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1-L-beta-aspartamido-(2-acetamido)-1,2-dideoxy-beta-D-galactose + H2O
L-aspartate + NH3 + 2-acetamido-2-deoxy-beta-D-galactose
-
low activity
-
?
1-L-beta-aspartamido-beta-D-galactose + H2O
L-aspartate + beta-D-galactose + NH3
-
-
-
?
1-L-beta-aspartamido-beta-D-glucose + H2O
L-aspartate + beta-D-glucose + NH3
-
high activity
-
?
1-L-beta-aspartamido-beta-D-mannose + H2O
L-aspartate + beta-D-mannose + NH3
-
-
-
?
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose + H2O
?
-
-
-
?
aspartic acid beta-(4-nitroanilide) + H2O
4-nitroaniline + L-aspartate
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
L-aspartic acid beta-(7-amido-4-methylcoumarin) + H2O
7-amino-4-methylcoumarin + L-aspartate
L-aspartic acid-b-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-aspartate
-
-
-
-
?
L-aspartic acid-p-nitrolanilide + H2O
p-nitroaniline + L-aspartate
-
-
-
?
L-aspartyl-beta-(7-amido-4-methylcoumarin) + H2O
L-aspartic acid + 7-amino-4-methylcoumarin
L-aspartylglucosamine + H2O
L-aspartate + glucosamine
N-[alpha-D-Man-(1-3)-alpha-D-Man-(1-6)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc]-L-aspartate + H2O
alpha-D-Man-(1-3)-alpha-D-Man-(1-6)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc + L-aspartate
-
fast hydrolysis rate
-
?
N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O
2-acetamido-2-deoxy-beta-D-glucopyranosylamine + L-asparagine
-
catalyzes the hydrolysis of the N-glycosylic bond
-
-
?
N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O
?
-
catabolism of N-linked oligosaccharides
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
N-acetyl-beta-D-glucosaminylamine + L-aspartate
N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
deficiency in the activity of human GA leads to a lysosomal storage disease aspartylglycosaminuria
-
-
?
N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O
N-acetyl-D-glucosaminylamine + L-aspartate
ovalbumin + H2O
L-aspartate + ?
-
-
-
?
ovalbumin glycopeptide + H2O
L-aspartate + ?
-
intermediate activity
-
?
ribonuclease B glycopeptide + H2O
L-aspartate + ?
-
poor substrate, more activity with the pure glycopeptide
-
?
sialo-transferrin + H2O
L-aspartate + ?
-
intermediate activity
-
?
Taka-amylase + H2O
L-aspartate + ?
-
-
-
?
additional information
?
-
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
2 stages of hydrolysis
non-enzymatic degradation of 1-amino-N-acetylglucosamine to NH3 + N-acetyl-beta-D-glucosamine
ir
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
complex enzyme system in tissue homogenates
-
?
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
no asparaginase activity
?
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
additional product: NH3, in equimolar amounts of N-acetylglucosamine and L-aspartate
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
ir
L-asparagine + H2O
L-aspartate + NH3
-
low activity
-
?
L-asparagine + H2O
L-aspartate + NH3
-
21% activity compared to N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine as substrate
-
r
L-asparagine + H2O
L-aspartate + NH3
-
-
-
ir
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
poor substrate in kidney
-
?
L-aspartic acid beta-(7-amido-4-methylcoumarin) + H2O
7-amino-4-methylcoumarin + L-aspartate
-
-
-
?
L-aspartic acid beta-(7-amido-4-methylcoumarin) + H2O
7-amino-4-methylcoumarin + L-aspartate
-
-
-
?
L-aspartyl-beta-(7-amido-4-methylcoumarin) + H2O
L-aspartic acid + 7-amino-4-methylcoumarin
-
-
-
ir
L-aspartyl-beta-(7-amido-4-methylcoumarin) + H2O
L-aspartic acid + 7-amino-4-methylcoumarin
-
-
-
ir
L-aspartylglucosamine + H2O
L-aspartate + glucosamine
-
-
-
ir
L-aspartylglucosamine + H2O
L-aspartate + glucosamine
-
-
-
ir
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
preferred substrate
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
belongs to N-terminal nucleophile hydrolase family
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
r
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
N-acetyl-beta-D-glucosaminylamine + L-aspartate
-
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
N-acetyl-beta-D-glucosaminylamine + L-aspartate
-
active site structure
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
N-acetyl-beta-D-glucosaminylamine + L-aspartate
-
enzyme catalyzes the hydrolysis of the N-glycosylic bond between asparagine and N-acetylglucosamine, mechanism involving formation of a tetra-hedral high-energy intermediate, presence of a second binding site that may recognize substituted acetamido groups
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
N-acetyl-beta-D-glucosaminylamine + L-aspartate
Thr-206 is the N-terminal nucleophile that acts as catalytic residue, Thr-206 is stabilized by hydrogen bonds from Ser-72 and Thr-224, enzyme structure
-
-
?
