Effects of introducing negative charges into the molecular surface of thermolysin by site-directed mutagenesis on its activity and stability.

doi:10.1016/j.bbapap.2007.12.004

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Article

Effects of introducing negative charges into the molecular surface of thermolysin by site-directed mutagenesis on its activity and stability.

Biochimica et biophysica acta - 1 Mar 2008

Takita Teisuke, Aono Takahiro, Sakurama Haruko, Itoh Takafumi, Wada Takumi, Minoda Masashi, Yasukawa Kiyoshi, Inouye Kuniyo

Abstract excerpt

Thermolysin is remarkably activated and stabilized by neutral salts, and surface charges are suggested important in its activity and stability. The effects of introducing negative charge into the molecular surface on its activity and stability are described. Seven serine residues were selected, and each of them was changed for aspartate by site-directed mutagenesis in a thermolysin mutant. In the hydrolysis of...

Topics

Acrylates
Amino Acid Substitution
Aspartic Acid
Bacillus
Bacterial Proteins
Calcium Chloride
Dipeptides
Enzyme Stability
Hydrolysis
Mutagenesis, Site-Directed
Mutation
Protein Conformation
Serine
Thermolysin

Source

Open in PubMed

Identifiers

PMID: 18187054
DOI: 10.1016/j.bbapap.2007.12.004

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