Substrate specificity and inhibitors of aspartic proteinases.
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.
Kay
J
J
Department of Biochemistry, University of Wales, Cardiff, U.K.
Dunn
B M
BM
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
D016282:Aspartic Acid Endopeptidases