N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O
N-acetyl-D-glucosaminylamine + L-aspartate
-
-
-
?
N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O
N-acetyl-D-glucosaminylamine + L-aspartate
-
-
-
?
additional information
?
-
AGA hydrolyzes the beta-N glycosidic linkage between the asparagines residue and the N-acetylglucosamine moiety. The enzyme fails to exhibit any glycopeptide N-glycosidase activity toward entire glycoproteins like fetuin, its activity is restricted to the deglycosylation of free glycosylasparagines like human aspartylglucosaminidase
-
-
?
additional information
?
-
-
AGA hydrolyzes the beta-N glycosidic linkage between the asparagines residue and the N-acetylglucosamine moiety. The enzyme fails to exhibit any glycopeptide N-glycosidase activity toward entire glycoproteins like fetuin, its activity is restricted to the deglycosylation of free glycosylasparagines like human aspartylglucosaminidase
-
-
?
additional information
?
-
-
glycosylasparaginase protein is synthesized as a single-chain precursor (inhibitor-free precursor) and requires a cis proteolysis of its own main-chain amide bond, splitting it into two subunits. Once autocleaved, the mature glycosylasparaginase with a free amino end exposed at Thr152 becomes active in glycoprotein degradation by binding to and processing its glycoasparagine substrate
-
-
?
additional information
?
-
-
enzyme catalyzes the hydrolysis of the N-glycosylic bond between asparagine and N-acetylglucosamine in the catabolism of N-linked glycoproteins
-
-
?
additional information
?
-
-
enzyme catalyzes the hydrolysis of a variety of asparagine and aspartyl compounds containing a free alpha-carboxyl group and a free alpha-amino group, study of enzyme specificity with 14 substrate analogues where the structure of the aspartyl group is changed, the alpha-carboxyl group is necessary for enzyme activity, but not the alpha-amino group, whose position acts as an anchor in the binding site for the substrate, no substrate: N-acetyl-D-glucosamine, intramolecular autoproteolytic activation reaction
-
-
?
additional information
?
-
aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population
-
-
?
additional information
?
-
-
aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population
-
-
?
additional information
?
-
-
enzyme level in plasma is elevated in congenital disorders of glycosylation type I, CDG I, a defect in biosynthesis or processing of O-linked glycans, overview
-
-
?
additional information
?
-
-
glycosylasparaginase hydrolyzes the N-glycosidic carbohydrate-to-protein linkage region, aspartylglucosamine, to L-aspartic acid and L-amino-N-acetylglucosamine through a reaction mechanism similar to L-asparaginase
-
-
?
additional information
?
-
processing and activation of aspartylglucosaminidase by autocatalytic cleavage, overview
-
-
?
additional information
?
-
-
processing and activation of aspartylglucosaminidase by autocatalytic cleavage, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-asparagine + H2O
L-aspartate + NH3
N-[alpha-D-Man-(1-3)-alpha-D-Man-(1-6)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc]-L-aspartate + H2O
alpha-D-Man-(1-3)-alpha-D-Man-(1-6)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc + L-aspartate
-
fast hydrolysis rate
-
?
N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O
?
-
catabolism of N-linked oligosaccharides
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
deficiency in the activity of human GA leads to a lysosomal storage disease aspartylglycosaminuria
-
-
?
N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O
N-acetyl-D-glucosaminylamine + L-aspartate
-
-
-
?
additional information
?
-
L-asparagine + H2O
L-aspartate + NH3
-
low activity
-
?
L-asparagine + H2O
L-aspartate + NH3
-
21% activity compared to N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine as substrate
-
r
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
preferred substrate
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
belongs to N-terminal nucleophile hydrolase family
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
r
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
additional information
?
-
AGA hydrolyzes the beta-N glycosidic linkage between the asparagines residue and the N-acetylglucosamine moiety. The enzyme fails to exhibit any glycopeptide N-glycosidase activity toward entire glycoproteins like fetuin, its activity is restricted to the deglycosylation of free glycosylasparagines like human aspartylglucosaminidase
-
-
?
additional information
?
