A consensus sequence for substrate hydrolysis by rhino virus 3C proteinase
- 12 November 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 258 (1) , 75-78
- https://doi.org/10.1016/0014-5793(89)81619-9
Abstract
Kinetic constants were determined for the hydrolysis of a series of synthetic peptide substrates by recombinant rhinovirus (HRV 14) 3C proteinase. Systematic removal or replacement of individual residues indicated that the minimum sequence required for effective cleavage by the viral cysteine proteinase was P5-Val/Thr-P3-P2-Gln-Gly-ProKeywords
This publication has 6 references indexed in Scilit:
- Hydrolysis of a Series of Synthetic Peptide Substrates by the Human Rhinovirus 14 3C Proteinase, Cloned and Expressed in Escherichia coliJournal of General Virology, 1989
- The expression and purification of human rhinovirus protease 3CEuropean Journal of Biochemistry, 1989
- Human rhinovirus 3C protease: cloning and expression of an active form in Escherichia coliBiochemistry, 1988
- Picornaviral processing: Some new ideasJournal of Cellular Biochemistry, 1987
- Expression and site-specific mutagenesis of the poliovirus 3C protease in Escherichia coli.Proceedings of the National Academy of Sciences, 1986
- The Autoactivation of TrypsinogenJournal of Biological Chemistry, 1971