Comparison of the active site specificity of the aspartic proteinases based on a systematic series of peptide substrates.
Department of Biochemistry and Molecular Biology, University of Florida College of Medicine, Gainesville 32610-0245, USA.
B M
BM
Dunn
P E
PE
Scarborough
W T
WT
Lowther
C
C
Rao-Naik
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D002402:Cathepsin D / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism*; D010434:Pepsin A / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012233:Rhizopus / Q000201:enzymology; D013379:Substrate Specificity; D013552:Swine
D009842:Oligopeptides; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A; D002402:Cathepsin D