Hydrolases articles within Nature Chemistry

Featured

• Article | 04 July 2016

  Installing hydrolytic activity into a completely de novo protein framework

  Functional catalytic triads have been designed into a hyperstable heptameric α-helical barrel protein. Twenty-one mutations were introduced to form seven Cys-His-Glu catalytic triads. The resulting protein hydrolyses p-nitrophenyl acetate with activities matching the most-efficient redesigned hydrolases based on natural protein scaffolds. This is the first example of a functional catalytic triad being engineered into a fully de novo protein.

  • Antony J. Burton
  • , Andrew R. Thomson
  •  & Derek N. Woolfson

• News & Views | 23 November 2010

  Detection by failure

  Testing for enzymes is important for diagnosing various medical conditions but can be problematic because of the complexity of physiological media such as blood. Now, a method of detecting phospholipases has been developed that neatly couples their concentration with the aggregation of gold nanoparticles.

  • Nicholas A. Melosh