| Mechanism | Inverting a |
|---|---|
| Clan | GH-L |
| 3D Structure Status | ( α / α ) 6 barrel |
| Catalytic Nucleophile/Base | Glu (experimental) |
| Catalytic Proton Donor | Glu (experimental) |
| Note | Although historically composed of anomeric-inverting glucosidases, a retaining mechanism has been molecularly revealed for transglucosylating dextran dextranases [PMID=40749827]. Although the catalytic machinery is similar for both enzyme categories, the rearrangement of the spatial position of one of the catalytic glutamates governs the reaction mechanism and outcome. |
| External resources | CAZypedia; Glucoamylase Page; PROSITE; |
| Statistics | GenBank accession (18843); Uniprot accession (84); PDB accession (30); 3D entries (11); cryst (1) |
| Activity Id | EC# | Activity Name | Residue -2 | Bond -1 | Residue -1 | Reacting Bond | Residue +1 | Bond +1 | Residue +2 | Reactant |
| H3 | 3.2.1.3 | amylose exo-a-1,4-glucosidase | [aDGlcp | 1,4 | aDGlcp | 1,4 | aDGlcp | H2O | ||
| H21 | 3.2.1.28 | trehalose a-1,1-glucosidase | [aDGlcp | 1,1 | aDGlcp] | H2O | ||||
| H52 | 3.2.1.70 | dextran exo-a-1,6-glucosidase | [aDGlcp | 1,6 | aDGlcp | 1,6 | aDGlcp | H2O | ||
| H158 | 3.2.1.205 | isomaltose a-1,6-glucosidase | [aDGlcp | 1,6 | DGlcp] | H2O | ||||
| T444 | 2.4.1.2 | dextrin dextranase | [aDGlcp | 1,6 | aDGlcp | 1,6 | aDGlcp | a-1,4-aDGlcp | ||
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