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Literature summary for 3.2.1.10 extracted from

  • Watanabe, K.; Miyake, K.; Suzuki, Y.
    Identification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6-glucosidase (2001), Biosci. Biotechnol. Biochem., 65, 2058-2064.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant enzymes in Escherichia coli MV1184 Bacillus cereus

Protein Variants

Protein Variants Comment Organism
D199N site-directed mutagenesis, active site mutant, highly reduced activity compared to the wild-type enzyme Bacillus cereus
D329N site-directed mutagenesis, active site mutant, catalytically inactive mutant Bacillus cereus
E255Q site-directed mutagenesis, active site mutant, highly reduced activity compared to the wild-type enzyme Bacillus cereus
H103N site-directed mutagenesis, substrate binding mutant, about 50% reduced activity compared to the wild-type enzyme Bacillus cereus
H328N site-directed mutagenesis, substrate binding mutant, highly reduced activity compared to the wild-type enzyme Bacillus cereus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
4-nitrophenyl alpha-D-glucopyranoside recombinant mutant D199N, pH 7.0, 35°C Bacillus cereus
0.015
-
4-nitrophenyl alpha-D-glucopyranoside recombinant mutant E255Q, pH 7.0, 35°C Bacillus cereus
0.8
-
4-nitrophenyl alpha-D-glucopyranoside recombinant wild-type enzyme, pH 7.0, 35°C Bacillus cereus
0.99
-
4-nitrophenyl alpha-D-glucopyranoside recombinant mutant H103N, pH 7.0, 35°C Bacillus cereus
13.3
-
4-nitrophenyl alpha-D-glucopyranoside recombinant mutant H328N, pH 7.0, 35°C Bacillus cereus

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
strain ATCC 7064
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli MV1184 Bacillus cereus

Reaction

Reaction Comment Organism Reaction ID
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose active sites residues are Asp199, Glu255, and Asp329, substrate binding residues are His103, and His328, catalytic mechanism from comparison with other enzymes' primary and crystal enzyme structures Bacillus cereus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl alpha-D-glucopyranoside + H2O
-
Bacillus cereus 4-nitrophenol + alpha-D-glucopyranose
-
?

Synonyms

Synonyms Comment Organism
dextrin 6-alpha-D-glucanohydrolase
-
Bacillus cereus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
assay at Bacillus cereus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.18
-
4-nitrophenyl alpha-D-glucopyranoside recombinant mutant D199N, pH 7.0, 35°C Bacillus cereus
0.39
-
4-nitrophenyl alpha-D-glucopyranoside recombinant mutant E255Q, pH 7.0, 35°C Bacillus cereus
3.11
-
4-nitrophenyl alpha-D-glucopyranoside recombinant mutant H328N, pH 7.0, 35°C Bacillus cereus
352
-
4-nitrophenyl alpha-D-glucopyranoside recombinant mutant H103N, pH 7.0, 35°C Bacillus cereus
483
-
4-nitrophenyl alpha-D-glucopyranoside recombinant wild-type enzyme, pH 7.0, 35°C Bacillus cereus

pH Optimum

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