Send to

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 1989 Oct 16;164(1):30-8.

Substitution mutations of the highly conserved arginine 87 of HIV-1 protease result in loss of proteolytic activity.

Author information

  • 1Division of Cancer Biology and Diagnosis, National Cancer Institute, Bethesda, MD 20892.


The 297bp gene coding for the HIV-1 protease was chemically synthesized and expressed in E. coli. Single amino acid substitutions (Arg 87 - greater than Lys; Arg 87 - greater than Glu) were introduced in the C-terminally located conserved region GlyArgAsn of the protease gene in the wild-type clone. The products of the mutant and the wild-type clones were expressed at approximately similar levels at 30 minutes of induction but the mutant protease proteins accumulated as a function of time of induction unlike the wild-type protease which declined after 60 minutes. The mutants were completely devoid of proteolytic activity as determined in assays employing as substrates a synthetic nonapeptide and a gag related recombinant polyprotein.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Loading ...
    Write to the Help Desk