Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acids / chemistry
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Amino Acids / pharmacology
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Animals
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Ascaris lumbricoides / chemistry
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Aspartic Acid Endopeptidases / antagonists & inhibitors*
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Binding Sites
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Cells, Cultured
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Humans
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Kinetics
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Models, Molecular
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Pepstatins / chemistry
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Pepstatins / pharmacology
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Peptides / pharmacology
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Recombinant Proteins / antagonists & inhibitors
Substances
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Amino Acids
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Enzyme Inhibitors
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Pepstatins
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Peptides
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Recombinant Proteins
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Aspartic Acid Endopeptidases
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NAPSA protein, human
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statine