2O
? + NH3
show the reaction diagram
-
protein-glutaminase deamidation induces the dissociation of casein micelle resulting in an increase of the oil/water surface area
-
-
?
beta-lactoglobulin + H2O
? + NH3
show the reaction diagram
-
-
-
-
?
casein + H2O
NH3 + ?
show the reaction diagram
-
after heat treatment at 100°C for 15 min, followed by proteolysis and alkali solubilization
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-
?
gamma-casein + H2O
? + NH3
show the reaction diagram
-
protein-glutaminase deamidation induces the dissociation of casein micelle resulting in an increase of the oil/water surface area
-
-
?
gluten + H2O
deaminated gluten + NH3
show the reaction diagram
gluten + H2O
NH3 + ?
show the reaction diagram
-
after heat treatment at 100°C for 15 min, followed by proteolysis and alkali solubilization
-
-
?
Gly-L-Gln + H2O
Gly-L-Glu + NH3
show the reaction diagram
-
-
-
-
?
insulin + H2O
NH3 + ?
show the reaction diagram
-
two L-Gln in oxidized insulin A chain are attacked
-
-
?
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
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-
-
-
?
L-Gln-Gly + H2O
L-Glu-Gly + NH3
show the reaction diagram
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-
-
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?
L-His-L-Ser-L-Gln-Gly-L-Thr-L-Phe-L-Thr + H2O
L-His-L-Ser-L-Glu-Gly-L-Thr-L-Phe-L-Thr + NH3
show the reaction diagram
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-
-
-
?
L-Ile-L-Gln-L-Asn-L-CysH-L-Pro-L-Leu-Gly-NH2 acetate + H2O
L-Ile-L-Glu-L-Asn-L-CysH-L-Pro-L-Leu-Gly-N-acetate + NH3
show the reaction diagram
-
-
-
-
?
L-Leu-Gly-L-Gln + H2O
L-Leu-Gly-L-Gln + NH3
show the reaction diagram
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-
-
-
?
L-Lys-L-Gln-Gly + H2O
L-Lys-L-Glu-Gly + NH3
show the reaction diagram
-
-
-
-
?
L-Phe-L-Gln-Gly + H2O
L-Phe-L-Glu-Gly + NH3
show the reaction diagram
-
-
-
-
?
L-phthaloyl-L-Gln-L-Ala + H2O
L-phthaloyl-L-Glu-L-Ala + NH3
show the reaction diagram
-
-
-
-
?
L-Pro-L-Gln + H2O
L-Pro-L-Glu + NH3
show the reaction diagram
-
-
-
-
?
L-Ser-L-Gln-Gly + H2O
L-Ser-L-Glu-Gly + NH3
show the reaction diagram
-
-
-
-
?
L-Tyr-L-Gln + H2O
L-Tyr-L-Glu + NH3
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Gln + H2O
N-acetyl-L-Glu + NH3
show the reaction diagram
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-
-
-
?
protein L-glutamine + H2O
protein L-glutamate + NH3
show the reaction diagram
soybean protein SPI Profam 974, 43.7% degree of deamidation
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-
?
skim milk + H2O
? + NH3
show the reaction diagram
-
protein-glutaminase catalyzes the deamidation of glutamine residues in skim milk proteins
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-
?
soy protein + H2O
? + NH3
show the reaction diagram
-
-
-
-
?
soy protein + H2O
NH3 + ?
show the reaction diagram
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after heat treatment at 100°C for 15 min, followed by proteolysis and alkali solubilization
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-
?
tert-amyloxycarbonyl-L-Gln-L-Leu-Gly + H2O
tert-amyloxycarbonyl-L-Gln-L-Leu-Gly + NH3
show the reaction diagram
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-
-
?
tert-amyloxycarbonyl-L-Gln-Pro + H2O
tert-amyloxycarbonyl-L-Glu-Pro + NH3
show the reaction diagram
-
-
-
-
?
Z-Gln-Gly + H2O
? + NH3
show the reaction diagram
-
-
-
-
?
Z-Glu-Gly + H2O
? + NH3
show the reaction diagram
-
-
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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-
protein-glutaminase catalyzes only the deamidation of the side chain amido group of protein-bound glutaminyl residues to release ammonia without catalyzing the transglutamination and hydrolysis of asparaginyl residues or producing other undesirable changes in protein structure
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-bromosuccinimide
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NH4+
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competitive inhibitor
sodium lauryl sulfate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.57
benzyloxycarbonyl-D-Gln
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22.2
benzyloxycarbonyl-L-Gln
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-
0.12
benzyloxycarbonyl-L-Gln-Gly
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1.25
benzyloxycarbonyl-L-Gln-Gly methyl ester
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-
0.21
benzyloxycarbonyl-L-Gln-L-Pro
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18.2
Gly-L-Gln
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5 - 50
L-Gln
0.66
L-Gln-Gly
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50
L-His-L-Ser-L-Gln-Gly-L-Thr-L-Phe-L-Thr
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44
L-Ile-L-Gln-L-Asn-L-CysH-L-Pro-L-Leu-Gly-N-acetate
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0.09
L-Lys-L-Gln-Gly
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0.12
L-Phe-L-Gln-Gly
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22.2
L-Pro-L-Gln
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0.12
L-Ser-L-Gln-Gly
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10
L-Tyr-L-Gln
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14.3
N-acetyl-L-Gln
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16.7
tert-amyloxycarbonyl-L-Gln-L-Leu-Gly
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0.12
tert-amyloxycarbonyl-L-Gln-L-Pro
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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optimal conditions based on achieving a high degree of deamidation with a concurrently low degree of hydrolysis are 44°C, enzyme:substrate ratio of 40 units/g protein and pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44
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optimal conditions based on achieving a high degree of deamidation with a concurrently low degree of hydrolysis are 44°C, enzyme:substrate ratio of 40 units/g protein and pH 7.0
50
-
hydrolysis of tert-amyloxycarbonyl-L-Gln-L-Pro
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
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calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19860
-
calculated from amino acid sequence
51000
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2 * 51000, peptidoglutaminase II, SDS-PAGE
105000
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equilibrium sedimentation
110000
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gel filtration
125000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 51000, peptidoglutaminase II, SDS-PAGE
monomer
-
1 * 19860, calculated from amino acid sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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a glycoprotein containing 2 mol of galactose and 11 mol of glucosamine per mol of enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
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1°C, 22 h, stable
288897
6 - 8
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40°C, 1 h, stable
288897
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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10 min, stable up to
50
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10 min, complete inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Chryseobacterium proteolyticum pro-protein-glutaminase fails to be secreted from Chryseobacterium glutamicum using a Sec-pathway dependent signal peptide. It is efficiently secreted in a Tat-dependent manner when fused with a twin-arginine signal peptide. Protein production using the Tat pathway in Chryseobacterium glutamicum may be useful for industrial-scale protein production
expressed in Corynebacterium glutamicum
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
nutrition
synthesis
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deamination of food proteins after treatment at 100°C for 15 min followed by proteolysis and alkali solubilization
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