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Literature summary for 3.2.1.41 extracted from

  • Wang, X.; Nie, Y.; Xu, Y.
    Improvement of the activity and stability of starch-debranching pullulanase from Bacillus naganoensis via tailoring of the active sites lining the aatalytic pocket (2018), J. Agric. Food Chem., 66, 13236-13242 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli BL21 (DE3) cells Pullulanibacillus naganoensis

Protein Variants

Protein Variants Comment Organism
D787C higher enzymatic activity than that of wild-type enzyme Pullulanibacillus naganoensis
D787C the enzymatic activity and specific activity of D787C are 1.5fold higher than those of the wild-type. The enzyme shows a 1.8fold increase in kcat and a 1.7-fold increase in kcat/Km. It maintains higher activity compared with that of wild-type enzyme at temperatures over 60°C. Higher acid resistance than wild-type enzyme, maintaining 90% residual activity at pH 4.0 Pullulanibacillus naganoensis
D787F higher enzymatic activity than that of wild-type enzyme Pullulanibacillus naganoensis
D787N higher enzymatic activity than that of wild-type enzyme Pullulanibacillus naganoensis

Organism

Organism UniProt Comment Textmining
Pullulanibacillus naganoensis G9JLV4
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-

Purification (Commentary)

Purification (Comment) Organism
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Pullulanibacillus naganoensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pullulan + H2O
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Pullulanibacillus naganoensis ?
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?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
pullulan pH 4.5, 60°C, kcat of wild-type enzyme and mutant enzyme Pullulanibacillus naganoensis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
pullulan pH 4.5, 60°C, kcat/Km of wild-type enzyme and mutant enzyme Pullulanibacillus naganoensis