Effective blocking of HIV-1 proteinase activity by characteristic inhibitors of aspartic proteinases.
Inhibitory constants (Ki) between 5 and 35 nM were derived (under different conditions of pH and ionic strength) for the interaction of HIV-1 proteinase with acetyl-pepstatin and H-261, two characteristic inhibitors of aspartic proteinases. Thus this enzyme, essential for replication of the AIDS virus, may be classified unequivocally as belonging to this proteinase family.
Richards
A D
AD
Department of Biochemistry, University of Wales College of Cardiff.
Roberts
R
R
Dunn
B M
BM
Graves
M C
MC
Kay
J
J
D016282:Aspartic Acid Endopeptidases; D001667:Binding, Competitive; D010450:Endopeptidases; D015497:HIV-1 / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D009842:Oligopeptides / Q000378:metabolism / Q000494:pharmacology; D009994:Osmolar Concentration; D010436:Pepstatins / Q000494:pharmacology; D010880:Piperidines / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology*; D000092502:Renin Inhibitors
D016282:Aspartic Acid Endopeptidases; D010450:Endopeptidases; D009842:Oligopeptides; D010436:Pepstatins; D010880:Piperidines; D011480:Protease Inhibitors; D000092502:Renin Inhibitors; C014195:Streptomyces pepsin inhibitor; C046598:H 261