title: 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.
authors.affiliation: Department of Biochemistry, University of Wales, Cardiff, U.K.
authors.forename: J
authors.initials: J
authors.lastname: Kay
authors.forename: B M
authors.initials: BM
authors.lastname: Dunn
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure; D013379:Substrate Specificity
chemical_list: D016282:Aspartic Acid Endopeptidases