EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.2.1.1 | enzyme complexed with 4-nitrophenyl alpha-D-maltoside, X-ray diffraction structure determination and analysis at 2.40 A resolution | Sus scrofa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.1 | Sus scrofa | P00690 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose | the reaction mechanism involves no typical conformational change of the flexible loop, residues 303-309, that constitutes the surface edge of the substrate binding cleft, but only a small movement of the segment from residues 304/305, conformational change of catalytic residue Asp300 upon substrate binding, flexibility of the active site depends on the substrate aglycon bound, overview | Sus scrofa |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.1 | pancreas | - |
Sus scrofa | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.1 | 4-nitrophenyl alpha-D-maltoside + H2O | 4-nitrophenol is bound at the ative site | Sus scrofa | 4-nitrophenol + alpha-D-maltose | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.1 | PPA | - |
Sus scrofa |