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Literature summary for 3.2.1.2 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.
    View publication on PubMed

Crystallization (Commentary)

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

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

Organism UniProt Comment Textmining
Bacillus cereus P36924 var. mycoides
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Reaction

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 and Products (Substrate)

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

Synonyms Comment Organism
More member of family 14 of the sequence-based classification of glycoside hydrolases Bacillus cereus