-
-
AGA hydrolyzes the beta-N glycosidic linkage between the asparagines residue and the N-acetylglucosamine moiety. The enzyme fails to exhibit any glycopeptide N-glycosidase activity toward entire glycoproteins like fetuin, its activity is restricted to the deglycosylation of free glycosylasparagines like human aspartylglucosaminidase
-
-
?
additional information
?
-
-
glycosylasparaginase protein is synthesized as a single-chain precursor (inhibitor-free precursor) and requires a cis proteolysis of its own main-chain amide bond, splitting it into two subunits. Once autocleaved, the mature glycosylasparaginase with a free amino end exposed at Thr152 becomes active in glycoprotein degradation by binding to and processing its glycoasparagine substrate
-
-
?
additional information
?
-
-
enzyme catalyzes the hydrolysis of the N-glycosylic bond between asparagine and N-acetylglucosamine in the catabolism of N-linked glycoproteins
-
-
?
additional information
?
-
aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population
-
-
?
additional information
?
-
-
aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population
-
-
?
additional information
?
-
-
enzyme level in plasma is elevated in congenital disorders of glycosylation type I, CDG I, a defect in biosynthesis or processing of O-linked glycans, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1 - 14
1-L-beta-aspartamido-(2-acetamido)-1,2-dideoxy-beta-D-galactose
0.05 - 1
1-L-beta-aspartamido-(2-acetamido)-1,2-dideoxy-beta-D-glucose
10.8
1-L-beta-aspartamido-beta-D-galactose
-
-
5.7
1-L-beta-aspartamido-beta-D-mannose
-
-
0.143 - 0.444
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose
0.4 - 0.64
2-acetamido-1-N-(4-L-aspartyl)-2-deoxy-beta-D-glycopyranosylamine
0.0449 - 0.0742
L-aspartyl-beta-(7-amido-4-methylcoumarin)
0.09 - 2.5
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
0.09 - 0.26
N4-(beta-N-acetylglucosaminyl)-L-asparagine
additional information
additional information
-
1
1-L-beta-aspartamido-(2-acetamido)-1,2-dideoxy-beta-D-galactose
-
-
14
1-L-beta-aspartamido-(2-acetamido)-1,2-dideoxy-beta-D-galactose
-
-
0.05
1-L-beta-aspartamido-(2-acetamido)-1,2-dideoxy-beta-D-glucose
-
-
0.059
1-L-beta-aspartamido-(2-acetamido)-1,2-dideoxy-beta-D-glucose
-
-
1
1-L-beta-aspartamido-(2-acetamido)-1,2-dideoxy-beta-D-glucose
-
-
0.143
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose
pH 7, 37°C, purified wild-type AGA
0.444
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose
pH 7, 37°C, wild-type AGA
0.4
2-acetamido-1-N-(4-L-aspartyl)-2-deoxy-beta-D-glycopyranosylamine
-
for amidase-3
0.64
2-acetamido-1-N-(4-L-aspartyl)-2-deoxy-beta-D-glycopyranosylamine
-
amidase-1 and amidase-2, value depending on enzyme concentration
0.66
L-asparagine
-
-
1.188
L-asparagine
pH 8.0, temperature not specified in the publication, recombinant enzyme
4.051
L-asparagine
pH 8.0, temperature not specified in the publication, recombinant enzyme
0.0449
L-aspartyl-beta-(7-amido-4-methylcoumarin)
pH 8.0, temperature not specified in the publication, recombinant enzyme
0.0742
L-aspartyl-beta-(7-amido-4-methylcoumarin)
pH 8.0, temperature not specified in the publication, recombinant enzyme
0.09
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
-
-
0.11
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
-
-
0.116
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
-
-
0.16
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
-
at 37°C and pH 7.7, pH- and temperature dependend
0.208
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
-
-
0.538
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
-
at pH 7.5 and 37°C
0.88
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
-
-
1.25
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
-
-
2.5
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
-
-
0.09
N4-(beta-N-acetylglucosaminyl)-L-asparagine
recombinant wild-type enzyme, pH 7.5, 37°C
0.166
N4-(beta-N-acetylglucosaminyl)-L-asparagine
mutant T203I, pH 7.5, 37°C
0.26
N4-(beta-N-acetylglucosaminyl)-L-asparagine
mutant T99K, pH 7.5, 37°C
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics of mutant T203I and wild-type enzymes, the specificity constant (kcat/Km) of mutant T203I is decreased by more than 300fold when compared to the wild-type enzyme
-
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evolution
belongs to the group of so-called N-terminal nucleophile (NTN) hydrolases. The members of the NTN hydrolase family, which in addition to AGA also include, e.g., the proteasome beta-subunit and penicillin acylase, show very little similarity at the amino acid sequence level, but they exhibit a highly similar folded structure
