Inhibition of the aspartic proteinase from HIV‐2

FEBS Letters

Dunn, Ben M.²  Ritchie, Alison J.¹  Richards, Anthony D.³  Broadhurst, Anne V.¹  Kay, John³ 

[1] Roche Products Ltd, PO Box 8, Welwyn Garden City AL7 3AY, England;Dept of Biochemistry and Molecular Biology, J. Hillis Miller Health Center, University of Florida, Gainesville, FL 32610, USA;Dept of Biochemistry, University of Wales College of Cardiff, PO Box 903, Cardiff, CF1 1ST, Wales, England

关键词: HIV-2 proteinase;    Acetyl-pepstatin;    Renin inhibitor;    H-261;    Tight binding inhibitor;    HIV-1 proteinase;    Iva;    isovaleryl;    Sta;    4-amino-3-hydroxy-6-methylheptanoic acid;    HIV;    human immunodeficiency virus;    the * in the sequence containing Phe*Pro indicates the scissile peptide bond in the substrate;   

DOI  :  10.1016/0014-5793(89)80961-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown