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Titolo:
Application of linear free energy relationships to the serpin-proteinase inhibition mechanism
Autore:
Nash, P; McFadden, G; Whitty, A;
Indirizzi:
Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada Univ Alberta Edmonton AB Canada T6G 2H7 hem, Edmonton, AB T6G 2H7, Canada Univ Western Ontario, John P Robarts Res Inst, London, ON N6G 2V4, Canada Univ Western Ontario London ON Canada N6G 2V4 London, ON N6G 2V4, Canada Univ Western Ontario, Dept Microbiol & Immunol, London, ON N6G 2V4, CanadaUniv Western Ontario London ON Canada N6G 2V4 London, ON N6G 2V4, Canada Biogen Inc, Dept Prot Engn, Cambridge, MA 02142 USA Biogen Inc Cambridge MA USA 02142 Dept Prot Engn, Cambridge, MA 02142 USA
Titolo Testata:
FEBS LETTERS
fascicolo: 1, volume: 475, anno: 2000,
pagine: 1 - 6
SICI:
0014-5793(20000609)475:1<1:AOLFER>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
MYXOMA VIRUS; BRONSTED ANALYSIS; EXOGENOUS AMINES; CYTOCHROME-P450; P21(RAS); COMPLEX; MUTANT; ALPHA-2-ANTIPLASMIN; HYDROLYSIS; OXIDATION;
Keywords:
inhibition kinetics; LFER; protease; proteinaceous inhibitor; poxvirus; structure-activity relationship;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Nash, P Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Programme Mol Biol & Canc, 600 Univ Ave,Room 1081, Toronto, ON M5G 1X5, Canada Mt Sinai Hosp 600 Univ Ave,Room 1081 Toronto ON Canada M5G 1X5 ada
Citazione:
P. Nash et al., "Application of linear free energy relationships to the serpin-proteinase inhibition mechanism", FEBS LETTER, 475(1), 2000, pp. 1-6

Abstract

Linear free energy relationships can be used to link the changes in rate constant for a reaction to changes in the equilibrium caused by alterations in structure. While they have most often been used in the analysis of chemical reactions, they have also been employed to resolve questions in enzymology and protein folding. Here we analyze the reaction of a serpin with a panel of six serine proteinases, and observe that a linear free energy relationship exists between the true second-order rate constant for reaction, k(inh), and the inhibition constant, K-I, indicating that formation of the covalent serpin-enzyme complex may be reversible. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 10:19:10