evolution
-
molecular phylogenetic analysis of aspartylglucosaminidases
evolution
the venom AGAs have a similar domain organization as mammalian AGAs. They share key residues for autocatalysis and activity, and the mature alpha- and beta-subunits also form an (alphabeta)2 structure in solution. Only one of the AGAs subunits, the beta for LhAGA, is glycosylated instead of the two subunits for lysosomal human AGA (hAGA)
evolution
the venom AGAs have a similar domain organization as mammalian AGAs. They share with them key residues for autocatalysis and activity, and the mature alpha- and beta-subunits also form an (alphabeta)2 structure in solution. Only one of the AGAs subunits (alpha for AtAGA) is glycosylated instead of the two subunits for lysosomal human AGA (hAGA)
malfunction
-
aspartylglycosaminuria is a lysosomal storage disease caused by deficient activity of glycosylasparaginase
malfunction
enzyme point mutation G172D inactivates the enzyme and causes the genetic disease aspartylglucosaminuria, a lysosomal storage disease due to metabolic disorder of lysosomes to digest Asn-linked glycoproteins, structural basis, overview
malfunction
aspartylglucosaminuria (AGU) is an inherited disease caused by mutations in a lysosomal amidase called aspartylglucosaminidase (AGA) or glycosylasparaginase. This disorder results in an accumulation of glycoasparagines in the lysosomes of virtually all cell types, with severe clinical symptoms affecting the central nervous system, skeletal abnormalities, and connective tissue lesions. Many AGU mutations remain as dimers but cannot undergo autoproteolysis and thus lack amidase activity for digesting glycoasparagines
malfunction
defects in the AGA gene result in a lysosomal storage disorder, aspartylglucosaminuria (AGU), that manifests mainly as progressive mental retardation. A number of AGU missense mutations have been identified that result in reduced AGA activity. Human variants contain either Ser or Thr in position 149, and Thr149 AGA, which is the rare variant, can be considered as a neutral or benign variant. AGU mutations result in reduced AGA activity in patient cells. Mutations in the AGA gene result in aspartylglucosaminuria (AGU, OMIM 208400), a lysosomal storage disorder that is characterized by progressive loss of intellectual capabilities and some skeletal abnormalities. AGU patients are born seemingly normal, but the progressive course of the disease manifests in, e.g., developmental delay, loss of speech and coarse facial features early in childhood. In adulthood, most AGU patients are severely retarded and require special care
malfunction
deficiency of the enzyme causes accumulation of glycoasparagines in lysosomes of cells, resulting in a genetic condition called aspartylglucosaminuria (AGU). AGU is a lysosomal storage disorder caused by defects of the hydrolase glycosylasparaginase. AGU mutations impair autoproteolysis of GA precursor and/or impair its hydrolase activity in lysosomes. This deficiency results in progressive mental decline of the patients, and leads to a lifelong condition affecting patient's appearance, cognition, adaptive skills, physical growth, personality, anatomical structure, and health. Early indicators of AGU include growth spurts in infants and the development of macrocephalia associated to hernias and respiratory infections
malfunction
-
lysosomal acidification inhibitors, chloroquine or bafilomycin A1, disturb medusa morphogenesis at the oral end, suggesting involvement of lysosomal hydrolases in strobilation
physiological function
aspartylglucosaminidase (AGA) is a lysosomal hydrolase that participates in the breakdown of glycoproteins
physiological function
once AGAs are injected into the larvae of the Drosophila melanogaster host, the asparaginase activity may play a role in modulating their physiology
physiological function
once AGAs are injected into the larvae of the Drosophila melanogaster host, the asparaginase activity may play a role in modulating their physiology
physiological function
the enzyme is involved in protein degradation by cleaving Asn-linked glycoproteins in lysosomes. During the metabolic turnover of Asn-linked glycoproteins, autocleaved enzyme hydrolyzes glycoasparagine N4-(beta-N-acetylglucosaminyl)-L-asparagine (NAcGlc-Asn) that connects a carbohydrate to the side chain of an asparagine
physiological function
the enzyme is is involved in protein degradation by catabolizing Asn-linked glycoproteins in lysosomes
