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

Engineering

Engineering on EC 3.2.1.49 - alpha-N-acetylgalactosaminidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N201Q
D217N
a naturally occuring Schindler disease and/or Kanzaki disease mutation
N124Q
-
35% activity in comparison to 100% activity of wild-type enzyme
N177Q
-
48% activity in comparison to 100% activity of wild-type enzyme
N359Q
-
57% activity in comparison to 100% activity of wild-type enzyme
N385Q
-
4% activity in comparison to 100% activity of wild-type enzyme
R329W
R329Q
S160C
E193X
a naturally occuring Schindler disease and/or Kanzaki disease mutation
E325K
E367K
a naturally occuring Schindler disease and/or Kanzaki disease mutation
S188E/A191L
Ser188 and Ala191 play important roles in the recognition of an N-acetylgalactosamine residue in NAGA, while lu203 and Leu206 play important roles in the recognition of a galactose residue in GLA. Construction of a modified alpha-N-acetylgalactosaminidase with alpha-galactosidase A-like substrate specificity. The enzyme acquires the ability to catalyze the degradation of 4-methylumbelliferyl-alpha-D-galactopyranoside, but retaines the wild-type NAGA's stability, overview
additional information