Engineered Metal Regulation of Trypsin Specificity

Histidine substrate specificity has been engineered into trypsin by creating metal binding sites for Ni2+ and Zn2+ ions. The sites bridge the substrate and enzyme on the leaving-group side of the scissile bond. Application of simple steric and geometric criteria to a crystallographically derived enz...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Biochemistry (Easton) 1995-02, Vol.34 (7), p.2172-2180
Hauptverfasser:	Willett, W. Scott, Gillmor, Sarah A, Perona, John J, Fletterick, Robert J, Craik, Charles S
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Amino Acid Sequence Computer Simulation Crystallography, X-Ray Drug Design GENIE GENETIQUE HISTIDINA HISTIDINE INGENIERIA GENETICA Kinetics MEDIO DE CULTIVO Metals - metabolism MILIEU DE CULTURE Models, Molecular Molecular Sequence Data MUTACION Mutagenesis, Site-Directed MUTATION Peptides - chemistry Peptides - metabolism SACCHAROMYCES CEREVISIAE Structure-Activity Relationship Substrate Specificity TRIPSINA Trypsin - metabolism TRYPSINE
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!