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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

Reaction

N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
+
H2O
=
N-acetyl-beta-D-glucosaminylamine
 +
L-aspartate

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

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.26 N4-(beta-N-acetylglucosaminyl)-L-asparaginase

Crystallization

Crystallization on EC 3.5.1.26 - N4-(beta-N-acetylglucosaminyl)-L-asparaginase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
D151N mutant AGA precursor, complexed with glycine and without glycine
-
hanging drop vapor diffusion technique, 1.9 A resolution, precursor and autoprocessed enzymes
-
mutant with lower turnover number to be able to get a crystal with natural substrate in complex
-
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