3.5.1.44: protein-glutamine glutaminase
This is an abbreviated version!
For detailed information about protein-glutamine glutaminase, go to the full flat file.
Word Map on EC 3.5.1.44
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3.5.1.44
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deamidation
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chryseobacterium
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proteolyticum
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foaming
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emulsification
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gliadin
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food industry
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emulsifying
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synthesis
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nutrition
- 3.5.1.44
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deamidation
- chryseobacterium
- proteolyticum
-
foaming
-
emulsification
- gliadin
- food industry
-
emulsifying
- synthesis
- nutrition
Reaction
Synonyms
PG, prgA, pro-PG, pro-protein glutaminase, protein glutaminase, protein-glutaminase
ECTree
3.5.1.44 protein-glutamine glutaminaseAdvanced search results
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Substrates Products on EC 3.5.1.44 - protein-glutamine glutaminase
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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
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protein-glutaminase deamidation induces the dissociation of casein micelle resulting in an increase of the oil/water surface area
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-
?
benzyloxycarbonyl-L-Gln + H2O
benzyloxycarbonyl-L-Glu + NH3
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-
-
-
?
benzyloxycarbonyl-L-Gln-Gly + H2O
benzyloxycarbonyl-L-Glu-Gly + NH3
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-
-
-
?
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
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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
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-
?
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
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-
?
gluten + 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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-
?
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-Ile-L-Gln-L-Asn-L-CysH-L-Pro-L-Leu-Gly-N-acetate + H2O
?
-
-
-
-
?
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
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-
?
skim milk + H2O
? + NH3
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protein-glutaminase catalyzes the deamidation of glutamine residues in skim milk proteins
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-
?
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-L-Pro + H2O
tert-amyloxycarbonyl-L-Glu-Pro + 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)
-
-
?
alpha-zein + H2O
?
-
insoluble substrate from maize, deamination up to 62% in presence of 11.7% ethanol, the deaminated product becomes more soluble
-
-
?
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
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-
?
benzyloxycarbonyl-Gln-Gly + H2O
benzyloxycarbonyl-Glu-Gly + NH3
-
-
-
-
?
benzyloxycarbonyl-Gln-Gly + H2O
benzyloxycarbonyl-Glu-Gly + NH3
-
-
-
?
benzyloxycarbonyl-Gln-Gly + H2O
benzyloxycarbonyl-Glu-Gly + NH3
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-
-
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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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?
additional information
?
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the enzyme catalyzes the incorporation of 15N-labeled ammonium ions into reactive glutamine amide groups
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?
additional information
?
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catalytic reaction method conditions optimization with coconut protein as substrate, overview. The main proteins in coconut milk are 11S and 7S globulins, over 80% of globulin is cocosin. The enzyme predominantly acts on the 22 kDa band of the minor globulin 7S
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?
additional information
?
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the microbial enzyme specifically catalyzes deamidation of proteins without protein hydrolysis pretreatment and only reacts with glutamine residues in the side-chains of proteins or long peptides. Strain QSH1265 can produce acid from D-glucose, maltose, L-arabinose, sucrose, glycerol, and mannitol but not fructose, and it is also positive for indole production and urease activity
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-
?
additional information
?
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-
the microbial enzyme specifically catalyzes deamidation of proteins without protein hydrolysis pretreatment and only reacts with glutamine residues in the side-chains of proteins or long peptides. Strain QSH1265 can produce acid from D-glucose, maltose, L-arabinose, sucrose, glycerol, and mannitol but not fructose, and it is also positive for indole production and urease activity
-
-
?
additional information
?
-
Chryseobacterium proteolyticum QSH1265
the microbial enzyme specifically catalyzes deamidation of proteins without protein hydrolysis pretreatment and only reacts with glutamine residues in the side-chains of proteins or long peptides. Strain QSH1265 can produce acid from D-glucose, maltose, L-arabinose, sucrose, glycerol, and mannitol but not fructose, and it is also positive for indole production and urease activity
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-
?
additional information
?
-
-
no activity against high molecular weight substrates
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-
?
