3.5.1.26: N4-(beta-N-acetylglucosaminyl)-L-asparaginase
This is an abbreviated version!
For detailed information about N4-(beta-N-acetylglucosaminyl)-L-asparaginase, go to the full flat file.
Word Map on EC 3.5.1.26
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3.5.1.26
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lysosomal
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aspartylglucosaminuria
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lepidoptera
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mitogenome
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protein-coding
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microsatellite-like
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attta
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poly-a
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butterfly
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a+t-rich
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glycoasparagines
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nymphalidae
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aspartylglucosamine
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dihydrouridine
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trnaseragn
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autoproteolysis
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meningosepticum
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hesperiidae
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papilionidae
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lrrna
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pieridae
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non-finnish
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glcnac-asn
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clover-leaf
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medicine
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lycaenidae
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trnamet
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diagnostics
- 3.5.1.26
- lysosomal
- aspartylglucosaminuria
- lepidoptera
-
mitogenome
-
protein-coding
-
microsatellite-like
-
attta
- poly-a
- butterfly
-
a+t-rich
- glycoasparagines
- nymphalidae
- aspartylglucosamine
- dihydrouridine
-
trnaseragn
-
autoproteolysis
- meningosepticum
- hesperiidae
- papilionidae
-
lrrna
- pieridae
-
non-finnish
- glcnac-asn
-
clover-leaf
- medicine
- lycaenidae
- trnamet
- diagnostics
Reaction
Synonyms
1-aspartamido-beta-N-acetylglucosamine amidohydrolase, 4-L-aspartylglucosylamine amido hydrolase, AGA, amidase-1, amidase-2, amidase-3, aspartylglucosaminidase, aspartylglucosylaminase, aspartylglucosylamine deaspartylase, aspartylglycosylamine amidohydrolase, AtAGA, beta-aspartylglucosylamine amidohydrolase, EC 3.5.1.37, GA, glucosylamidase, glycoasparaginase, glycosylasparaginase, LhAGA, More, N-aspartyl-beta-glucosaminidase, N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
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General Information
General Information on EC 3.5.1.26 - N4-(beta-N-acetylglucosaminyl)-L-asparaginase
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evolution
malfunction
physiological function
additional information
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
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)
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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
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lysosomal acidification inhibitors, chloroquine or bafilomycin A1, disturb medusa morphogenesis at the oral end, suggesting involvement of lysosomal hydrolases in strobilation
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
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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
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
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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
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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
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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