Nicholas J. Weise

TL;DR: The discovery and mechanistic investigations of these commercially relevant enzymes are detailed, along with comparisons of their various applications as stand-alone catalysts, components of artificial biosynthetic pathways and biocatalytic or chemoenzymatic cascades, and therapeutic tools for the potential treatment of various pathologies.

TL;DR: The synthesis of substituted d-phenylalanines in high yield and excellent optical purity has been achieved with a novel one-pot approach by coupling phenylalanine ammonia lyase (PAL) amination with a chemoenzymatic deracemization (based on stereoselective oxidation and nonselective reduction).

TL;DR: A diverse library of novel enzymes were expressed and screened as cell‐free lysates for their ability to facilitate reductive amination to expand the known suite of biocatalysts for this transformation and to identify more enzymes with potential industrial applications.

TL;DR: Mechanistic studies using site-directed mutagenesis suggest that, following initial enzymatic adenylation of substrates, amidation of the carboxylic acid proceeds by direct reaction of the acylAdenylate with amine nucleophiles.

TL;DR: The discovery and characterisation of enzymes with both monoamine and diamine transaminase activity are reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor.