Literatur vom gleichen Autor/der gleichen Autor*in
plus bei Google Scholar

Bibliografische Daten exportieren
 

Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding

Titelangaben

Scholz, Christian ; Stoller, Gerlind ; Zarnt, Toralf ; Fischer, Gunter ; Schmid, Franz X.:
Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding.
In: The EMBO Journal. Bd. 16 (1997) Heft 1 . - S. 54-58.
ISSN 1460-2075
DOI: https://doi.org/10.1093/emboj/16.1.54

Abstract

The trigger factor of Escherichia coli is a prolyl isomerase and accelerates proline-limited steps in protein folding with a very high efficiency. It associates with nascent polypeptide chains at the ribosome and is thought to catalyse the folding of newly synthesized proteins. In its enzymatic mechanism the trigger factor follows the Michaelis-Menten equation. The unusually high folding activity of the trigger factor originates from its tight binding to the folding protein substrate, as reflected in the low Km value of 0.7 microM. In contrast, the catalytic constant kcat is small and shows a value of 1.3 s(-1) at 15 degrees C. An unfolded protein inhibits the trigger factor in a competitive fashion. The isolated catalytic domain of the trigger factor retains the full prolyl isomerase activity towards short peptides, but in a protein folding reaction its activity is 800-fold reduced and no longer inhibited by an unfolded protein. Unlike the prolyl isomerase site, the polypeptide binding site obviously extends beyond the FKBP domain. Together, this suggests that the good substrate binding, i.e. the chaperone property, of the intact trigger factor is responsible for its high efficiency as a catalyst of proline-limited protein folding.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Zusätzliche Informationen: PubMed-ID: 6395866
Institutionen der Universität: Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Ehemalige Professoren > Professur Biochemie - Univ.-Prof. Dr. Franz Xaver Schmid
Fakultäten
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Professur Biochemie
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Ehemalige Professoren
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 540 Chemie
Eingestellt am: 18 Mai 2015 08:41
Letzte Änderung: 28 Feb 2023 13:30
URI: https://eref.uni-bayreuth.de/id/eprint/13521