Inhibition of the aspartic proteinase from HIV-2

Kinetic constants were determined for the interaction of the HIV-2 aspartic proteinase with a synthetic substrate and a number of inhibitors at several pH values. Acetyl-pepstatin was more effective towards HIV-2 proteinase than the renin inhibitor, H-261; this effect is exactly the opposite from th...

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Veröffentlicht in:	FEBS letters 1989-08, Vol.253 (1), p.214-216
Hauptverfasser:	Richards, Anthony D., Broadhurst, Anne V., Ritchie, Alison J., Dunn, Ben M., Kay, John
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetyl-pepstatin AIDS/HIV Analytical, structural and metabolic biochemistry Aspartic Acid Endopeptidases Biological and medical sciences Endopeptidases Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology HIV, human immunodeficiency virus HIV-1 proteinase HIV-2 - enzymology HIV-2 proteinase Hydrogen-Ion Concentration Hydrolases Iva, isovaleryl Kinetics Molecular Weight Protease Inhibitors - pharmacology Renin inhibitor, H-261 Sta, 4-amino-3-hydroxy-6-methylheptanoic acid Substrate Specificity the in the sequence containing PhePro indicates the scissile peptide bond in the substrate Tight binding inhibitor
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Zusammenfassung:	Kinetic constants were determined for the interaction of the HIV-2 aspartic proteinase with a synthetic substrate and a number of inhibitors at several pH values. Acetyl-pepstatin was more effective towards HIV-2 proteinase than the renin inhibitor, H-261; this effect is exactly the opposite from that observed previously for the proteinase from the HIV-1 AIDS virus.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(89)80961-5