Carbon–carbon bond formation is the key reaction for organic synthesis to construct the
carbon framework of organic molecules. The review gives a selection of biocatalytic C–C …

Enzymes, at the turn of the 21st century, are gaining a momentum. Especially in the field of
synthetic organic chemistry, a broad variety of biocatalysts are being applied in an …

Despite the astonishing breadth of enzymes in nature, no enzymes are known for many of
the valuable catalytic transformations discovered by chemists. Recent work in enzyme …

Many enzymes work in tandem with small molecule cofactors, which have inspired
organocatalyst designs. Chemical modification of cofactor scaffolds has increased …

The reliable design and prediction of enzyme promiscuity to access transformations not
observed in nature remains a long‐standing challenge. Herein, we present the first example …

Enzymatic carbon–carbon (C–C) bond formation reactions have become an effective and
invaluable tool for designing new biological and medicinal molecules, often with asymmetric …

The human 2-oxoadipate dehydrogenase complex (OADHc) in L-lysine catabolism is
involved in the oxidative decarboxylation of 2-oxoadipate (OA) to glutaryl-CoA and NADH (+ …

Biocatalytic approaches are used widely for the synthesis of amines from abundant or low
cost starting materials. This is a fast-developing field where novel enzymes and enzyme …

The intermolecular asymmetric Stetter reaction is a rarely found biocatalysts transformation.
MenD, the second enzyme of the menaquinone biosynthetic pathway, catalyzes as a …

Using a protein scaffold covalently functionalised with a thiamine-inspired N-heterocyclic
carbene (NHC), we created an artificial Stetterase (ArtiSt) which catalyses a stereoselective …