Exploring the subsite‐structure of vimelysin and thermolysin using FRETS‐libraries
抄録
<jats:p>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.</jats:p>
収録刊行物
-
- FEBS Letters
-
FEBS Letters 579 (22), 5013-5018, 2005-08-18
Wiley
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1362262944838790400
-
- NII論文ID
- 30002591021
-
- ISSN
- 18733468
- 00145793
-
- データソース種別
-
- Crossref
- CiNii Articles