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J. Biol. Chem., Vol. 268, Issue 16, 11711-11720, Jun, 1993
CE Cameron, B Grinde, P Jacques, J Jentoft, J Leis, A Wlodawer and IT Weber
A steady state kinetic analysis of the avian myeloblastosis virus/Rous
sarcoma virus (AMV/RSV) and human immunodeficiency virus Type 1 (HIV-1)
retroviral proteases (PRs) was carried out using a series of 40 peptide
substrates that are derivatives of the AMV/RSV nucleocapsid-PR cleavage
site. These peptides contain single amino acid substitutions in each of the
seven positions of the minimum length substrate required by the PR for
specific and efficient cleavage. These peptide substrates are distinguished
by the individual enzyme subsites of the AMV/RSV and HIV- 1 PRs. The
molecular basis for similarities and differences of the individual subsites
for both proteases is discussed using steady state kinetic data and
modeling based on crystal structures.
Comparison of the substrate-binding pockets of the Rous sarcoma virus and human immunodeficiency virus type 1 proteases
Case Western Reserve University School of Medicine, Cleveland, Ohio 44106-4935.
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