Structure-Activity and X-Ray Crystallographic Analysis of Potent Inhibitors of Rhizopuspepsin: Design, Kinetics and Active Site Modeling of Synthetic Peptidyl Substrate/Inhibitor Templates,
Abstract
The active site preferences of recombinant rhizopuspepsin, and aspartic proteinase, have been evaluated by the use of two set of inhibitors containing different peptide bond replacements. The interpretation of the kinetic parameters derived from these studies is facilitated by the crystallographic dat of the rhizopuspepsin-inhibitor complexes U85548E and U70531E.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1992
- Accession Number
- ADP008427
Entities
People
- C. W. Smith
- D. J. Staples
- L. L. Maggiora
- T. K. Sawyer
- W. T. Lowther
Organizations
- University of Florida