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
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3.2.1.49
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n-acetylgalactosamine
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sialidase
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fabry
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schindler
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exoglycosidase
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neuroaxonal
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d3-binding
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gcmaf
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angiokeratoma
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alpha-linked
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beta-galnac
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macrophage-activating
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pomatia
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corporis
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diffusum
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biflorus
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mucin-type
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medicine
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alpha-n-acetylgalactosaminyltransferase
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alpha-n-acetylgalactosamine
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asialo
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diagnostics
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biotechnology
- 3.2.1.49
- n-acetylgalactosamine
- sialidase
- fabry
-
schindler
-
exoglycosidase
-
neuroaxonal
-
d3-binding
-
gcmaf
- angiokeratoma
-
alpha-linked
-
beta-galnac
-
macrophage-activating
- pomatia
-
corporis
- diffusum
- biflorus
-
mucin-type
- medicine
-
alpha-n-acetylgalactosaminyltransferase
- alpha-n-acetylgalactosamine
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asialo
- diagnostics
- biotechnology
Reaction
Synonyms
2-acetamido-2-deoxy-alpha-D-galactoside acetamidodeoxygalactohydrolase, 4-nitrophenyl-alpha-N-acetylgalactosaminidase, AglA, alpha-acetylgalactosaminidase, alpha-galactosidase B, alpha-GalNAc, alpha-GalNAc-ase, alpha-GalNAcase, alpha-GalNAcase I, alpha-GalNAcase II, alpha-N acetylgalactosaminidase, alpha-N-acetylgalactosaminidase blood group A2 degrading enzyme, alpha-N-galactosaminidase IV, alpha-NAGA, alpha-NAGAL, alpha-NaGalase, envelope glycoprotein gp160, exo-alpha-N-acetylgalactosaminidase, N-acetyl-alpha-D-galactosaminidase, N-acetyl-alpha-galactosaminidase, NagA, NaGalase
ECTree
3.2.1.49 alpha-N-acetylgalactosaminidaseAdvanced search results
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results (Engineering
Engineering on EC 3.2.1.49 - alpha-N-acetylgalactosaminidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D217N
a naturally occuring Schindler disease and/or Kanzaki disease mutation
E193X
a naturally occuring Schindler disease and/or Kanzaki disease mutation
E325K
E367K
a naturally occuring Schindler disease and/or Kanzaki disease mutation
N201Q
R329Q
R329W
S160C
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
E325K
a naturally occuring Schindler disease and/or Kanzaki disease mutation
E325K
less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease
N201Q
site-directed mutagenesis, one of the proteins with the third N-linked carbohydrate attachment site is removed
R329Q
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site-specific mutagenesis, construction of the naturally occurring mutation at R329 in Kanzaki disease, less severe phenotype compared to R329W
R329Q
a naturally occuring Schindler disease and/or Kanzaki disease mutation
R329Q
less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease
R329W
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site-specific mutagenesis, construction of the naturally occurring mutation at R329 in Kanzaki disease, more severe phenotype compared to R329Q
R329W
a naturally occuring Schindler disease and/or Kanzaki disease mutation
R329W
less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease
S160C
a naturally occuring Schindler disease and/or Kanzaki disease mutation
S160C
less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease
additional information
construction of mutants of each of the five N-linked glycosylation sites
additional information
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construction of mutants of each of the five N-linked glycosylation sites
