Enzymatic cascade reactions experience tremendous attention by cutting short conventional step-by-step synthesis in a highly efficient and elegant fashion. Focusing on ω-transaminases, this review provides an overview of different biocatalytic strategies to afford variety (chiral) amines employing diverse systems: Cascades shift the reaction equilibrium as well cascades for amination alcohols nonactivated C–H bonds are discussed. enable deracemization rac-amines, other ones involve...

During the last decade use of transaminases for production pharmaceutical and fine chemical intermediates has attracted a great deal attention. Transaminases are versatile biocatalysts efficient amine many have (S)-enantiospecificity. with (R)-specificity needed to expand applications these enzymes in biocatalysis. In this work we identified fungal putative (R)-specific transaminase from Eurotiomycetes Nectria haematococca, cloned synthetic version gene, demonstrated (R)-selective...

The Friedel-Crafts acylation is commonly used for the synthesis of aryl ketones, and a biocatalytic version, which may benefit from chemo- regioselectivity enzymes, has not yet been introduced. Described here bacterial acyltransferase can catalyze C-acylation phenolic substrates in buffer without need CoA-activated reagents. Conversions reach up to >99 %, various C- or O-acyl donors, such as DAPG isopropenyl acetate, are accepted by this enzyme. Furthermore enzyme enables Fries...

A whole-cell catalyst using Escherichia coli BL21(DE3) as a host, co-expressing glycerol dehydrogenase (GlyDH) from Gluconobacter oxydans and glucose (GDH) Bacillus subtilis for cofactor regeneration, has been successfully constructed used the reduction of aliphatic aldehydes, such hexanal or glyceraldehyde to corresponding alcohols. This was characterized in terms growth conditions, temperature pH dependency, regarding influence external permeabilization. In case addition we found 4.6-fold...

Stereoselective methods for the synthesis of tetrahydro-ß-carbolines are significant interest due to broad spectrum biological activity target molecules. In plant kingdom, strictosidine synthases catalyze C-C coupling through a Pictet-Spengler reaction tryptamine and secologanin exclusively form (S)-configured tetrahydro-ß-carboline (S)-strictosidine. Investigating biocatalytic with small-molecular-weight aliphatic aldehydes revealed that give unexpectedly access (R)-configured product....

The acetic acid bacterium Gluconobacter oxydans has a high potential for oxidoreductases with variety of different catalytic abilities. One putative oxidoreductase gene codes an enzyme similarity to the NADP+-dependent glycerol dehydrogenase (GlyDH) from Hypocrea jecorina. Due this homology, GlyDH (Gox1615) been cloned, over-expressed in Escherichia coli, purified and characterised. Gox1615 shows apparent native molecular mass 39 kDa, which corresponds well 37.213 kDa calculated primary...

Abstract Natural L ‐α‐amino acids and ‐norleucine were transformed to the corresponding α‐hydroxy by formal biocatalytic inversion or retention of absolute configuration. The one‐pot transformation was achieved a concurrent oxidation reduction cascade in aqueous media. A representative panel enantiopure ( R )‐ S )‐2‐hydroxy possessing aliphatic, aromatic heteroaromatic moieties isolated high yield (67–85 %) form (>99 % ee ) without requiring chromatographic purification.

An efficient and stereoselective biocatalytic route for the synthesis of 17α-amino steroids has been developed.

A synthetic biology approach enabled the design of a single <italic>E. coli</italic> cell catalyst co-expressing three enzymes (<sc>l</sc>-AAD, <sc>l</sc>- or <sc>d</sc>-HIC and FDH) for quantitatively transformation <sc>l</sc>-amino acids to corresponding optically pure (<italic>R</italic>)- (<italic>S</italic>)-α-hydroxy acids.

Abstract Organofluorine compounds have become important building blocks for a broad range of advanced materials, polymers, agrochemicals, and increasingly pharmaceuticals. Despite tremendous progress within the area fluorination chemistry, methods direct introduction fluoroalkyl-groups into organic molecules without prefunctionalization are still highly desired. Here we present concept trifluoromethyl group unprotected phenols by employing biocatalyst (laccase), t BuOOH, either Langlois’...

