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The prolyl isomerase SlyD is a highly efficient enzyme but decelerates the conformational folding of a client protein.

Title data

Zoldák, Gabriel ; Geitner, Anne-Juliane ; Schmid, Franz X.:
The prolyl isomerase SlyD is a highly efficient enzyme but decelerates the conformational folding of a client protein.
In: Journal of the American Chemical Society. Vol. 135 (20 March 2013) Issue 11 . - pp. 4372-4379.
ISSN 1520-5126
DOI: https://doi.org/10.1021/ja311775a

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Abstract in another language

Folding enzymes often use distinct domains for the interaction with a folding protein chain and for the catalysis of intrinsically slow reactions such as prolyl cis/trans isomerization. Here, we investigated the refolding reaction of ribonuclease T1 in the presence of the prolyl isomerase SlyD from Escherichia coli to examine how this enzyme catalyzes the folding of molecules with an incorrect trans proline isomer and how it modulates the conformational folding of the molecules with the correct cis proline. The kinetic analysis suggests that prolyl cis → trans isomerization in the SlyD-bound state shows a rate near 100 s(-1) and is thus more than 10(4)-fold accelerated, relative to the uncatalyzed reaction. As a consequence of its fast binding and efficient catalysis, SlyD retards the conformational folding of the protein molecules with the correct cis isomer, because it promotes the formation of the species with the incorrect trans isomer. In the presence of ≥1 μM SlyD, protein molecules with cis and trans prolyl isomers refold with identical rates, because SlyD-catalyzed cis/trans equilibration is faster than conformational folding. The cis or trans state of a particular proline is thus no longer a determinant for the rate of folding.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 23445547
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 22 Apr 2015 07:15
Last Modified: 22 Apr 2015 07:15
URI: https://eref.uni-bayreuth.de/id/eprint/10538