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Titolo:
THEORY OF ALLOSTERIC EFFECTS IN SERINE PROTEASES
Autore:
DICERA E; HOPFNER KP; DANG QD;
Indirizzi:
WASHINGTON UNIV,SCH MED,DEPT BIOCHEM & MOLEC BIOPHYS,660 S EUCLID AVE,BOX 8231 ST LOUIS MO 63110
Titolo Testata:
Biophysical journal
fascicolo: 1, volume: 70, anno: 1996,
pagine: 174 - 181
SICI:
0006-3495(1996)70:1<174:TOAEIS>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
MONO-VALENT CATIONS; PROTEIN-C; THROMBOMODULIN; STIMULATION; THROMBIN; AMIDASE; ENZYME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
E. Dicera et al., "THEORY OF ALLOSTERIC EFFECTS IN SERINE PROTEASES", Biophysical journal, 70(1), 1996, pp. 174-181

Abstract

The classical Botts-Morales theory for the action of a modifier on the catalytic properties of an enzyme has been extended to deal with allosteric effects in serine proteases. The exact analytical solution derived for the linkage scheme at steady state provides a rigorous framework for the study of many biologically relevant systems, including enzymes activated by monovalent cations and cofactor-controlled protease-zymogen interactions in blood coagulation, When the enzyme obeys Michaelis-Menten kinetics, the exact solution of the kinetic linkage schemesimplifies considerably, Of particular importance for practical applications is a simple equation expressing the dependence of the specificity constant of the enzyme, k(cat)/K-m, on the concentration of the modifier, from which the equilibrium binding constant for the formation of the enzyme-modifier complex can be estimated, Analysis of the allosteric changes in thrombin activity induced by thrombomodulin and Na+ in terms of this equation yields accurate determinations of the equilibrium binding constants for both effecters.

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Documento generato il 22/09/20 alle ore 20:46:12