Themed collection Enzyme catalysis in organic synthesis

Editorial to accompany the Green Chemistry themed issue “Enzyme Catalysis in Organic Chemistry”.

Transaminase biocatalysis shows immense potential in industrial applications, and optimizations of both proteins and processes are of great importance.

Imine reductases (IREDs) show great potential as catalysts for reductive amination of ketones to produce chiral secondary amines.

By the combination of biocatalyst design and reaction engineering, the so far not stereoselectively accessible (S)-phenylacetylcarbinol could be enzymatically synthesized with product concentrations >48 g L⁻¹ and an enantiomeric excess up to 97%.

The photocatalytic oxidation of NADH using a flavin photocatalyst and a simple blue LED light source is reported.

Bifunctional transaminases enable a strategy for the production of chiral amines using small excesses of diamine donors.

The continuous flow synthesis of a series of amines was successfully achieved by exploiting the enhanced stability and broad substrate scope of an immobilised transaminase from Halomonas elongata (HEWT).

We investigated the valorisation of limonene containing waste product orange peel, and performed a biocatalytic cascade for the production of chiral carvolactone solely in water.

An immobilization engineering approach using bioinformatics and experimental design tools was applied to improve the sol–gel enzyme entrapment methodology.

N-Acetyl glucosamine (GlcNAc) is one of the most abundant biomolecules on Earth and is cheaply available from chitin, a major component of crustaceans.

Hydroxypyruvate was shown to be a nucleophile for class II pyruvate aldolases isolated from biodiversity, allowing unprecedented stereoselective cross-aldol reactions.

α,β-Unsaturated γ-keto esters were asymmetrically reduced by ene-reductases to yield versatile chiral intermediates in up to 99% ee.

Transketolase variants were engineered to utilize arylalkanals and benzaldehyde as substrates with up to 28-fold rate acceleration for C–C bond formation with good yields (50–73%) and virtually complete (3S)-stereoselectivity (>99% ee).

D-Amino acid transaminase plus mutant phenylalanine dehydrogenase offer an effective one-pot system for 100% conversion of DL-amino acids to the L-form.

A one-pot/two-step chemoenzymatic sequential methodology has been developed for the selective amination of secondary alcohols by combining the laccase from Trametes versicolor/TEMPO catalytic system with the stereoselective action of transaminases.

The present study addresses comprehensively the problem of producing polyesters through sustainable processes while using fully renewable raw materials and biocatalysts.

A biocatalytic approach using transaminases has been used for the generation of a range of furfurylamines in good yields.

In this study 26 new oligophenol cellulase inhibitors were discovered from wheat straw pretreatment liquors.

Oxidation of amino groups in amines or amino acids activates the sp³ C_α–H bond to form imines, making the alpha carbon atom a preferable target for nucleophilic reagents such as cyanide.

Chloroperoxidase (C. fumago) catalyzes the aerobic halogenative 5-endo-trig cyclization of allenes in an aqueous emulsion system yielding functionalized O-heterocyclic building blocks.

Naturally rare L-erythro (3S,4S)-ketoses were prepared at high temperatures through a simultaneous two-step enzymatic cascade synthesis with excellent stereoselectivity.

Optimised dual-enzyme (AmDH–FDH) reductive amination of a broad range of carbonyl compounds affords enantiopure amines with a conversion of up to 99% using ammonia as an amine donor and formate as a reducing reagent.

Whole-cell catalysts overexpressing two enzymes for a double reduction cascade in which aliphatic α-branched α,β-unsaturated aldehydes are converted into Guerbet alcohols as a highly demanded class of lubricants were constructed and applied in such biotransformations.

High enantioselective lipase catalyzed resolution of several cis and trans 3-aminopyridinylmethyl-4-hydroxypyrrolidines has been described. Some of these pyrrolidines are precursors in the synthesis of selective nNOS inhibitors.

Monoacylglycerides are biocatalytically synthesized by direct esterification in sponge-like ionic liquids with high selectivity (e.g. up to 100% monolaurin in [C₁₂mim][BF₄]).

A novel asymmetric synthesis of the title compounds was developed via the chemoenzymatic connection of three prochiral and achiral components.