Inhibition of human napsin A.
The newly-discovered human aspartic proteinase, napsin A was not susceptible to protein inhibitors from potato, squash or yeast but was weakly inhibited by the 17 kDa polypeptide from Ascaris lumbricoides and potently by isovaleryl and lactoyl-pepstatins. A series of synthetic inhibitors was also investigated which contained in the P(1)-P(1)' positions the dipeptide analogue statine or its phenylalanine or cyclohexylalanine homologues and in which the residues occupying P(4)-P(3)' were varied systematically. On this basis, the active site of napsin A can be readily distinguished from other human aspartic proteinases.
Cronshaw
Rebecca F
RF
School of Biosciences, Cardiff University, P.O. Box 911, Cardiff CF10 3US, Wales, UK.
Schauer-Vukasinovic
Vesna
V
Powell
David J
DJ
Giller
Thomas
T
Bur
Daniel
D
Kay
John
J
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry / Q000494:pharmacology; D000818:Animals; D017164:Ascaris lumbricoides / Q000737:chemistry; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors*; D001665:Binding Sites; D002478:Cells, Cultured; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D010436:Pepstatins / Q000737:chemistry / Q000494:pharmacology; D010455:Peptides / Q000494:pharmacology; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors
D000596:Amino Acids; D004791:Enzyme Inhibitors; D010436:Pepstatins; D010455:Peptides; D011994:Recombinant Proteins; D016282:Aspartic Acid Endopeptidases; C498549:NAPSA protein, human; C013165:statine