physiological function
-
the life cycle of the moon jellyfish, Aurelia aurita, alternates between a benthic asexual polyp stage and a planktonic sexual medusa (jellyfish) stage. Transition from polyp to medusa is called strobilation. Aspartylglucosaminidase (AGA), a lysosomal hydrolase, is upregulated during strobilation
additional information
a surface loop blocks the catalytic center of the mature hydrolase, autoproteolysis is therefore required to remove this P loop and open up the hydrolase center. Structures of the precursor and the mature form are found in a single crystal, structure comparisons, overview
additional information
AGA belongs to the group of so-called N-terminal nucleophile (NTN) hydrolases, as the free alpha-amino group of Thr206 is involved in the catalysis as the base, whereas the OH group of Thr206 functions as a nucleophile during the catalysis
additional information
-
AGA belongs to the group of so-called N-terminal nucleophile (NTN) hydrolases, as the free alpha-amino group of Thr206 is involved in the catalysis as the base, whereas the OH group of Thr206 functions as a nucleophile during the catalysis
additional information
residue T206 is essential for enzyme catalysis and autocatalytic activation, and the W34, R234 and D237 residues, involved in substrate binding, are conserved. Homology structure modeling, structure comparisons, overview
additional information
-
residue T206 is essential for enzyme catalysis and autocatalytic activation, and the W34, R234 and D237 residues, involved in substrate binding, are conserved. Homology structure modeling, structure comparisons, overview
additional information
residues T206 residue, essential for enzyme catalysis and autocatalytic activation, and the W34, R234 and D237 residues, involved in substrate binding, are conserved. Homology structure modeling, structure comparisons, overview
additional information
-
residues T206 residue, essential for enzyme catalysis and autocatalytic activation, and the W34, R234 and D237 residues, involved in substrate binding, are conserved. Homology structure modeling, structure comparisons, overview
additional information
structure comparison of mutant T203I with the wild-type enzyme
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16000
-
alpha1, 1 * 18000 + beta1, 1 * 16000, SDS-PAGE
16500
2 * 20700 + 2 * 16500, calculated from amino acid sequence
19000
-
heavy-chain2, 2 * 25000 + light-chain2, 2 * 19000
20000
-
alpha1, 1 * 24000 + beta1, 1 * 20000, SDS-PAGE
20700
2 * 20700 + 2 * 16500, calculated from amino acid sequence
24600
-
alpha1, 1 * 24600 + beta1, 1 * 18000, SDS-PAGE and heat-inactivation
30000
2 * 30000 + 2 * 18000, active enzyme, SDS-PAGE
36740
deduced polypeptide with the signal peptide cleaved off, calculated from amino acid sequence
38000
-
HPLC/Blue chromatography
56000
-
SDS-PAGE without heat-inactivation
70000
-
disc electrophoresis, ultracentrifugation
76000
-
1 * 76000, SDS-PAGE
780000
-
gel filtration, analytical PAGE
80000
-
non-denaturing PAGE
84000
precursor, SDS-PAGE
88000
-
non-denaturing PAGE
101000
-
gel filtration
101000
-
gel filtration, sucrose density gradient centrifugation
17000
-
alpha 1, 1 * 28000 + beta 1, 1 * 17000, SDS-PAGE
17000
-
alpha2,beta2, 2 * 28000 + 2 * 17000, SDS-PAGE
17000
-
1 * 25000 + 1 * 24000 + 1 * 18000 + 1 * 17000, SDS-PAGE
18000
-
alpha1, 1 * 24600 + beta1, 1 * 18000, SDS-PAGE and heat-inactivation
18000
-
alpha1, 1 * 18000 + beta1, 1 * 16000, SDS-PAGE
18000
-
heavy-chain2, 2 * 25000 + light-chain2, 2 * 18000, SDS-PAGE
18000
-
1 * 25000 + 1 * 24000 + 1 * 18000 + 1 * 17000, SDS-PAGE
18000
2 * 30000 + 2 * 18000, active enzyme, SDS-PAGE
24000
-
alpha1, 1 * 24000 + beta1, 1 * 20000, SDS-PAGE
24000
-
1 * 25000 + 1 * 24000 + 1 * 18000 + 1 * 17000, SDS-PAGE
25000
-
heavy-chain2, 2 * 25000 + light-chain2, 2 * 18000, SDS-PAGE
25000
-
1 * 25000 + 1 * 24000 + 1 * 18000 + 1 * 17000, SDS-PAGE
25000
-
heavy-chain2, 2 * 25000 + light-chain2, 2 * 19000
28000
-
alpha 1, 1 * 28000 + beta 1, 1 * 17000, SDS-PAGE
28000
-
alpha2,beta2, 2 * 28000 + 2 * 17000, SDS-PAGE
44000
1 * 44000, monomeric AGA precursor, SDS-PAGE
44000
2 * 44000, precursor, SDS-PAGE
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phosphoprotein
-
phosphate on high-mannose type glycosyl groups
glycoprotein
two potential N-glycosylation sites are detected along the sequence at Asn52 and Asn153
glycoprotein
only the alpha AGA subunits are glycosylated, and these glycosylations are partially resistant to PGNase F treatment, N-glycosylation sites prediction, overview
