Peptidyl thioamides as substrates and inhibitors of papain, and as probes of the kinetic significance of the oxyanion hole
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference37 articles.
1. Oxyanion Hole Interactions in Serine and Cysteine Proteases
2. DIRECT EVIDENCE FOR AN ACYLATED THIOL AS AN INTERMEDIATE IN PAPAIN- AND FICIN-CATALYSED HYDROLYSES
3. Kinetic specificity in papain-catalysed hydrolyses
4. Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: hydrolyses of thiono and oxygen esters
5. Thionesters as a probe for electrophilic catalysis in the serine protease mechanism.
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