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Titolo:
THE SYNTHESIS OF INHIBITORS FOR PROCESSING PROTEINASES AND THEIR ACTION ON THE KEX2 PROTEINASE OF YEAST
Autore:
ANGLIKER H; WIKSTROM P; SHAW E; BRENNER C; FULLER RS;
Indirizzi:
FRIEDRICH MIESCHER INST,POB 2543 CH-4002 BASEL SWITZERLAND STANFORD UNIV,MED CTR,SCH MED,DEPT BIOCHEM STANFORD CA 94305
Titolo Testata:
Biochemical journal
, volume: 293, anno: 1993,
parte:, 1
pagine: 75 - 81
SICI:
0264-6021(1993)293:<75:TSOIFP>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
SERINE PROTEASE; GENE-PRODUCT; PROHORMONE; ENDOPEPTIDASE; KETONES; RESIDUES; ARGININE; THROMBIN; COMPLEX; ENZYMES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
H. Angliker et al., "THE SYNTHESIS OF INHIBITORS FOR PROCESSING PROTEINASES AND THEIR ACTION ON THE KEX2 PROTEINASE OF YEAST", Biochemical journal, 293, 1993, pp. 75-81

Abstract

Peptidyl chloromethane and sulphonium salts containing multiple Arg and Lys residues were synthesized as potential inhibitors of prohormoneand pro-protein processing proteinases. The potencies of these compounds were assayed by measuring the kinetics of inactivation of the yeast Kex2 proteinase, the prototype of a growing family of eukaroytic precursor processing proteinases. The most potent inhibitor, Pro-Nvl-Tyr-Lys-Arg-chloromethane, was based on cleavage sites in the natural Kex2substrate pro-alpha-factor. This inhibitor exhibited a K(i) of 3.7 nMand a second-order inactivation rate constant (k2/K(i)) of 1.3 x 10(7) M-1 . s-1 comparable with the value of k(cat)/K(m) obtained with Kex2 for the corresponding peptidyl methylcoumarinylamide substrate. The enzyme exhibited sensitivity to the other peptidyl chloromethanes overa range of concentrations, depending on peptide sequence and alpha-amino decanoylation, but was completely resistant to peptidyl sulphoniumsalts. Kinetics of inactivation by these new inhibitors of a set of 'control' proteinases, including members of both the trypsin and subtilisin families, underscored the apparent specificity of the compounds most active against Kex2 proteinase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:20:47