glycoprotein
-
Aurelia AGA possesses potential N-glycosylation sites, Asn36, Asn48, Asn168, and Asn213
glycoprotein
-
each polypeptide N-glycosylated
glycoprotein
-
each polypeptide N-glycosylated
glycoprotein
-
mannose-glycosyl groups at N38, T310 and N308
glycoprotein
-
each polypeptide N-glycosylated
glycoprotein
AGA contains two glycosylation sites at Asn38 and Asn308
glycoprotein
only the beta AGA subunits are glycosylated, and these glycosylations are partially resistant to PGNase F treatment, N-glycosylation sites prediction, overview
glycoprotein
-
each polypeptide N-glycosylated
glycoprotein
-
each polypeptide N-glycosylated
glycoprotein
-
each polypeptide N-glycosylated
proteolytic modification
the enzyme is processed through autocatalytic cleavage, extracellular autocleavage and autoactivation
proteolytic modification
-
in the lysosomes, the C-termini of both alpha- and beta-subunits are trimmed by proteases, resulting in the mature form of AGA, though these trimming steps are not necessary for the catalytic activity of AGA
proteolytic modification
-
Asp-151 plays a dual role in the autoproteolytic processing mechanism, acting as the general base to activate the nucleophile and holding the distorted trans conformation that is critical for initiating an N-O acyl shift, generation of a mature/active enzyme from a single-chain precursor, autoproteolysis into two subunits: alpha and beta, mechanism
proteolytic modification
autoproteolytic removal of a surface P loop blocking the catalytic center of the mature hydrolase is required to open up the hydrolase center, wild-type Genzyme autocleaves spontaneously
proteolytic modification
-
intramolecular autoproteolytic activation reaction
proteolytic modification
intramolecular autoproteolytic activation with Gly-258 playing an important structural role, molecular activation mechanism, dimerization and correct folding of the AGA precursor, activation cleavage of the dimerized AGA precursors into the N-terminal alpha- and the C-terminal beta-subunits takes place in the endoplasmic reticulum and results in the tetrameric, enzymically active (alpha,beta)2 molecule
proteolytic modification
the enzyme contains a subcellular targeting signal sequence
proteolytic modification
processing and activation of aspartylglucosaminidase by autocatalytic cleavage, overview. AGA is synthesized in the endoplasmic reticulum as a 346 amino acid (aa) polypeptide from which 23 residues of the signal peptide are removed. Very soon after synthesis in the endoplasmic reticulum, two AGA precursors homodimerize, inducing an autocatalytic cleavage of both precursors N-terminally to Thr206 into 27 kDa pro-alpha and 17 kDa subunits. After transport to lysosomes, the pro-alpha is C-terminally cleaved into 24 kDa mature alpha-subunit, whereas processing of the beta-subunit gives rise to the 14 kDa beta'-subunit. Neither of these lysosomal processing steps displays an effect on the enzyme activity
proteolytic modification
the enzyme is processed through autocatalytic cleavage. A subsequent autoprocessing results in a main-chain cleavage at the P-loop by a self-catalyzed peptide bond rearrangement via an N -> O acyl shift. This autoproteolysis event results in an active form of the hydrolase with separate alpha- and beta-subunits
proteolytic modification
the enzyme is synthesized as a single-chain precursor that requires an intramolecular autoprocessing to form a mature amidase
proteolytic modification
the enzyme is precessed through autocatalytic cleavage, extracellular autocleavage and autoactivation
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D151N
-
mutation completely abolishes autoproteolysis, mutation eradicates the backbone distortion near the scissile peptide bond
T152A
-
autoproteolytically deficient, no hydrolase activity
T152C
-
mutant with lower turnover number to get a crystall in complex with natural substrate
G172D
the naturally occuring point mutation results in misprocessing of its precursor and is deficient in hydrolyzing glycoasparagines, the mutant can be stabilized by L-aspartic acid beta-hydroxamate for crystallization against proteolysis by other enzymes
T203I
the naturally occuring point mutation results in misprocessing of its precursor and is deficient in hydrolyzing glycoasparagines. The mutant shows increased thermostability but 93% reduced enzyme activity compared to the wild-type enzyme. The mutant is unstable to proteolysis by other enzymes
T152C
-
the autoproteolysis-active precursor is kinetically slower than the wild type enzyme
