Catalytic hydroxyl/amine dyads within serine proteases
- 1 January 1997
- journal article
- review article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 22 (1), 28-31
- https://doi.org/10.1016/s0968-0004(96)10065-7
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Identification of Active Site Residues of the Tsp ProteasePublished by Elsevier ,1995
- Structural and Functional Roles of Asparagine 175 in the Cysteine Protease PapainJournal of Biological Chemistry, 1995
- Structural basis of substrate specificity in the serine proteasesProtein Science, 1995
- A novel variant of the catalytic triad in the Streptomyces scabies esteraseNature Structural & Molecular Biology, 1995
- [2] Families of serine peptidasesMethods in Enzymology, 1994
- Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyadJournal of Bacteriology, 1993
- Refined atomic model of wheat serine carboxypeptidase II at 2.2-.ANG. resolutionBiochemistry, 1992
- An investigation into the minimum requirements for peptide hydrolysis by mutation of the catalytic triad of trypsinJournal of the American Chemical Society, 1992
- Dissecting the catalytic triad of a serine proteaseNature, 1988
- The Catalytic Role of the Active Site Aspartic Acid in Serine ProteasesScience, 1987