Document 0575
 DOCN  M9550575
 TI    Use of steady state kinetic methods to elucidate the kinetic and
       chemical mechanisms of retroviral proteases.
 DT    9505
 AU    Meek TD; Rodriguez EJ; Angeles TS; Department of Cardiovascular
       Biochemistry, Bristol-Myers Squibb; Pharmaceutical Research Institute,
       Princeton, New Jersey 08540.
 SO    Methods Enzymol. 1994;241:127-56. Unique Identifier : AIDSLINE
       MED/95157307
 AB    Despite the current plethora of structural data of HIV-1 protease and
       the availability of potent inhibitors, whose structures are based in
       part on the presumed mechanism of action of this enzyme, our actual
       understanding of its chemical mechanism has been until now based largely
       on the precedents of the mammalian and fungal aspartic proteases and
       static three-dimensional data. The available steady state kinetic data
       of the protease, as reviewed here, constitute a first step in a detailed
       description of the mechanism of the enzyme to complement the structural
       data.
 DE    Amino Acid Sequence  Catalysis  Chromatography, High Pressure
       Liquid/METHODS  Chromatography, Ion Exchange/METHODS  Chromogenic
       Compounds  Colorimetry/METHODS  Deuterium/METABOLISM
       Fluorometry/METHODS  Hydrogen-Ion Concentration  Hydrolysis  HIV
       Protease/CHEMISTRY/*METABOLISM  HIV Protease Inhibitors/PHARMACOLOGY
       HIV-1/*ENZYMOLOGY  Kinetics  *Models, Chemical  Molecular Sequence Data
       Nitrogen Isotopes  Oxygen Isotopes  Peptide Fragments/ANALYSIS
       Peptides/CHEMICAL SYNTHESIS/METABOLISM  Radiometry/METHODS  JOURNAL
       ARTICLE  REVIEW  REVIEW, TUTORIAL

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