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Literature summary for 3.2.1.41 extracted from

  • Li, J.X.; Wang, S.Q.; Du, Q.S.; Wei, H.; Li, X.M.; Meng, J.Z.; Wang, Q.Y.; Xie, N.Z.; Huang, R.B.; Chou, K.C.
    Simulated protein thermal detection (SPTD) for enzyme thermostability study and an application example for pullulanase from Bacillus deramificans (2018), Curr. Pharm. Des., 24, 4023-4033 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D332H/D398Y mutant enzyme shows remarkable improvement of thermal stability in higher temperature range (above 55 °C). The best temperature of the relative activity moves to 60°C. The activity performance in the middle temperature range (40 to 55°C) is worse than that of the wild type pullulanase Bacillus deramificans
D332H/D398Y/V390N the activity performance of mutations D332H/D398Y/V390N is better than that of mutations D332H/D398Y/V390S in all temperature range from 40°C to 65°C Bacillus deramificans
D332H/D398Y/V390S the activity performance of the mutant enzyme is better than the wild pullulanase-BDPulA in all temperature range from 40°C to 65°C. In the temperature range lower than 55°C the activity is worse than mutation V390S alone, and in the temperature range higher than 55°C the activity of the mutant enzyme is worse than the mutation D332H/D398Y, but better than the wild type enzyme and V390S-mutated BDPulA Bacillus deramificans

Organism

Organism UniProt Comment Textmining
Bacillus deramificans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus deramificans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pullulan + H2O
-
Bacillus deramificans ?
-
?

Synonyms

Synonyms Comment Organism
BDPulA324
-
Bacillus deramificans
CAC60157 locus name Bacillus deramificans