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Exploring the subsite‐structure of vimelysin and thermolysin using FRETS‐libraries
Author(s) -
Oda Kohei,
Takahashi Toshihiro,
Takada Katsumi,
Tsunemi Masahiko,
Ng Kenneth K.-S.,
Hiraga Kazumi,
Harada Shigeharu
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.07.089
Subject(s) - thermolysin , chemistry , substrate (aquarium) , mutant , sequence homology , stereochemistry , homology modeling , homology (biology) , biochemistry , amino acid , peptide sequence , enzyme , biology , ecology , trypsin , gene
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.