86838-20-2Relevant academic research and scientific papers
Engineering transketolase to accept both unnatural donor and acceptor substrates and produce α-hydroxyketones
Yu, Haoran,Hernández López, Roberto Icken,Steadman, David,Méndez-Sánchez, Daniel,Higson, Sally,Cázares-K?rner, Armando,Sheppard, Tom D.,Ward, John M.,Hailes, Helen C.,Dalby, Paul A.
, p. 1758 - 1776 (2020)
A narrow substrate range is a major limitation in exploiting enzymes more widely as catalysts in synthetic organic chemistry. For enzymes using two substrates, the simultaneous optimisation of both substrate specificities is also required for the rapid expansion of accepted substrates. Transketolase (TK) catalyses the reversible transfer of a C2-ketol unit from a donor substrate to an aldehyde acceptor and suffers the limitation of narrow substrate scope for industrial applications. Herein, TK from Escherichia?coli was engineered to accept both pyruvate, as a novel donor substrate, and unnatural acceptor aldehydes, including propanal, pentanal, hexanal and 3-formylbenzoic acid (FBA). Twenty single-mutant variants were first designed and characterised experimentally. Beneficial mutations were then recombined to construct a small library. Screening of this library identified the best variant with a 9.2-fold improvement in the yield towards pyruvate and propionaldehyde, relative to wild-type (WT). Pentanal and hexanal were used as acceptors to determine stereoselectivities of the reactions, which were found to be higher than 98% enantiomeric excess (ee) for the S configuration. Three variants were identified to be active for the reaction between pyruvate and 3-FBA. The best variant was able to convert 47% of substrate into product within 24?h, whereas no conversion was observed for WT. Docking experiments suggested a cooperation between the mutations responsible for donor and acceptor recognition, which would promote the activity towards both the acceptor and donor. The variants obtained have the potential to be used for developing catalytic pathways to a diverse range of high-value products.
Synthesis of Longhorn Beetle Pheromone Components by Proline-Mediated α-Hydroxylation of Alkyl Ketones
Do Carmo, Hugo,Amorós, María Eugenia,González, Andrés,Heguaburu, Viviana Lucía
, p. 4501 - 4506 (2021/08/17)
The stereoselective synthesis of several components of the aggregation pheromones of numerous longhorn beetle species is described. These attractants consist of 3-hydroxy-2-alkanones and 2,3-alkyldiols with chain lengths varying from six to ten carbons. T
Regio- and stereoselective reduction of diketones and oxidation of diols by biocatalytic hydrogen transfer
Edegger, Klaus,Stampfer, Wolfgang,Seisser, Birgit,Faber, Kurt,Mayer, Sandra F.,Oehrlein, Reinhold,Hafner, Andreas,Kroutil, Wolfgang
, p. 1904 - 1909 (2007/10/03)
The asymmetric reduction of symmetrical and nonsymmetrical diketones as well as the stereoselective oxidation of various diols by biocatalytic hydrogen transfer was investigated by employing lyophilized cells of Rhodococcus ruber DSM 44541 containing alcohol dehydrogense ADH-'A'. Symmetrical and nonsymmetrical diketones at the (ω-1)- and (ω-2)-positions are reduced to the Prelog product with high stereopreference, while sterically more demanding ketone moieties, for example those at the (ω-3)-position, remain unchanged. For the oxidation mode, differentiation between primary and secondary alcohols is achieved, and the (S)-configured secondary alcohols at the (ω-1)- and (ω-2)-positions are oxidized preferentially. Wiley-VCH Verlag GmbH & Co. KGaA, 2006.
Bio-catalysed synthesis of optically active Undecavertol enantiomers
Abate, Agnese,Brenna, Elisabetta,Fregosi, Ginevra
, p. 1997 - 1999 (2007/10/03)
Two enantiomers of Undecavertol were prepared by enzymatic methods and their odour properties evaluated.
A new route to protected acyloins and their enzymatic resolution with lipases
Scheid, Guenther,Kuit, Wouter,Ruijter, Eelco,Orru, Romano V. A.,Henke, Erik,Bornscheuer, Uwe,Wessjohann, Ludger A.
, p. 1063 - 1074 (2007/10/03)
A series of 16 different 3-acyloxy methyl ketones, the acyloin acetates and butyrates (±)-5, was synthesised by a straight-forward new method through alkylation of tert-butyl 2-acyloxyacetoacetates 3, followed by chemoselective dealkoxy-carbonylation of the tert-butyloxycarbonyl group in the presence of other ester groups. Subsequent hydrolysis of (±)-5 can be achieved with base to give racemic acyloins 6, or with lipase catalysis to afford the corresponding non-racemic acyloins (S)-6. The remaining (R)-acyloin esters 5 can be racemised and resubjected to the procedure, or hydrolysed chemically. The kinetic resolution with two of the six tested enzymes, CAL-B and BCL (PS) lipase, proceeded selectively [enantiomeric ratio (E) values between 50 and > 200] and most of the acyloins (S)-6 were obtained in very high enantiomeric excesses (up to > 99% ee). Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2004.
Kinetic resolution of vic-diols by Bacillus stearothermophilus diacetyl reductase
Bortolini, Olga,Casanova, Elena,Fantin, Giancarlo,Medici, Alessandro,Poli, Silvia,Hanau, Stefania
, p. 647 - 651 (2007/10/03)
The kinetic resolution of several racemic syn- and anti-1,2-diols by enzymatic oxidation with Bacillus stearothermophilus diacetyl reductase is described. The enantiomerically pure (R,R)- and (R,S)-diols are recovered in almost quantitative yield.
Chemoenzymatic synthesis of 'α-bichiral' synthons. Application to the preparation of chiral epoxides
Besse,Veschambre
, p. 1271 - 1285 (2007/10/02)
Microbiological reduction of 3-bromo-2-octanone and 3-azido-2-octanone led to all the stereoisomers of 3-bromo-2-octanol and 3-azido-2-octanol. Chiral 2,3-epoxyoctanes were prepared from the 3-bromo-2-octanols.
