Substrate specificity and inhibitors of aspartic proteinases

Abstract

Aspartic proteinases of vertebrate, fungal and retroviral origin have been characterised by utilisation of chromogenic peptide substrates and synthetic inhibitors as probes. By this means, the molecular topography of sub-sites within the active site cleft of individual enzymes has been elucidated. With suitable selection of residues to occupy each sub-site, the design of effective inhibitors specifically targetted against individual aspartic proteinases has become feasible.

Key Words:

• Aspartic proteinases
• naturally-occurring and recombinant
• pepsin
• rennin
• chymosin
• cathepsin D
• cathepsin E
• HIV proteinase
• active site mapping
• individual sub-sites
• chromogenic substrates
• specific inhibitors