Engineering cyclophilin into a proline-specific endopeptidase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-01

AUTHORS

Eric Quéméneur, Mireille Moutiez, Jean-Baptiste Charbonnier, Andr Ménez

ABSTRACT

Designing an enzyme requires, among a number of parameters, the appropriate positioning of catalytic machinery within a substrate-binding cleft. Using the structures of cyclophilin-peptide complexes, we have engineered a new catalytic activity into an Escherichia coli cyclophilin by mutating three amino acids, close to the peptide binding cleft, to form a catalytic triad similar to that found in serine proteases. In conjunction with cyclophilin's specificity for proline-bearing peptides, this creates a unique endopeptidase, cyproase 1, which cleaves peptides on the amino-side of proline residues. When acting on an Ala-Pro dipeptide, cyproase 1 has an efficiency (kcat/Km) of 0.7 x 10(4) M(-1) s(-1) and enhances the rate of reaction (kcat/kuncat) 8 x 10(8)-fold. This activity depends upon a deprotonated histidine and is inhibited by nucleophile-specific reagents, as occurs in natural serine proteases. Cyproase 1 can hydrolyse a protein substrate with a proline-specific endoprotease activity. More... »

PAGES

301-304

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/34687

DOI

http://dx.doi.org/10.1038/34687

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022559417

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9440697


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