| Known Activities | β-xylosidase (EC 3.2.1.37). |
|---|---|
| Mechanism | Retaining |
| Catalytic Nucleophile/Base | Glu |
| Catalytic Proton Donor | Asp |
| External resources | InterPro; PFAM; PRINTS; |
| Commercial Enzyme Provider(s) | PROZOMIX; |
| Statistics | GenBank accession (29); Uniprot accession (22); PDB accession (0); 3D entries (1); cryst (1) |
| Bacteria | ||||||
| Protein Name | EC# | Organism | GenBank | Uniprot | PDB/3D | |
| β-xylosidase (peptide fragment) | 3.2.1.37 | Aeribacillus pallidus | ||||
| β-xylosidase B (XysB) | 3.2.1.37 | Aeromonas caviae ME-1 | BAA74507.1 | Q9Z487 | ||
| β-xylosidase (XylA) | 3.2.1.37 | Geobacillus stearothermophilus 21 | BAA05667.1 | P45702 | ||
| β-xylosidase (XylA) | 3.2.1.37 | Geobacillus stearothermophilus 236 | AAA50863.1 | P45704 | ||
| β-xylosidase (XynB2;β-X;LβX) | 3.2.1.37 | Geobacillus stearothermophilus T-6 NCIMB 40222 | AAC98122.1 ABI49956.1 CAC29083.1 |
Q09LZ0 Q9AL84 Q9ZFM9 |
cryst | |
| β-xylosidase (XylA) | 3.2.1.37 | Paenibacillus sp. DG-22 | ABV46494.1 | B6C867 | ||
Experimental characterization exclusively covers enzyme activities at present. If you are aware of any missing experimental characterization that should be mentioned here, we encourage you to send your comment and support of the experimental evidence, including an electronic copy or appropriate link to the support material (i.e., article(s), thesis, database, etc), to cazy@afmb.univ-mrs.fr.