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Literature summary for 3.2.1.2 extracted from

  • Miyake, H.; Otsuka, C.; Nishimura, S.; Nitta, Y.
    Catalytic mechanism of beta-amylase from Bacillus cereus var. mycoides: chemical rescue of hydrolytic activity for a catalytic site mutant (Glu367-->Ala) by azide (2002), J. Biochem., 131, 587-591.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E172A catalytic site mutant, no hydrolytic activity, no rescue of activity by 2 M azide Bacillus cereus
E172A/E367A catalytic site double mutant, no hydrolytic activity, no rescue of activity by 2 M azide Bacillus cereus
E367A catalytic site mutant, no hydrolytic activity in the absence of azide, in the presence of 2 M azide the mutant enzyme hydrolyzes maltopentaose at pH 7 and 25°C producing maltose, mechanism Bacillus cereus

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
var. mycoides
-

Purification (Commentary)

Purification (Comment) Organism
E172A, E367A and E172A/E367A mutant enzymes Bacillus cereus

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 catalytic mechanism, reaction mechanism Bacillus cereus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltopentaose + H2O beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base Bacillus cereus ?
-
?
starch + H2O beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base Bacillus cereus ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Bacillus cereus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Bacillus cereus