Literature summary extracted from
Oyama, T.; Miyake, H.; Kusunoki, M.; Nitta, Y.
Crystal structures of beta-amylase from Bacillus cereus var. mycoides in complexes with substrate analogs and affinity-labeling reagents (2003), J. Biochem., 133, 467-474.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.2.1.2 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.2.1.2 |
2,3-epoxypropyl-alpha-D-glucopyranoside |
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172, inactivation mechanism |
Bacillus cereus |
|
3.2.1.2 |
3,4-epoxybutyl-alpha-D-glucopyranoside |
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172 |
Bacillus cereus |
|
3.2.1.2 |
D-glucose |
mode of binding in the active site cleft |
Bacillus cereus |
|
3.2.1.2 |
D-maltose |
mode of binding in the active site cleft |
Bacillus cereus |
|
3.2.1.2 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.2.1.2 |
Bacillus cereus |
P36924 |
var. mycoides |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
3.2.1.2 |
(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 and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.2.1.2 |
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 |
? |
- |
? |
|
3.2.1.2 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
3.2.1.2 |
More |
member of family 14 of the sequence-based classification of glycoside hydrolases |
Bacillus cereus |