Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Cloned

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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, overexpression of mutant L15R in BHK and COS-1 cells, low expression level in endoplasmic reticulum, the recombinant active enzyme does not reach the lysosomes
expression in COS cells
-
expression in COS-1 cells and in BHK-21 cells
expression in Escherichia coli
-
expression in NIH-3T3 cells
-
gene AGA, DNA and amino acid sequence determination and analysis, genomic organization of Aurelia gene AGA and exon-intron structure, molecular phylogenetic analysis based on the nucleotide sequences of N-terminal nucleophile (Ntn)_asparaginase_2_like superfamily genes, quantitative real-time PCR enzyme expresssion analysis
-
gene AGA, DNA and amino acid sequence determination and analysis, sequence comparisons with human enzyme and Asobara tabida enzyme
gene AGA, DNA and amino acid sequence determination and analysis, sequence comparisons with human enzyme and Leptopilina heterotoma enzyme
gene AGA, genotyping, recombinant expression of codon-optimized genes encoding enzyme variants S149 and T149 in HEK-293T and HeLa cells, the Thr149 variant exhibits a slightly higher expression level than the Ser149 variant. Recombinant expression of AGA variants in transgenic patient fibroblasts, both wild-type and AGUFin-major mutant type. The transfection with the AGA variants improves the lysosomal morphology in AGU fibroblasts, low transfection efficiency
recombinant expression of wild-type and mutant enzymes