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Literature summary extracted from

  • Clark, N.E.; Garman, S.C.
    The 1.9 A structure of human alpha-N-acetylgalactosaminidase: The molecular basis of Schindler and Kanzaki diseases (2009), J. Mol. Biol., 393, 435-447.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.49 expression in CHO and COS-1 cells. Expression of wild-type and mutant enzymes in Escherichia coli as insoluble proteins, and in Kluyveromyces lactis as soluble hyperglycosylated proteins. Expression of wild-type and mutant enzymes in Trichoplusia ni Tn5 insect cells using the baculovirus transfection system leads to suitable proteins Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.49 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 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.49 D217N a naturally occuring Schindler disease and/or Kanzaki disease mutation Homo sapiens
3.2.1.49 E193X a naturally occuring Schindler disease and/or Kanzaki disease mutation Homo sapiens
3.2.1.49 E325K a naturally occuring Schindler disease and/or Kanzaki disease mutation Homo sapiens
3.2.1.49 E367K a naturally occuring Schindler disease and/or Kanzaki disease mutation Homo sapiens
3.2.1.49 additional information construction of mutants of each of the five N-linked glycosylation sites Homo sapiens
3.2.1.49 N201Q site-directed mutagenesis, one of the proteins with the third N-linked carbohydrate attachment site is removed Homo sapiens
3.2.1.49 R329Q a naturally occuring Schindler disease and/or Kanzaki disease mutation Homo sapiens
3.2.1.49 R329W a naturally occuring Schindler disease and/or Kanzaki disease mutation Homo sapiens
3.2.1.49 S160C a naturally occuring Schindler disease and/or Kanzaki disease mutation Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.49 additional information
-
 additional information kinetics, recombinant wild-type and mutant enzymes Homo sapiens
3.2.1.49 0.7
-
 4-nitrophenyl alpha-D-N-acetylgalactosaminide recombinant wild-type enzyme Homo sapiens
3.2.1.49 0.89
-
 4-nitrophenyl alpha-D-N-acetylgalactosaminide recombinant mutant N201Q Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.49 lysosome
-
 Homo sapiens 5764
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.49 additional information Homo sapiens alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.49 Homo sapiens P17050
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.49 glycoprotein the enzyme contains five N-linked glycosylation sites. The N201 glycosylation is critical for enzyme stability and activity Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.49 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, or ping-pong, reaction mechanism and active site structure, overview Homo sapiens
a

Storage Stability

EC Number Storage Stability Organism
3.2.1.49 the purified wild-type and N201Q mutant proteins expressed in insect cells retain nearly full activity for months at 4°C, but the CHO-expressed material loses most of its activity within 72 h Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.49 4-nitrophenyl alpha-D-N-acetylgalactosaminide + H2O substrate binding and active site structure, active-site interactions and ligand binding, overview. Inactive enzyme conformation, overview Homo sapiens 4-nitrophenol + N-acetyl-D-galactosamine
-
 ?
3.2.1.49 additional information alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids Homo sapiens ?
-
 ?
3.2.1.49 additional information the enzyme also shows activity with 4-nitrophenyl alpha-D-galactosaminide Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.49 homodimer alpha-NAGAL is a homodimer with each monomer divided into two domains. Domain 1 forms a (beta/alpha)8 barrel, and domain 2 contains eight antiparallel beta strands in two beta sheets Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.2.1.49 alpha-NAGAL
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.49 16.3
-
 4-nitrophenyl alpha-D-N-acetylgalactosaminide recombinant wild-type enzyme Homo sapiens
3.2.1.49 17.1
-
 4-nitrophenyl alpha-D-N-acetylgalactosaminide recombinant mutant N201Q Homo sapiens

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.49 Homo sapiens recombinant enzyme
-
 4.58

General Information

EC Number General Information Comment Organism
3.2.1.49 malfunction deficiency of alpha-NAGAL activity results in the lysosomal storage disorders Schindler disease and Kanzaki disease, molecular basis, overview Homo sapiens