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Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein folding

Title data

Lang, Kurt ; Schmid, Franz X.:
Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein folding.
In: Nature. Vol. 331 (4 February 1988) Issue 6155 . - pp. 453-455.
ISSN 1476-4687
DOI: https://doi.org/10.1038/331453a0

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Abstract in another language

Two enzymes are now known that catalyse slow steps in protein folding. Peptidyl-prolyl cis-trans isomerase catalyses the cis-trans isomerization of Xaa-Pro peptide bonds in oligopeptides and during the refolding of several proteins. The other enzyme, protein-disulphide isomerase, accelerates the reactivation of reduced proteins, presumably by catalysis of thiol-disulphide exchange reactions. Recent evidence indicates that the beta-subunit of prolyl 4-hydroxylase, an enzyme involved in collagen biosynthesis, is identical with disulphide isomerase. On the basis of this important finding, it was suggested that disulphide isomerase accelerates protein folding, not by 'reshuffling' incorrect disulphide bonds, but in the same way as prolyl isomerase by catalysing proline isomerization which is known to be important for the folding of collagen and other proteins. Here we show that the catalytic activities of these two enzymes are different. Disulphide isomerase accelerates the reformation of native disulphide bonds during protein reoxidation. We find no evidence that this enzyme can catalyse the isomerization of proline peptide bonds, a reaction efficiently accelerated by prolyl isomerase. When both enzymes are present simultaneously during protein folding, they act independently of one another.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 3277061
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: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 30 Apr 2015 12:55
Last Modified: 30 Apr 2015 12:55
URI: https://eref.uni-bayreuth.de/id/eprint/11234