Featured
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Article |
Regio- and stereoselectivity of P450-catalysed hydroxylation of steroids controlled by laboratory evolution
Selective reaction of one C–H bond among many in complex organic molecules is a grand challenge for organic chemistry. Here, starting from an enzyme that oxidizes two positions in a steroid without bias, laboratory evolution is used to prepare mutants that can regio- and stereoselectively oxidize either position.
- Sabrina Kille
- , Felipe E. Zilly
- & Manfred T. Reetz
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News & Views |
C–H activation is a Reiske business
Enzymes that selectively oxidize unactivated C–H bonds are capable of constructing complex molecules with high efficiency. A new member of this enzyme family is RedG, a Reiske-type oxygenase that catalyses chemically challenging cyclizations in the biosynthesis of prodiginine natural products.
- Steven D. Bruner
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Article |
Stereoselective C–C bond formation catalysed by engineered carboxymethylproline synthases
The reaction of enols and enolates with electrophiles is used extensively in synthesis. Here, protein engineering — substituting amino acid residues in an enzyme active site — is used to produce biocatalysts for the control of enolate chemistry. The adapted enzymes enable stereoselective C–C bond formation yielding N-heterocycles in high diastereomeric excess by the reaction of trisubstituted-enolates.
- Refaat B. Hamed
- , J. Ruben Gomez-Castellanos
- & Christopher J. Schofield
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News & Views |
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
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News & Views |
Control of active-site compression
Compression of the active sites of enzymes has been linked to the bulk of amino acid side chains, but now experiments highlight that the harder we look, the more curious the relationship between protein structure and function becomes.
- Judith P. Klinman
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News & Views |
Access granted
Enzymes keep their catalytic reactivity under fine control, letting appropriate molecules approach their active sites to perform reactions. Now, studies of calixarenes attached to gold clusters to emulate this behaviour in synthetic systems suggest that the key to accessibility could be a matter of the relative sizes of ligands and metal clusters.
- Graham J. Hutchings
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Research Highlights |
Nitrogenase branches out
A vanadium-containing nitrogenase enzyme can reduce carbon monoxide to ethane and propane.
- Neil Withers
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News & Views |
Shaping enzyme inhibitors
Small-molecule enzyme-inhibitors often display insufficient affinity and selectivity for their targets causing unwanted side effects when used as drugs. Molecularly imprinted polymers prepared using the enzyme as a template could offer a solution.
- Börje Sellergren