EC number:3.5.1.26

Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.26
Description:N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase.
Alternative Name: N-aspartyl-beta-glucosaminidase.
Glycosylasparaginase.
Glucosylamidase.
Beta-aspartylglucosylamine amidohydrolase.
Aspartylglycosylamine amidohydrolase.
Aspartylglucosylaminidase.
Aspartylglucosylamine deaspartylase.
Aspartylglucosylaminase.
Aspartylglucosaminidase.
Cath: 1.10.1740.90; 1.20.5.1540; 3.10.620.30; 3.60.20.30; 1.20.58.2190; 2.20.25.10; 2.60.120.10; 2.60.120.1020; 2.60.120.230;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.26
BRENDA Enzyme Link: BRENDA 3.5.1.26
KEGG Enzyme Link: KEGG3.5.1.26
BioCyc Enzyme Link: BioCyc 3.5.1.26
ExPASy Enzyme Link: ExPASy3.5.1.26
EC2PDB Enzyme Link: EC2PDB 3.5.1.26
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.26
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.26
IntEnz Enzyme Link: IntEnz 3.5.1.26
MEDLINE Enzyme Link: MEDLINE 3.5.1.26

EC number:3.5.1.26

MSA:

3.5.1.26;
Phylogenetic Tree:

3.5.1.26;
Uniprot:
M-CSA:
RHEA:11544 H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H(+) + L-aspartate + N-acetyl-beta-D-glucosaminylamine
RULE(radius=1) [*:1]-[NH;+0:2]-[C;H0;+0:3](-[*:4])=[*:5].[OH2;+0:6]>>[*:4]-[C;H0;+0:3](=[*:5])-[OH;+0:6].[*:1]-[NH2;+0:2]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure of glycosylasparaginase from Flavobacterium meningosepticum.Xuan J, Tarentino AL, Grimwood BG, Plummer TH Jr, Cui T, Guan C, Van Roey P1998 Mar9541410
Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits.Fisher KJ, Aronson NN Jr1991 Jun 251904874
Crystallographic snapshot of a productive glycosylasparaginase-substrate complex.Wang Y, Guo HC2007 Feb 917157318
Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.Ikonen E, Baumann M, Grön K, Syvänen AC, Enomaa N, Halila R, Aula P, Peltonen L1991 Jan1703489