| Literature DB >> 1551417 |
C M Kam1, J E Kerrigan, K M Dolman, R Goldschmeding, A E Von dem Borne, J C Powers.
Abstract
Various amino acid and peptide thioesters were tested as substrates for human proteinase 3 and the best substrate is Boc-Ala-Ala-Nva-SBzl with a kcat/Km value of 1.0 x 10(6) M-1.s-1. Boc-Ala-Ala-AA-SBzl (AA = Val, Ala, or Met) are also good substrates with kcat/Km values of (1-4) x 10(5) M-1.s-1. Substituted isocoumarins are potent inhibitors of proteinase 3 and the best inhibitors are 7-amino-4-chloro-3-(2-bromoethoxy)isocoumarin and 3,4-dichloroisocoumarin (DCI) with kobs/[I] values of 4700 and 2600 M-1.s-1, respectively. Substituted isocoumarins, peptide phosphonates and chloromethyl ketones inhibited proteinase 3 less potently than human neutrophil elastase (HNE) by 1-2 orders of magnitude.Entities:
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Year: 1992 PMID： 1551417 DOI： 10.1016/0014-5793(92)80340-m
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124