Glycoside Hydrolase Family 13

Activities in Family[retaining] α-glucoside phosphorylase (EC 2.4.1.-);
[retaining] α-maltosyltransferase (EC 2.4.1.-);
[retaining] α-transglucosidase / α-glucosyltransferase (EC 2.4.1.-);
[retaining] acarviosyltransferase (EC 2.4.1.-);
α-1,6-maltooligosyltransferase (EC 2.4.1.-);
α-glucosyltransferase (EC 2.4.1.-);
Oligosaccharide α-4-glucosyltransferase (EC 2.4.1.161);
[retaining] α-1,4-glucan branching enzyme (EC 2.4.1.18);
[retaining] cyclomaltodextrin glucanotransferase (EC 2.4.1.19);
[retaining] 4-α-glucanotransferase / amylomaltase (EC 2.4.1.25);
[retaining] sucrose 6(F)-phosphate phosphorylase (EC 2.4.1.329);
Glucosylglycerate phosphorylase (EC 2.4.1.352);
[retaining] glucosylglycerol phosphorylase (EC 2.4.1.359);
[retaining] amylosucrase (EC 2.4.1.4);
[retaining] sucrose phosphorylase (EC 2.4.1.7);
α-1,4-glucan: phosphate α-maltosyltransferase (EC 2.4.99.16);
[retaining] cyclic α-1,6-maltosyl-maltose hydrolase (EC 3.2.1.-);
[retaining] maltopentaose-producing α-amylase (EC 3.2.1.-);
Palatinase (EC 3.2.1.-);
[retaining] α-amylase (EC 3.2.1.1);
[retaining] oligo-α-1,6-glucosidase (EC 3.2.1.10);
[retaining] maltotriose-producing α-amylase (EC 3.2.1.116);
[retaining] maltogenic α-amylase (EC 3.2.1.133);
[retaining] neopullulanase (EC 3.2.1.135);
[retaining] maltooligosyltrehalose trehalohydrolase (EC 3.2.1.141);
α-glucosidase (EC 3.2.1.20);
α,α-trehalase (EC 3.2.1.28);
[retaining] pullulanase (EC 3.2.1.41);
[retaining] sucrose α-glucosidase (EC 3.2.1.48);
[retaining] cyclomaltodextrinase (EC 3.2.1.54);
[retaining] maltotetraose-producing α-amylase (EC 3.2.1.60);
Isoamylase (EC 3.2.1.68);
Glucodextranase (EC 3.2.1.70);
[retaining] a,α-trehalose-6-phosphate hydrolase (EC 3.2.1.93);
[retaining] maltohexaose-producing α-amylase (EC 3.2.1.98);
[retaining] isomaltulose synthase / sucrose isomerase / sucrose glucosylmutase (EC 5.4.99.11);
Malto-oligosyltrehalose synthase (EC 5.4.99.15);
Trehalose synthase / maltose glucosylmutase (EC 5.4.99.16);
Mechanism Retaining a
ClanGH-H
3D Structure Status( β / α ) 8 barrel
Catalytic Nucleophile/BaseAsp (experimental)
Catalytic Proton DonorGlu (experimental)
NoteNew: many members have been assigned to subfamilies as described by Stam et al. (2006) Protein Eng Des Sel. 19, 555-562 (PMID: 17085431)
External resourcesCAZypedia; EBI Protein of the Month; HOMSTRAD; PDB Molecule of the Month; PRINTS;
Commercial Enzyme Provider(s)MEGAZYME; PROZOMIX;
Statistics GenBank accession (180918); Uniprot accession (1005); PDB accession (663); 3D entries (162); cryst (2)


Last update: 2024-05-24 © Copyright 1998-2024
AFMB - CNRS - Université d'Aix-Marseille