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Mapping of the substrate-binding site of the human granulocyte elastase by the aid of tripeptidyl-p-nitroanilide substrates
Authors:Katalin Marossy  Gabriella Cs Szabó  Marianne Pozsgay  Pál Elődi
Institution:Department of Biochemistry, University Medical School, Debrecen, Hungary
Abstract:The kinetic properties of the human granulocyte elastase /EC 3.4.21.11/ were investigated with 24 tripeptidyl-pNA substrates. By the regression analysis of the kinetic data obtained with 15 substrates a relatively hydrophobic compound, Boc-D-Phe-Ala-Nle-pNA, was predicted as the optimal substrate sequence. The compound was synthesized, assayed and the predicted Km = 4.2 uM was confirmed experimentally. The substrate-binding site of granulocyte elastase appeared to be hydrophobic and very much similar to that of the pancreatic enzyme at the S2–S4 subsites, but the S1 subsite, which determines the primary specificity, could accomodate bulkier residues and it was less selective than that in the pancreatic enzyme.
Keywords:pNA  p-nitroanilide  Nle  norleucine  Suc  succinyl-  Bz  benzoyl-  Boc  tert-butoxycarbonyl-
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