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Information on EC 3.5.1.44 - protein-glutamine glutaminase
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3.5.1.44 protein-glutamine glutaminaseIUBMB Comments
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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Word Map
- 3.5.1.44
-
deamidation
- chryseobacterium
- proteolyticum
- amide
- food industry
- maltol
-
repulsion
-
glutenin
- glutamicum
-
tat-dependent
-
twin-arginine
-
glutaminyl
-
emulsification
- vanillin
- spi
-
enzyme:substrate
-
emulsifying
-
fourier
-
viscosity
-
pro-sequence
- gliadin
- nutrition
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
PG, pro-PG, pro-protein glutaminase, protein glutaminase, protein-glutaminase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PG
protein-glutaminase
protein-glutaminase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein L-glutamine + H2O = protein L-glutamate + NH3
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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.
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CAS REGISTRY NUMBER
COMMENTARY
62213-11-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-casein + H2O
? + NH3
-
protein-glutaminase deamidation induces the dissociation of casein micelle resulting in an increase of the oil/water surface area
-
-
?
benzyloxycarbonyl-L-Gln + H2O
benzyloxycarbonyl-L-Glu + NH3
-
-
-
-
?
benzyloxycarbonyl-L-Gln-Gly + H2O
benzyloxycarbonyl-L-Glu-Gly + NH3
-
-
-
-
?
benzyloxycarbonyl-L-Gln-Gly methyl ester + H2O
benzyloxycarbonyl-L-Glu-Gly methyl ester + NH3
-
-
-
-
?
benzyloxycarbonyl-L-Gln-L-Pro + H2O
benzyloxycarbonyl-L-Glu-L-Pro + NH3
-
-
-
-
?
beta-casein + H2O
? + NH3
-
protein-glutaminase deamidation induces the dissociation of casein micelle resulting in an increase of the oil/water surface area
-
-
?
casein + H2O
NH3 + ?
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after heat treatment at 100°C for 15 min, followed by proteolysis and alkali solubilization
-
-
?
gamma-casein + H2O
? + NH3
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protein-glutaminase deamidation induces the dissociation of casein micelle resulting in an increase of the oil/water surface area
-
-
?
gluten + H2O
NH3 + ?
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after heat treatment at 100°C for 15 min, followed by proteolysis and alkali solubilization
-
-
?
insulin + H2O
NH3 + ?
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two L-Gln in oxidized insulin A chain are attacked
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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
-
-
-
-
?
L-Ile-L-Gln-L-Asn-L-Cys-L-Pro-L-Leu-Gly-NH2 + H2O
L-Ile-L-Gln-L-Asn-L-Cys-L-Pro-L-Leu-Gly + NH3
-
-
-
-
?
L-pyroglutamyl-L-Gln-L-Ala + H2O
L-pyroglutamyl-L-Glu-L-Ala + NH3
-
-
-
-
?
protein L-glutamine + H2O
protein L-glutamate + NH3
soybean protein SPI Profam 974, 43.7% degree of deamidation
-
-
?
skim milk + H2O
? + NH3
-
protein-glutaminase catalyzes the deamidation of glutamine residues in skim milk proteins
-
-
?
soy protein + H2O
NH3 + ?
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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
-
-
-
-
?
tert-amyloxycarbonyl-L-Gln-Pro + H2O
tert-amyloxycarbonyl-L-Glu-Pro + NH3
-
-
-
-
?
alpha-lactalbumin + H2O
? + NH3
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glutamine residues Gln2, Gln39, Gln43, Gln54, Gln65, and Gln117, in alpha-lactalbumin can be modified by protein-glutaminase (Gln117 is the most reactive)
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-
?
alpha-zein + H2O
?
-
insoluble substrate from maize, deamination up to 62% in presence of 11.7% ethanol, the deaminated product becomes more soluble
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-
?
alpha-zein + H2O
?
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insoluble substrate from maize, deamination up to 62% in presence of 11.7% ethanol, the deaminated product becomes more soluble
-
-
?
benzyloxycarbonyl-Gln-Gly + H2O
benzyloxycarbonyl-Glu-Gly + NH3
-
-
-
-
?
benzyloxycarbonyl-Gln-Gly + H2O
benzyloxycarbonyl-Glu-Gly + NH3
-
-
-
?
benzyloxycarbonyl-Gln-Gly + H2O
benzyloxycarbonyl-Glu-Gly + NH3
-
-
-
-
?
additional information
?
-
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no activity against high molecular weight substrates
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-
-
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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-
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additional information
?
-
-
the enzyme catalyzes the incorporation of 15N-labeled ammonium ions into reactive glutamine amide groups
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-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
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
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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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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PDB
SCOP
CATH
UNIPROT
ORGANISM
Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
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
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
nutrition
synthesis
-
deamination of food proteins after treatment at 100°C for 15 min followed by proteolysis and alkali solubilization
food industry
-
in food industry, protein deamination is regarded as a promising method to improve protein functionality (solubility, emulsion, foam and gelling properties) desired in food systems. The enzyme produced from Chryseobacterium proteolyticum is not toxigenic so that consumer safety is assured. The enzyme can be reproducibly produced and purified into a consistent enzyme product
food industry
-
protein-glutaminase is contributes to improving the quality of various dairy products such as yoghurt, cheese, acid milk drinks, etc. Deamidation by protein-glutaminase improves the emulsion capacity of skim milk solution
food industry
-
in food industry, protein deamination is regarded as a promising method to improve protein functionality (solubility, emulsion, foam and gelling properties) desired in food systems. The enzyme produced from Chryseobacterium proteolyticum is not toxigenic so that consumer safety is assured. The enzyme can be reproducibly produced and purified into a consistent enzyme product
-
nutrition
-
the enzyme might be useful to improve solubility and susceptibility of zeins from maize, which have high antioxidant potential and important functional properties in nutrition
nutrition
-
the enzyme might be useful to improve solubility and susceptibility of zeins from maize, which have high antioxidant potential and important functional properties in nutrition
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kikuchi, M.; Sakaguchi, K.
