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Biocatalysis is the chemical process through which enzymes or other biological catalysts perform reactions between organic components. Biocatalysis has been used widely in the pharmaceutical industry to make small molecule drugs.
The emergence of novel catalytic functions in ancient proteins likely played a role in the evolution of modern enzymes. Here, the authors use protein sequences from Precambrian beta-lactamases and demonstrate that a single hydrophobic-to-ionizable amino acid mutation can lead to substantial Kemp eliminase activity.
Palladium (Pd) is a well-known catalyst in organic chemistry but its use in nanomedicine is limited. Here, the authors design a Pd nanoparticle that triggers the activation of an antitumour prodrug in vivo, which shows efficacy and improves toxicity compared to traditional solvent- and nanoparticle-drug formulations.
Obafluorin is a β-lactone antibiotic produced by Pseudomonas fluorescens. Here the authors present the biosynthetic gene cluster and biosynthetic pathway of obafluorin, which is characterized by a central transaldolase step catalysed by a rare L-threonine transaldolase.
Two papers provide insight into the reactivity of cytochrome P450s. A direct link between electron donation and reactivity has been shown with a selenocysteine-ligated P450 compound I, whereas a serine-ligated P450 (P411) has been engineered to catalyse an intermolecular C–H amination via nitrene transfer.
An artificial esterase with no known natural structural analogues has been formed via the homo-heptameric self-assembly of a designed peptide. This esterase represents the first report of a functional catalytic triad rationally engineered into a de novo protein framework.