Literature summary for 3.2.1.49 extracted from

Garman, S.C.; Hannick, L.; Zhu, A.; Garboczi, D.N.
The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases (2002), Structure, 10, 425-434.

Search for more literature for 3.2.1.49

Crystallization (Commentary)

Crystallization (Comment)	Organism
X-ray crystallography	Gallus gallus

Organism

Organism	UniProt	Comment	Textmining
Gallus gallus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
alpha-D-GalNAc-(1->3)-beta-D-GalNAc-(1->3)-alpha-D-Gal-(1->4)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-ceramide + H2O = D-GalNAc + beta-D-GalNAc-(1->3)-alpha-D-Gal-(1->4)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-ceramide	double-displacement mechanism. First step: an oxygen atom from Asp140 attacks the electrophilic C1 of the hexose ring, cleaving the glycosidic linkage and creating a covalent enzyme-substrate intermediate. The second step involves a nucleophilic attack by a water molecule, which has been deprotonated by Asp201, on the covalent intermediate.	Gallus gallus	a

Synonyms

Synonyms	Comment	Organism
alpha-NAGAL	-	Gallus gallus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)