3.2.1.49: alpha-N-acetylgalactosaminidase

This is an abbreviated version!
For detailed information about alpha-N-acetylgalactosaminidase, go to the full flat file.

Word Map on EC 3.2.1.49

Reaction

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

Synonyms

alpha-acetylgalactosaminidase, N-acetyl-alpha-D-galactosaminidase, N-acetyl-alpha-galactosaminidase, 4-nitrophenyl-alpha-N-acetylgalactosaminidase, 2-acetamido-2-deoxy-alpha-D-galactoside acetamidodeoxygalactohydrolase, exo-alpha-N-acetylgalactosaminidase, alpha-galactosidase B, AglA, alpha-NAGAL, alpha-GalNAc, alpha-NaGalase, alpha-N-galactosaminidase IV, NaGalase, alpha-N-acetylgalactosaminidase blood group A2 degrading enzyme, alpha-NAGA, envelope glycoprotein gp160, NagA, alpha-GalNAcase I, alpha-GalNAcase II, alpha-GalNAcase, alpha-GalNAc-ase, alpha-N acetylgalactosaminidase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.49 alpha-N-acetylgalactosaminidase

Crystallization

Crystallization on EC 3.2.1.49 - alpha-N-acetylgalactosaminidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme and in complex with alpha-N-acetylgalactosamine, to 2.3 and 2.4 A resolution, respectively. Each monomer of NagA consists of two closely associated domains, forming a narrow tunnel in which the NAD+ molecule is anchored. The NAD+ is embedded within a narrow tunnel, almost exclusively shielded from solvent. It is bound with its diphosphate group oriented towards the N-terminus of the first alpha-helix of the N-terminal dinucleotide-binding domain and has both the adenine ring and the nicotinamide ring in the anti conformation. No major structural changes are observed in NagA upon product binding
X-ray crystallography
-
purified recombinant wild-type and mutant enzymes in complexes with two catalytic products, the alpha-galactose and alpha-GalNAc monosaccharides, and a covalent intermediate bound in the enzyme active site, X-ray diffraction structure determination and analysis at 1.9 A resolution