Hydrolysis of synthetic chromogenic substrates by HIV-1 and HIV-2 proteinases.
Kinetic constants (Km,Kcat) are derived for the hydrolysis of a number of chromogenic peptide substrates by the aspartic proteinase from HIV-2. The effect of systematic replacement of the P2 residue on substrate hydrolysis by HIV-1 and HIV-2 proteinases is examined.
Department of Biochemistry, University of Wales College, Cardiff, U.K.
L H
LH
Phylip
A D
AD
Richards
J
J
Kay
J
J
Kovalinka
P
P
Strop
I
I
Blaha
J
J
Velek
V
V
Kostka
A J
AJ
Ritchie
A V
AV
Broadhurst
D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000378:metabolism*; D015684:Gene Products, pol / Q000378:metabolism*; D016333:HIV Protease; D015497:HIV-1 / Q000201:enzymology*; D015498:HIV-2 / Q000201:enzymology*; D066298:In Vitro Techniques; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D015684:Gene Products, pol; D009842:Oligopeptides; D010450:Endopeptidases; D016333:HIV Protease