Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Miyake, H.; Kurisu, G.; Kusunoki, M.; Nishimura, S.; Kitamura, S.; Nitta, Y.
    Crystal structure of a catalytic site mutant of beta-amylase from Bacillus cereus var. mycoides cocrystallized with maltopentaose (2003), Biochemistry, 42, 5574-5581.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.2 X-ray crystal structures of wild-type enzyme complexed with maltose and of E172A catalytic site mutant complexed with maltopentaose Bacillus cereus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.2 E172A catalytic site mutant 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 catalytic mechanism Bacillus cereus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 maltopentaose + H2O hydrolyzes the alpha-1,4-glucosidic linkage liberating beta-maltose from the non-reducing end of substrate, good substrate, mode of binding in the active site, catalytic mechanism, enzyme/domain structure Bacillus cereus ?
-
 ?
3.2.1.2 additional information beta-amylase does not catalyze a transglycosylation reaction Bacillus cereus ?
-
 ?
3.2.1.2 starch + H2O hydrolyzes the alpha-1,4-glucosidic linkage liberating beta-maltose from the non-reducing end of substrate, enzyme/domain structure, starch binding site in domain C, catalytic mechanism Bacillus cereus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.2 More belongs to family 14 Bacillus cereus