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Updated: Aug 16, 2026

Curation of Computational Chemical Libraries Demonstrated with Alpha-Amino Acids
Published on: April 13, 2022
Exploring the subsite-structure of vimelysin and thermolysin using FRETS-libraries
Kohei Oda1, Toshihiro Takahashi, Katsumi Takada
1Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan. bika@kit.ac.jp
Abstract:
Vimelysin is a metalloproteinase with high activity at low temperature and an unusual resistance to organic solvents. Substrate specificities of vimelysin and thermolysin were examined using FRETS-libraries, revealing a significant difference at the P3' position: vimelysin preferred acidic amino acid residues, whereas thermolysin preferred basic residues. Homology modeling of vimelysin suggests that oppositely charged residues in the S3' subsites (R215 in vimelysin and D213 in thermolysin) may be responsible for this specificity difference. This hypothesis was confirmed by examining the R215D mutant of vimelysin, which showed a substrate specificity profile intermediate between thermolysin and vimelysin.
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