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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 anthraquinone and enediyne halves of the antitumor antibiotic dynemicin A were previously thought to be assembled by two separate polyketide synthases (PKS). Now, a single polyketide synthase has been proposed to be responsible for their production, and a working model for their biosynthesis from a common octaketide intermediate has been suggested.
Biocatalysis, if selective, offers great potential for the well-controlled release of drugs and other payloads. Here, Minko and co-workers separate enzymes and substrates by loading them onto individual, polymer-coated nanoparticles, and show that a magnetic field switches on the catalytic activity by merging the polymer shells.
Peroxygenases can selectively functionalize organic compounds, but are sensitive to the co-substrate H2O2. Hollmann and co-workers show that water oxidation catalysts can provide a controlled supply of H2O2 to the enzyme in the presence of visible light, allowing efficient oxyfunctionalization without stoichiometric reductants.
The biosynthetic pathway of fusidane-type antibiotics, such as helvolic acid, is largely undiscovered. Here, the authors investigate the biosynthesis of helvolic acid, thereby determining the sequence of the enzymatic reactions involved in the process and the intermediates formed.
Within natural product biosynthetic pathways, nature has evolved highly selective catalysts capable of complexity generating reactions. Leveraging these tools, a suite of catalysts with complementary site- and stereoselectivity have been applied to the oxidative dearomatization of phenolic compounds, enabling one-pot transformations of phenols into various natural products.
The eukaryotic release factor eRF1 is able to recognize the three stop codons UAA, UAG and UGA with high accuracy, while discriminating against near-cognate codons. Here the authors use molecular dynamic simulation to provide insight into the molecular basis behind the remarkable codon specificity of eRF1.
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.