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
ECTree
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Crystallization
Crystallization on EC 3.5.1.26 - N4-(beta-N-acetylglucosaminyl)-L-asparaginase
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D151N mutant AGA precursor, complexed with glycine and without glycine
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hanging drop vapor diffusion technique, 1.9 A resolution, precursor and autoprocessed enzymes
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mutant with lower turnover number to be able to get a crystal with natural substrate in complex
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purified recombinant mutant G172D enzyme precursor in presence of L-aspartic acid beta-hydroxamate, X-ray diffraction structure determination and analysis at 2.1 A resolution. Structures of the precursor and the mature form are found in a single crystal
purified recombinant enzyme mutant T203I free and in complex with N4-(beta-N-acetylglucosaminyl)-L-asparagine, hanging drop vapor diffusion technique, mixing of 2mg/ml protein solution with reservoir oslution containing 0.2 M NaCl, 0.1 M bis-Tris, pH 6.5, and 25% PEG 3350, cryoprotection in solution containing 100 mM Tris-HCl, pH 8.0, and 20% glycerol, X-ray diffraction structure determination and analysis, molecular replacement using the structure of the wild-type enzyme (PDB ID 2GAW) as the starting model
purified recombinant enzyme mutant T99K free and in complex with substrate N4-(beta-N-acetylglucosaminyl)-L-asparagine, hanging drop vapor diffusion technique, mixing of 2mg/ml protein solution with reservoir oslution containing 0.2 M NaCl, 0.1 M bis-Tris, pH 6.5, and 25% PEG 3350, cryoprotection in solution containing 100 mM Tris-HCl, pH 8.0, and 20% glycerol, X-ray diffraction structure determination and analysis at 1.5 A resolution, molecular replacement using the structure of the wild-type enzyme (PDB ID 2GAW) as the starting model