| Activities in Family | α-glucosidase (EC 3.2.1.20); α-galactosidase (EC 3.2.1.22); [inverting] glucoamylase (EC 3.2.1.3); [retaining] β-L-arabinopyranosidase / β-L-arabinosidase (EC 3.2.1.88); |
|---|---|
| Mechanism | Inverting and retaining a |
| 3D Structure Status | ( β / α ) 8 barrel |
| Catalytic Nucleophile/Base | Glu for inverting members; Asp for retaining members |
| Catalytic Proton Donor | Glu |
| Note | Created based on a paper by Hughes et al. (2003) Oral Microbiol Immunol. 18:309-312 (PMID: 12930523); *Mechanistic and structural elucidation by Gloster et al. (2008) Chem. Biol., Oct 8 (PMID:18848471); the inverting a-glucosidases (EC 3.2.1.20) could be renamed glucoamylases (EC 3.2.1.3 according to Kitamura et al. (2008) J. Biol. Chem., Nov 3 (PMID:18981178) |
| External resources | CAZypedia; |
| Statistics | GenBank accession (5639); Uniprot accession (11); PDB accession (13); 3D entries (4); cryst (0) |