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Literature summary for 3.2.1.49 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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)
| Crystallization (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| D217N | a naturally occuring Schindler disease and/or Kanzaki disease mutation | Homo sapiens |
| E193X | a naturally occuring Schindler disease and/or Kanzaki disease mutation | Homo sapiens |
| E325K | a naturally occuring Schindler disease and/or Kanzaki disease mutation | Homo sapiens |
| E367K | a naturally occuring Schindler disease and/or Kanzaki disease mutation | Homo sapiens |
| additional information | construction of mutants of each of the five N-linked glycosylation sites | Homo sapiens |
| N201Q | site-directed mutagenesis, one of the proteins with the third N-linked carbohydrate attachment site is removed | Homo sapiens |
| R329Q | a naturally occuring Schindler disease and/or Kanzaki disease mutation | Homo sapiens |
| R329W | a naturally occuring Schindler disease and/or Kanzaki disease mutation | Homo sapiens |
| S160C | a naturally occuring Schindler disease and/or Kanzaki disease mutation | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics, recombinant wild-type and mutant enzymes | Homo sapiens | |
| 0.7 | - |
4-nitrophenyl alpha-D-N-acetylgalactosaminide | recombinant wild-type enzyme | Homo sapiens |  |
| 0.89 | - |
4-nitrophenyl alpha-D-N-acetylgalactosaminide | recombinant mutant N201Q | Homo sapiens | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| lysosome | - |
Homo sapiens | 5764 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P17050 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the enzyme contains five N-linked glycosylation sites. The N201 glycosylation is critical for enzyme stability and activity | Homo sapiens |
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, or ping-pong, reaction mechanism and active site structure, overview | Homo sapiens |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 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)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| additional information | alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids | Homo sapiens | ? | - |
? | |
| additional information | the enzyme also shows activity with 4-nitrophenyl alpha-D-galactosaminide | Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| alpha-NAGAL | - |
Homo sapiens |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 16.3 | - |
4-nitrophenyl alpha-D-N-acetylgalactosaminide | recombinant wild-type enzyme | Homo sapiens | |
| 17.1 | - |
4-nitrophenyl alpha-D-N-acetylgalactosaminide | recombinant mutant N201Q | Homo sapiens | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Homo sapiens | recombinant enzyme | - |
4.58 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | deficiency of alpha-NAGAL activity results in the lysosomal storage disorders Schindler disease and Kanzaki disease, molecular basis, overview | Homo sapiens |
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