Mechanism | Retaining a |
---|---|
Clan | GH-H |
3D Structure Status | ( β / α ) 8 barrel |
Catalytic Nucleophile/Base | Asp (experimental) |
Catalytic Proton Donor | Glu (experimental) |
Note | New: many members have been assigned to subfamilies as described by Stam et al. (2006) Protein Eng Des Sel. 19, 555-562 (PMID: 17085431) |
External resources | CAZypedia; EBI Protein of the Month; HOMSTRAD; PDB Molecule of the Month; PRINTS; |
Commercial Enzyme Provider(s) | MEGAZYME; PROZOMIX; |
Statistics | GenBank accession (7); Uniprot accession (65); PDB accession (42); 3D entries (12); cryst (0) |
Activity Id | EC# | Activity Name | Residue -2 | Bond -1 | Residue -1 | Reacting Bond | Residue +1 | Bond +1 | Residue +2 | Reactant |
H1 | 3.2.1.1 | amylose endo-a-1,4-glucosidase | aDGlcp | 1,4 | aDGlcp | 1,4 | aDGlcp | 1,4 | aDGlcp | H2O |
H31 | 3.2.1.41 | pullulan endo-a-1,6-glucosidase | aDGlcp | 1,4 | aDGlcp | 1,6 | aDGlcp | 1,4 | aDGlcp | H2O |
H40 | 3.2.1.54 | cyclomaltodextrin endo-a-1,4-glucosidase | aDGlcp | 1,4 | aDGlcp | 1,4 | aDGlcp | 1,4 | aDGlcp(cyclic) | H2O |
H107 | 3.2.1.133 | amylose exo-a-1,4-glucobiosidase | [aDGlcp | 1,4 | aDGlcp | 1,4 | aDGlcp | 1,4 | aDGlcp | H2O |
H108 | 3.2.1.135 | pullulan exo-a-1,4-panosidase | [(aDGlcp-1,6)aDGlcp | 1,4 | aDGlcp | 1,4 | aDGlcp | 1,4 | aDGlcp | H2O |
H196 | 3.2.1.- | cyclic maltosyl-maltose a-1,6-glucosidase | aDGlcp | 1,4 | aDGlcp | 1,6 | aDGlcp | 1,4 | aDGlcp(cyclic) | H2O |
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