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Sub‐site preferences of the aspartic proteinase from the human immunodeficiency virus, HIV‐1
Author(s) -
Konvalinka Jan,
Strop Petr,
Velek Jiri,
Cerna Vera,
Kostka Vladimir,
Phylip Lowri H.,
Richards Anthony D.,
Dunn Ben M.,
Kay John
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80966-m
Subject(s) - hydrolysis , residue (chemistry) , chemistry , peptide , human immunodeficiency virus (hiv) , stereochemistry , enzyme , chromogenic , enzyme kinetics , fast protein liquid chromatography , biochemistry , active site , chromatography , biology , virology
A series of synthetic, chromogenic substrates for HIV‐1 proteinase with the general structure Ala‐Thr‐His‐Xaa‐Yaa‐Zaa∗Nph‐Val‐Arg‐Lys‐Ala was synthesised with a variety of residues introduced into the Xaa, Yaa and Zaa positions. Kinetics parameters for hydrolysis of each peptide by HIV‐1 proteinase at pH 4.7, 37°C and u = 1.0 M were measured spectrophotometrically and/or by reverse phase FPLC. A variety of residues was found to be acceptable in the P 3 , position whilst hydrophobic/aromatic residues were preferable in P 1 . The nature of the residue occupying the P 2 ; position had a strong influence on k cat (with little effect on k m ;β‐branched residues Val or Ile in this position resulted in considerably faster peptide hydrolysis than when e.g. the Leu‐containing analogue was present in P 2 .