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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Rational engineering of activity and specificity in a serine protease.

The discovery of the Na(+)-dependent allosteric regulation in serine proteases makes it possible to control catalytic activity and specificity in this class of enzymes in a way never considered before. We demonstrate that rational site-directed mutagenesis of residues controlling Na+ binding can profoundly after the properties of a serine protease. By suppressing Na+ binding to thrombin, we shift the balance between procoagulant and anticoagulant activities of the enzyme. Those mutants, compared to wild-type, have reduced specificity toward fibrinogen, but enhanced or slightly reduced specificity toward protein C. Because this engineering strategy targets a fundamental regulatory mechanism, it is amenable of extension to other enzymes of biological and pharmacological importance.[1]


  1. Rational engineering of activity and specificity in a serine protease. Dang, Q.D., Guinto, E.R., di Cera, E. Nat. Biotechnol. (1997) [Pubmed]
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