Abstract The NAD + ‐dependent lactate dehydrogenase from Bacillus subtilis (BsLDH) catalyzes the enantioselective reduction of pyruvate to lactate. BsLDH is highly specific and exhibits only a low activity with NADP as cofactor. Based on high good stability LDHs, these enzymes have been frequently used for regeneration . While an application in not sufficient due cofactor preference BsLDH. In addition, LDHs yet found nature. Therefore, structure‐based approach was performed predict amino...

The potential of several enantiocomplementary ω-transaminases (ω-TAms) for the amination cyclic ketones has been investigated.

Introduction of an alanine racemase allowed the use of<sc>l</sc>-alanine as initial amine source for biocatalytic amination leading to (<italic>R</italic>)-amines.

Abstract Synthetically established methods for methylation of phenols and demethylation methyl phenyl ethers rely in general on hazardous reagents or/and harsh reaction conditions are irreversible. Consequently, alternative regioselective the reversible formation breakage C-O-ether bonds to be performed under mild sustainable highly desired. Here we present a biocatalytic shuttle concept making use corrinoid-dependent transferases from anaerobic bacteria. The two-component enzymatic system...

Readily available phenol derivatives were substituted in para-position via a C–C bond formation to give enantiomerically pure (R)- or (S)-3-(para-hydroxyphenyl) lactic acids. The transformation was achieved by designing biocatalytic cascade consisting of three linear steps, namely, (i) the coupling and pyruvate presence ammonia afford corresponding l-tyrosine derivative, followed (ii) oxidative deamination (iii) enantioselective reduction. Compatibility analysis showed that reaction rate...

A chemoenzymatic two-step one-pot process in aqueous media combining a Wittig synthesis and subsequent enzymatic CC double bond reduction the presence of recombinant enoate reductase from Gluconobacter oxydans as biocatalyst has been developed. The desired saturated ketones are obtained with an overall conversion greater than 95 %.

The cleavage of aryl methyl ethers is a common reaction in chemistry requiring rather harsh conditions; consequently, it prone to undesired reactions and lacks regioselectivity. Nevertheless, O-demethylation tool valorize natural pharmaceutical compounds by deprotecting reactive hydroxyl moieties. Various oxidative enzymes are known catalyze this at the expense molecular oxygen, which may lead case phenols/catechols side (e.g., oxidation, polymerization). Here an oxygen-independent...

Abstract A two‐step synthesis of various enantiomerically pure 1‐aryl‐3‐methylisochroman derivatives was accomplished through asymmetric biocatalytic ketone reduction followed by an oxa‐Pictet–Spengler reaction. The compounds were obtained in good to excellent yield (47–92 %) favor the syn diastereomers [ dr ( / anti ) up 99:1]. Enantiopure arylpropanols serving as pronucleophiles for C–C bond‐formation step employing enantiocomplementary alcohol dehydrogenases, which gave access S and R...

Abstract Stereoselective methods for the synthesis of tetrahydro‐ß‐carbolines are significant interest due to broad spectrum biological activity target molecules. In plant kingdom, strictosidine synthases catalyze C−C coupling through a Pictet–Spengler reaction tryptamine and secologanin exclusively form ( S )‐configured tetrahydro‐ß‐carboline )‐strictosidine. Investigating biocatalytic with small‐molecular‐weight aliphatic aldehydes revealed that give unexpectedly access R product....

Abstract The Friedel–Crafts acylation is commonly used for the synthesis of aryl ketones, and a biocatalytic version, which may benefit from chemo‐ regioselectivity enzymes, has not yet been introduced. Described here bacterial acyltransferase can catalyze C‐acylation phenolic substrates in buffer without need CoA‐activated reagents. Conversions reach up to &gt;99 %, various C‐ or O‐acyl donors, such as DAPG isopropenyl acetate, are accepted by this enzyme. Furthermore enzyme enables Fries...