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Literature summary extracted from

  • Ye, Z.; Miyake, H.; Tatsumi, M.; Nishimura, S.; Nitta, Y.
    Two additional carbohydrate-binding sites of beta-amylase from Bacillus cereus var. mycoides are involved in hydrolysis and raw starch-binding (2004), J. Biochem., 135, 355-363.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.2 wild-type and mutant enzymes, expression in Escherichia coli BL21(DE3) Bacillus cereus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.2
-
Bacillus cereus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.2 additional information mutation of two of the three carbohydrate-binding sites aside from the active site: Site2 in domain B and Site1 in domain C Bacillus cereus
3.2.1.2 S235A binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 88% of wild-type activity with soluble starch as substrate Bacillus cereus
3.2.1.2 S235A/Y249A double mutant, binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 63% of wild-type activity with soluble starch as substrate Bacillus cereus
3.2.1.2 S235A/Y249A/W449F/W495F quadruple mutant, kinetic parameters for the hydrolysis of amylose, 51% of wild-type activity with soluble starch as substrate Bacillus cereus
3.2.1.2 W449F binding parameters to raw corn starch Bacillus cereus
3.2.1.2 W449F/W495F double mutant, binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 61% of wild-type activity with soluble starch as substrate Bacillus cereus
3.2.1.2 W495F binding parameters to raw corn starch Bacillus cereus
3.2.1.2 W51F beta-amylase mutant Bacillus cereus
3.2.1.2 Y249A binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 80% of wild-type activity with soluble starch as substrate Bacillus cereus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.2 cyclohexaamylose alpha-CD, competitive inhibitor Bacillus cereus
3.2.1.2 maltitol behaves as a mixed-type or competitive inhibitor depending on the chain length of the substrate, inhibition mechanism, binds to Site2 in domain B and forms an abortive ESI complex when amylose is used as substrate Bacillus cereus
3.2.1.2 O-alpha-D-xylopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranoside mixed-type inhibition, two molecules bind to enzyme Bacillus cereus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.2 additional information
-
additional information binding parameters of wild-type and mutant enzymes to raw corn starch Bacillus cereus
3.2.1.2 0.6
-
amylose pH 7, 25°C, DPn: 16, S235A/Y249A/W449F/W495F quadruple mutant Bacillus cereus
3.2.1.2 0.61
-
amylose pH 7, 25°C, DPn: 16, W449F/W495F double mutant Bacillus cereus
3.2.1.2 0.65
-
amylose pH 7, 25°C, DPn: 16, S235A/Y249A double mutant Bacillus cereus
3.2.1.2 0.7
-
amylose pH 7, 25°C, DPn: 16, S235A mutant Bacillus cereus
3.2.1.2 0.71
-
amylose pH 7, 25°C, DPn: 16, Y249A mutant Bacillus cereus
3.2.1.2 0.72
-
amylose pH 7, 25°C, DPn: 16, wild-type enzyme Bacillus cereus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.2 58300
-
x * 58300, Western blot analysis Bacillus cereus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Bacillus cereus P36924 var. mycoides
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.2 recombinant wild-type and mutant enzymes Bacillus cereus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 amylose + H2O DPn is 16 Bacillus cereus ?
-
?
3.2.1.2 maltopentaose + H2O binding mode of substrate in the active site Bacillus cereus ?
-
?
3.2.1.2 additional information no hydrolysis of alpha-1,6-glucosidic linkages Bacillus cereus ?
-
?
3.2.1.2 starch + H2O catalyzes the hydrolysis of alpha-1,4-glucosidic linkages of soluble starch, and liberates beta-anomeric maltose from the nonreducing ends, exo-acting enzyme, composed of two functional domains, a catalytic domain: domains A and B, and starch-binding domain: domain C, beta-amylase has three carbohydrate-binding sites aside from the active site: two in domain B named Site2 and Site3, one in domain C named Site1, roles of these sites in the catalytic reaction and raw starch-binding, beta-amylase hardly hydrolyzes raw starch from wheat, corn, potato or sweet potato, but binds to it strongly Bacillus cereus ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.2 ? x * 58300, Western blot analysis Bacillus cereus
3.2.1.2 More enzyme is composed of two functional domains, a catalytic domain: domains A and B, and starch-binding domain: domain C, beta-amylase has three carbohydrate-binding sites aside from the active site: two in domain B named Site2 and Site3, one in domain C named Site1, roles of these sites in the catalytic reaction and raw starch-binding Bacillus cereus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 25
-
assay at Bacillus cereus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.2 additional information
-
additional information
-
Bacillus cereus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 7
-
assay at Bacillus cereus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.2 0.45
-
O-alpha-D-xylopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranoside pH 7, 25°C, wild-type enzyme, amylose as substrate Bacillus cereus
3.2.1.2 0.8
-
cyclohexaamylose pH 7, 25°C, wild-type enzyme, amylose as substrate Bacillus cereus
3.2.1.2 2.8
-
maltitol pH 7, 25°C, wild-type enzyme, amylose as substrate Bacillus cereus
3.2.1.2 3.1
-
maltitol pH 7, 25°C, wild-type enzyme, maltopentaose as substrate Bacillus cereus
3.2.1.2 5.1
-
maltitol pH 7, 25°C, S235A/Y249A double mutant, amylose as substrate Bacillus cereus
3.2.1.2 5.7
-
maltitol pH 7, 25°C, S235A/Y249A/W449F/W495F quadruple mutant, amylose as substrate Bacillus cereus