Crystallization (Comment) | Organism |
---|---|
beta-amylase complexed with the inhibitors glucose, maltose and O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)D-xylopyranose and the affinity-labeling reagents 2,3-epoxypropyl-alpha-D-glucopyranoside and 3,4-epoxybutyl-alpha-D-glucopyranoside, X-ray analysis | Bacillus cereus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2,3-epoxypropyl-alpha-D-glucopyranoside | affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172, inactivation mechanism | Bacillus cereus | |
3,4-epoxybutyl-alpha-D-glucopyranoside | affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172 | Bacillus cereus | |
D-glucose | mode of binding in the active site cleft | Bacillus cereus | |
D-maltose | mode of binding in the active site cleft | Bacillus cereus | |
O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)D-xylopyranose | mode of binding in the active site cleft | Bacillus cereus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus cereus | P36924 | var. mycoides | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose | mechanism | Bacillus cereus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltopentaose + H2O | beta-amylase is an exo-enzyme that catalyzes the hydrolysis of the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, Glu-172 and Glu-367 are catalytic residues, binding mode of substrate, substrate recognition mechanism, enzyme structure | Bacillus cereus | ? | - |
? | |
starch + H2O | beta-amylase is an exo-enzyme that catalyzes the hydrolysis of the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, Glu-172 and Glu-367 are catalytic residues, substrate recognition mechanism, enzyme structure | Bacillus cereus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | member of family 14 of the sequence-based classification of glycoside hydrolases | Bacillus cereus |