C140S
the substitution is the causative mutation for enzyme deficiency. In addition to preventing the disulfide bond formation between C140 and C156, the C140S substitution also causes destabilization of the unique/longer loop structure in the human sequence and thus prevent dimerization of GA essential for autoproteolytic activation
D200A
87% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
D201A
93% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
D205G
-
essential for activation by autocatalytic proteolytic processing
D70A
44% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
G226A
inactive mutant, study of folding, transport and catalytic kinetics of mutant AGA
G258A
inactive mutant, study of folding, transport and catalytic kinetics of mutant AGA
H124R
-
reduced dimerization of the precursor polypeptide, total secretion into the medium
H124W
-
reduced dimerization of the precursor polypeptide, total secretion into the medium
K230A
86% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
L15R
naturally occuring L15R, mutating the signal sequence, causes aspartylglucosaminuria and affects translocation of aspartylglucosaminidase
N225A
45% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
N308D
-
less than 10% of wild-type activity, misprocessing of precursor
N38D
-
30% of wild-type activity, proper processing to its mature lysosomal form
R138Q
the single mutation does not affect either the enzyme's autoproteolysis or its hydrolase activity
R138Q/C140S
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU). Due to a founder effect, AGU incidence in Finland is unexcelled, with one major allele (denoted AGUFIN) found in 98% of the AGU patients. The AGUFIN allele carries the two concurrent substitutions R138Q andC140S
R161Q/C163S
naturally occuring mutation, the AGUFin-major mutation is a combination of two missense mutations, abolishing a disulfide bond and destabilizing the AGA structure. The pathogenic C163S substitution is always combined with a functionally neutral Arg161Gln substitution. Mutations in the AGA gene result in aspartylglucosaminuria (AGU, OMIM 208400), a lysosomal storage disorder that is characterized by progressive loss of intellectual capabilities and some skeletal abnormalities. AGU patients are born seemingly normal, but the progressive course of the disease manifests in, e.g. developmental delay, loss of speech and coarse facial features early in childhood. In adulthood, most AGU patients are severely retarded and require special care
R234A
-
nearly complete decrease of activity, misprocessing of precursor in ER
R234L
-
nearly complete decrease of activity, misprocessing of precursor in ER
R234Q
-
nearly complete decrease of activity, misprocessing of precursor in ER
S238A
40% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
T224A
-
nearly complete decrease of activity
T224S
-
nearly complete decrease of activity
T257I
naturally occuring mutation in Canadian population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T310A
-
less than 10% of wild-type activity, more properly cleaved form than N308D
T33A
48% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
T33S
same activity as wild-type AGA
G172D
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU)
G172D
site-directed mutagenesis, the mutation causes a local conformational change, which in turn disrupts the requisite autoprocessing step to generate metabolically functional mature hydrolase
G203D
naturally occuring mutation in Canadian population, causing aspartylglucosaminuria (AGU)
G203D
naturally occuring mutation in US-American population causing aspartylglucosaminuria (AGU)
G226D
naturally occuring mutation in Canadian population causing aspartylglucosaminuria (AGU)
G226D
naturally occuring mutation in Canadian population, causing aspartylglucosaminuria (AGU)
T122K
naturally occuring mutation in Canadian population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T122K
naturally occuring mutation in US-American population causing aspartylglucosaminuria (AGU)
T203I
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T203I
site-directed mutagenesis, corresponds to mutation T234I, the replacement of the conserved threonine with an isoleucine has negative impacts on both KM and, to a greater extent, kcat of hydrolase activity, the mutant is almost inactive. Structure comparison of mutant T203I with the wild-type enzyme. Mutant T203I is capable of autoprotolysis. In the T203I-substrate complex model, all the previously identified substrate binding residues (W11, F13, S50, T152, R180, D183, G204, G206) are in close contact distances from the substrate model, except the mutated residue Ile203
