Synthesis, structure and activity of artificial, rationally designed catalytic polypeptides View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-10

AUTHORS

K Johnsson, R K Allemann, H Widmer, S A Benner

ABSTRACT

Biological macromolecules with catalytic activity can be created artificially using two approaches. The first exploits a system that selects a few catalytically active biomolecules from a large pool of randomly generated (and largely inactive) molecules. Catalytic antibodies and many catalytic RNA molecules are obtained in this way. The second involves rational design of a biomolecule that folds in solution to present to the substrate an array of catalytic functional groups. Here we report the synthesis of rationally designed polypeptides that catalyse the decarboxylation of oxaloacetate via an imine intermediate. We determine the secondary structures of the polypeptides by two-dimensional NMR spectroscopy. We are able to trap and identify intermediates in the catalytic cycle, and to explore the kinetics in detail. The formation of the imine by our artificial oxaloacetate decarboxylases is three to four orders of magnitude faster than can be achieved with simple amine catalysts: this performance rivals that of typical catalytic antibodies. More... »

PAGES

530

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/365530a0

DOI

http://dx.doi.org/10.1038/365530a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1025053769

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8413606


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