Peptidoglutaminase (Bacillus circulans)
Methods Enzymol.
45B
485-492
1976
Bacillus circulans
brenda
Kikuchi, M.; Sakaguchi, K.
Chemical and physical properties of peptidoglutaminase I and II from Bacillus circulans
Biochim. Biophys. Acta
427
285-294
1976
Bacillus circulans
brenda
Kikuchi, M.; Sakaguchi, K.
Some enzymatic properties and substrate specificities of peptidoglutaminase-I and II
Agric. Biol. Chem.
37
1813-1821
1973
Bacillus circulans
-
brenda
Kikuchi, M.; Sakaguchi, K.
Peptidoglutaminase-I and II: Isolation in homogeneous form
Agric. Biol. Chem.
37
827-835
1973
Bacillus circulans
-
brenda
Kikuchi, M.; Hayashida, H.; Nakano, E.; Sakaguchi, K.
Peptidoglutaminase. Enzymes for selective deamidation of gamma-amide of peptide-bound glutamine
Biochemistry
10
1222-1229
1971
Bacillus circulans
brenda
Hamada, J.S.
High performance liquid chromatography of Bacillus circulans peptidoglutaminase for laboratory and industrial uses
J. Chromatogr. A
702
163-172
1995
Bacillus circulans
-
brenda
OæShaughnessy, A.J.; Gill, B.P.; Headon, D.R.
An assessment of the potential of peptidoglutaminase II in modifying the charge characteristics of proteins
Biochem. Soc. Trans.
13
498
1985
Bacillus circulans
-
brenda
Hamada, J.S.
Effects of heat and proteolysis on deamidation of food proteins using peptidoglutaminase
J. Agric. Food Chem.
40
719-723
1992
Bacillus circulans
-
brenda
Yong, Y.H.; Yamaguchi, S.; Gu, Y.S.; Mori, T.; Matsumura, Y.
Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of alpha-zein
J. Agric. Food Chem.
52
7094-7100
2004
Chryseobacterium proteolyticum, Chryseobacterium proteolyticum 9670
brenda
Kikuchi, Y.; Itaya, H.; Date, M.; Matsui, K.; Wu, L.F.
Production of Chryseobacterium proteolyticum protein-glutaminase using the twin-arginine translocation pathway in Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
78
67-74
2008
Chryseobacterium proteolyticum, Chryseobacterium proteolyticum (Q9AQQ8)
brenda
Yong, Y.H.; Yamaguchi, S.; Matsumura, Y.
Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten
J. Agric. Food Chem.
54
6034-6040
2006
Chryseobacterium proteolyticum, Chryseobacterium proteolyticum 9670
brenda
Scheuplein, R.J.; Mizutani, A.; Yamaguchi, S.
Studies on the non-pathogenicity of Chryseobacterium proteolyticum and on the safety of the enzyme: protein-glutaminase
Regul. Toxicol. Pharmacol.
49
79-89
2007
Chryseobacterium proteolyticum, Chryseobacterium proteolyticum 9670
brenda
Kikuchi, Y.; Itaya, H.; Date, M.; Matsui, K.; Wu, L.F.
TatABC overexpression improves Corynebacterium glutamicum Tat-dependent protein secretion
Appl. Environ. Microbiol.
75
603-607
2009
Corynebacterium glutamicum
brenda
Miwa, N.; Yokoyama, K.; Wakabayashi, H.; Nio, N.
Effect of deamidation by protein-glutaminase on physicochemical and functional properties of skim milk
Int. Dairy J.
20
393-399
2010
Chryseobacterium proteolyticum
-
brenda
Kumeta, H.; Miwa, N.; Ogura, K.; Kai, Y.; Mizukoshi, T.; Shimba, N.; Suzuki, E.; Inagaki, F.
The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum
J. Biomol. NMR
46
251-255
2010
Chryseobacterium proteolyticum
brenda
Suppavorasatit, I.; De Mejia, E.G.; Cadwallader, K.R.
Optimization of the enzymatic deamidation of soy protein by protein-glutaminase and its effect on the functional properties of the protein
J. Agric. Food Chem.
59
11621-11628
2011
Chryseobacterium proteolyticum
brenda
Miwa, N.; Shimba, N.; Nakamura, M.; Yokoyama, K.; Nio, N.; Suzuki, E.; Sonomoto, K.
Incorporation of 15N-labeled ammonia into glutamine amide groups by protein-glutaminase and analysis of the reactivity for alpha-lactalbumin
J. Agric. Food Chem.
59
12752-12760
2011
Chryseobacterium proteolyticum
brenda
Suppavorasatit, I.; Cadwallader, K.R.
Effect of enzymatic deamidation of soy protein by protein-glutaminase on the flavor-binding properties of the protein under aqueous conditions
J. Agric. Food Chem.
60
7817-7823
2012
Chryseobacterium proteolyticum (Q9AQQ8)
brenda
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