T234I
naturally occuring mutation in Canadian population,located at the rim of the substrate binding site , causing aspartylglucosaminuria (AGU). The mutatnt enzyme shows reduced autoprocessing capability compared to wild-type
T234I
naturally occuring mutation in US-American population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T257A
-
nearly complete decrease of activity
T257A
-
nearly complete decrease of activity, misprocessing of precursor in ER
T99K
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T99K
naturally occuring mutation in US-American population causing aspartylglucosaminuria (AGU). This T99K model enzyme still has autoprocessing capacity to generate a mature form, its amidase activity to digest glycoasparagines remains low. A molecular clamp capable of fixing local disorders at the dimer interface might be able to rescue the deficiency of this AGU variant. The mutant lacks the signal peptide, but shows relatively high amidase activity, about 75% compared to wild-type. T99K has its substratebinding site fully opened through autoproteolysis and is ready to accommodate the substrate NAcGlc-Asn
additional information
in vitro activation of autoproteolysis can be applied to enhance the hydrolase activity of the AGU mutant
additional information
aspartylglucosaminuria-causing mutations, most of them lead to defective molecular maturation of AGA, effects of targeted amino acid substitutions on the activation process of AGA
additional information
-
aspartylglucosaminuria-causing mutations, most of them lead to defective molecular maturation of AGA, effects of targeted amino acid substitutions on the activation process of AGA
additional information
construction of a model enzyme corresponding to a Finnish AGU allele, the naturally occuring T234I mutant variant. The Finnish variant is capable of a slow autoprocessing to generate detectible hydrolyzation activity of the natural substrate of the enzyme. Determination of a 1.6 A-resolution structure of the Finnish AGU model and construction of an enzyme-substrate complex to provide a structural basis for analyzing the negative effects of the point mutation on Km and kcat of the mature enzyme, overview
additional information
single nucleotide polymorphism rs2228119 (NM_000027.3:c.446C>G - p.(Thr149Ser)) results in amino acid variation Ser vs. Thr at position 149 (base and amino acid variation in red) of the human AGA enzyme. Functional analysis of the Ser149/Thr149 variants of human aspartylglucosaminidase and optimization of the coding sequence for protein production. Codon-optimized versions of the two variants are expressed at significantly higher levels than AGA with the natural codon-usage. The second most common allele in Finland is a 2 bp deletion called AGUFin-minor (NM_000027.3; c.199_200del - p.Glu67fc*3). Genotype frequency of single nucleotide polymorphism (SNP) rs2228119 in various populations
additional information
-
single nucleotide polymorphism rs2228119 (NM_000027.3:c.446C>G - p.(Thr149Ser)) results in amino acid variation Ser vs. Thr at position 149 (base and amino acid variation in red) of the human AGA enzyme. Functional analysis of the Ser149/Thr149 variants of human aspartylglucosaminidase and optimization of the coding sequence for protein production. Codon-optimized versions of the two variants are expressed at significantly higher levels than AGA with the natural codon-usage. The second most common allele in Finland is a 2 bp deletion called AGUFin-minor (NM_000027.3; c.199_200del - p.Glu67fc*3). Genotype frequency of single nucleotide polymorphism (SNP) rs2228119 in various populations
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Noronkoski, T.; Stoineva, I.B.; Petkov, D.D.; Mononen, I.
Recombinant human glycosylasparaginase catalyzes hydrolysis of L-asparagine
FEBS Lett.
412
149-152
1997
Homo sapiens
brenda
Saarela, J.; Laine, M.; Tikkanen, R.; Oinonen, C.; Jalanko, A.; Rouvinen, J.; Peltonen, L.
Activation and oligomerization of aspartylglucosaminidase
J. Biol. Chem.
273
25320-25328
1998
Homo sapiens
brenda
Cui, T.; Liao, P.H.; Guan, C.; Guo, H.C.
Purification and crystallization of precursors and autoprocessed enzymes of Flavobacterium glycosylasparaginase: an N-terminal nucleophile hydrolase
Acta Crystallogr. Sect. D
55
1961-1964
1999
Elizabethkingia meningoseptica
brenda
Liu, Y.; Dunn, G.S.; Aronson, N.N.
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