Novel Developments Employing Redox Enzymes: Old Enzymes in New Clothes

Faber, Kurt; Glueck, Silvia M.; Seisser, Birgit; Kroutil, Wolfgang

doi:10.1002/9780470627303.ch7

Cited by 5 publications

(1 citation statement)

References 185 publications

(173 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For instance the alcohol dehydrogenase from Lactobacillus brevis was successfully employed as a robust biocatalyst for stereoselective reduction of prochiral ketones (Leuchs and Greiner, 2011). Further leading examples are the ADHs isolated from Thermoanaerobacter brockii (Röthig et al, 1990), Candida boidinii (Bommarius et al, 1995), Rhodococcus erythropolis (Gröger et al, 2004) and Saccharomyces cerevisiae (Katz et al, 2003) and the carbonyl reductase from Candida parapsilosis (Stillger et al, 2002), which are currently implemented in stereoselective biotransformations at lab‐ as well as industrial‐scale (de Wildeman and Sereinig, 2011; Faber et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterization of an alcohol dehydrogenase from Ralstonia sp.

Kulig

Frese

Kroutil

et al. 2013

Biotech & Bioengineering

Self Cite

View full text Add to dashboard Cite

Stereoselective reduction towards pharmaceutically potent products with multi-chiral centers is an ongoing hot topic, but up to now catalysts for reductions of bulky aromatic substrates are rare. The NADPH-dependent alcohol dehydrogenase from Ralstonia sp. (RADH) is an exception as it prefers sterically demanding substrates. Recent studies with this enzyme indicated outstanding potential for the reduction of various alpha-hydroxy ketones, but were performed with crude cell extract, which hampered its detailed characterization. We have established a procedure for the purification and storage of RADH and found a significantly stabilizing effect by addition of CaCl(2). Detailed analysis of the pH-dependent activity and stability yielded a broad pH-optimum (pH 6-9.5) for the reduction reaction and a sharp optimum of pH 10-11.5 for the oxidation reaction. The enzyme exhibits highest stability at pH 5.5-8 and 8-15°C; nevertheless, biotransformations can also be carried out at 25°C (half-life 80 h). Under optimized reaction parameters a thorough study of the substrate range of RADH including the reduction of different aldehydes and ketones and the oxidation of a broad range of alcohols was conducted. In contrast to most other known alcohol dehydrogenases, RADH clearly prefers aromatic and cyclic aliphatic compounds, which makes this enzyme unique for conversion of space demanding substrates. Further, reductions are catalyzed with extremely high stereoselectivity (>99% enantio- and diastereomeric excess). In order to identify appropriate substrate and cofactor concentrations for biotransformations, kinetic parameters were determined for NADP(H) and selected substrates. Among these, we studied the reduction of both enantiomers of 2-hydroxypropiophenone in more detail.

show abstract

Section: Introductionmentioning

confidence: 99%

Biochemical characterization of an alcohol dehydrogenase from Ralstonia sp.

Kulig

Frese

Kroutil

et al. 2013

Biotech & Bioengineering

Self Cite

View full text Add to dashboard Cite

show abstract

The Substrate Spectrum of the Inverting sec‐Alkylsulfatase Pisa1

et al. 2012

View full text Add to dashboard Cite

The substrate spectrum of the inverting alkylsulfatase Pisa1 was investigated using a range of sec‐alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties. Perfect enantioselectivities were obtained for substrates bearing groups of different size adjacent to the sulfate ester moiety. Insufficient selectivities could be doubled by using dimethyl sulfoxide (DMSO) as co‐solvent. Hydrolytically unstable benzylic sulfate esters could be sufficiently stabilised by introduction of electron‐withdrawing substituents. Overall, Pisa1 appears to be a very useful inverting alkylsulfatase for the deracemisation of rac‐sec‐alcohols via enzymatic hydrolysis of their corresponding sulfate esters, which furnishes homochiral products possessing the ‘anti‐Kazlauskas’ configuration.

show abstract

Oxidation von Aldehyden mit Alkoholdehydrogenasen

et al. 2012

View full text Add to dashboard Cite

Neuigkeiten von alten Bekannten: Alkoholdehydrogenasen (ADHs) sind etablierte Redoxbiokatalysatoren, die noch für Überraschungen gut sind. Sie können auch für die Oxidation von Aldehyden verwendet werden, was anhand der oxidativen dynamischen Racematspaltung von Profenaldehyden demonstriert wird. In Gegenwart eines effizienten Cofaktor‐Regenerationssystems werden Aldehyde mit hoher Selektivität oxidiert.

show abstract

Novel Developments Employing Redox Enzymes: Old Enzymes in New Clothes

Cited by 5 publications

References 185 publications

Biochemical characterization of an alcohol dehydrogenase from Ralstonia sp.

Biochemical characterization of an alcohol dehydrogenase from Ralstonia sp.

The Substrate Spectrum of the Inverting sec‐Alkylsulfatase Pisa1

Oxidation von Aldehyden mit Alkoholdehydrogenasen

Contact Info

Product

Resources

About