Glycoside Hydrolase Family 97

Known Activitiesα-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/BaseGlu for inverting members; Asp for retaining members
Catalytic Proton DonorGlu
NoteCreated 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 resourcesCAZypedia;
Statistics GenBank accession (132); Uniprot accession (63); PDB accession (6); 3D entries (2); cryst (0)
All (113) Archaea (4) Bacteria (109) Structure (2 ) Characterized (3)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 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]
 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) 3.2.1.20 Tannerella forsythia ATCC 43037 AAO33827.1 Q84FT4  

Footnotes

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.