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Titolo:
RATIONAL ENGINEERING OF ACTIVITY AND SPECIFICITY IN A SERINE-PROTEASE
Autore:
DANG QD; GUINTO ER; DICERA E;
Indirizzi:
WASHINGTON UNIV,SCH MED,DEPT BIOCHEM & MOL BIOPHYS ST LOUIS MO 63110 WASHINGTON UNIV,SCH MED,DEPT BIOCHEM & MOL BIOPHYS ST LOUIS MO 63110
Titolo Testata:
Nature biotechnology
fascicolo: 2, volume: 15, anno: 1997,
pagine: 146 - 149
SICI:
1087-0156(1997)15:2<146:REOAAS>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
SUBSTRATE-SPECIFICITY; BLOOD-COAGULATION; STRUCTURAL BASIS; THROMBIN; FIBRINOGEN; THROMBOMODULIN; ANTICOAGULANT; SUBSTITUTION; ACTIVATION; EVOLUTION;
Keywords:
BLOOD COAGULATION; PROTEIN ENGINEERING; THROMBIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
Q.D. Dang et al., "RATIONAL ENGINEERING OF ACTIVITY AND SPECIFICITY IN A SERINE-PROTEASE", Nature biotechnology, 15(2), 1997, pp. 146-149

Abstract

The discovery of the Na+-dependent allosteric regulation in serine proteases makes it possible to control catalytic activity and specificity in this class of enzymes in a way never considered before. We demonstrate that rational site-directed mutagenesis of residues controlling Na+ binding can profoundly alter the properties of a serine protease. By suppressing Na+ binding to thrombin, we shift the balance between procoagulant and anticoagulant activities of the enzyme. Those mutants,compared to wild-type, have reduced specificity toward fibrinogen, but enhanced or slightly reduced specificity toward protein C. Because this engineering strategy targets a fundamental regulatory mechanism, it is amenable of extension to other enzymes of biological and pharmacological importance.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 16/07/20 alle ore 05:13:42