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Nat Chem Biol. 2008 May;4(5):290-4. doi: 10.1038/nchembio.80.

Highly active and selective endopeptidases with programmed substrate specificities.

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1
Institute for Cell and Molecular Biology, University of Texas, Austin, Texas 78712, USA.

Abstract

A family of engineered endopeptidases has been created that is capable of cleaving a diverse array of peptide sequences with high selectivity and catalytic efficiency (kcat/KM > 10(40 M(- 1) s(- 1)). By screening libraries with a selection-counterselection substrate method, protease variants were programmed to recognize amino acids having altered charge, size and hydrophobicity properties adjacent to the scissile bond of the substrate, including GluArg, a specificity that to our knowledge has not been observed among natural proteases. Members of this artificial protease family resulted from a relatively small number of amino acid substitutions that (at least in one case) proved to be epistatic.

PMID:
18391948
PMCID:
PMC2654239
DOI:
10.1038/nchembio.80
[Indexed for MEDLINE]
Free PMC Article
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