| Known Activities | α-glucosidase (EC 3.2.1.20); α-galactosidase (EC 3.2.1.22) |
|---|---|
| Mechanism | inverting and retain |
| 3D Structure Status | ( β / α ) 8 |
| 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 (251); Uniprot accession (146); PDB accession (6); 3D entries (2); cryst (0) |
| Bacteria | ||||||
| Protein Name | EC# | Organism | GenBank | Uniprot | PDB/3D | |
| α-galactosidase (BtGH97b;BT1871;BT_1871) | 3.2.1.22 | Bacteroides thetaiotaomicron VPI-5482 | AAO76978.1 NP_810784.1 |
3A24[A,B] | ||
| α-glucosidase (SusB;BtGH97a;BT3703;BT_3703) | 3.2.1.20 | Bacteroides thetaiotaomicron VPI-5482 | AAC44671.1 AAO78808.1 NP_812614.1 |
P71094 | 2D73[A,B] 2JKA[A,B] 2JKE[A,B] 2JKP[A,B] 2ZQ0[A,B] |
|