Information on EC 3.5.1.44 - protein-glutamine glutaminase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
3.5.1.44
-
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RECOMMENDED NAME
GeneOntology No.
protein-glutamine glutaminase
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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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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.
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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
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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
-
-
?
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
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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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-
-
-
?
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
-
-
-
-
?
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
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-
-
-
?
L-Leu-Gly-L-Gln + H2O
L-Leu-Gly-L-Gln + NH3
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
protein L-glutamine + H2O
protein L-glutamate + NH3
show the reaction diagram
soybean protein SPI Profam 974, 43.7% degree of deamidation
-
-
?
skim milk + H2O
? + NH3
show the reaction diagram
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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
-
-
?
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
-
-
-
-
?
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
?
-
-
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
-
-
NH4+
-
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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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44
-
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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
calculated from amino acid sequence
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19860
-
calculated from amino acid sequence
51000
-
2 * 51000, peptidoglutaminase II, SDS-PAGE
105000
-
equilibrium sedimentation
110000
-
gel filtration
125000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 51000, peptidoglutaminase II, SDS-PAGE
monomer
-
1 * 19860, calculated from amino acid sequence
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
-
1°C, 22 h, stable
288897
6 - 8
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40°C, 1 h, stable
288897
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
10 min, stable up to
50
-
10 min, complete inactivation
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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
-
deamination of food proteins after treatment at 100°C for 15 min followed by proteolysis and alkali solubilization
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LINKS TO OTHER DATABASES (specific for EC-Number 3.5.1.44)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)