Mechanism | Inverting e |
---|---|
Clan | GH-M |
3D Structure Status | ( α / α ) 6 barrel |
Catalytic Nucleophile/Base | Not known |
Catalytic Proton Donor | Glu |
Note | formerly known as cellulase family L. Some cellobiohydrolases of this family have been reported to act from the reducing ends of cellulose (EC 3.2.1.-), while others have been reported to operate from the non-reducing ends to liberate cellobiose or cellotriose or cellotetraose (EC 3.2.1.-). This family also contains endo-processive cellulases (EC 3.2.1.-), whose activity is hard to distinguish from that of cellobiohydrolases. |
External resources | CAZypedia; HOMSTRAD; PRINTS; |
Commercial Enzyme Provider(s) | NZYTech; |
Statistics | GenBank accession (1970); Uniprot accession (25); PDB accession (30); 3D entries (11); cryst (0) |
Activity Id | EC# | Activity Name | Residue -2 | Bond -1 | Residue -1 | Reacting Bond | Residue +1 | Bond +1 | Residue +2 | Reactant |
H4 | 3.2.1.4 | cellulose endo-b-1,4-glucosidase | bDGlcp | 1,4 | bDGlcp | 1,4 | bDGlcp | 1,4 | bDGlcp | H2O |
H10 | 3.2.1.14 | chitin endo-b-1,4-N-acetylglucosaminidase | bDGlcpNAc | 1,4 | bDGlcpNAc | 1,4 | bDGlcpNAc | 1,4 | bDGlcpNAc | H2O |
H68 | 3.2.1.91 | cellulose exo-b-1,4-glucobiosidase | [bDGlcp | 1,4 | bDGlcp | 1,4 | bDGlcp | 1,4 | bDGlcp | H2O |
H141 | 3.2.1.176 | reducing end cellulose exo-b-1,4-glucobiosidase | bDGlcp | 1,4 | bDGlcp | 1,4 | bDGlcp | 1,4 | DGlcp] | H2O |
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