Enantioselective Reduction of Diaryl Ketones Catalyzed by a Carbonyl Reductase from <i>Sporobolomyces salmonicolor</i> and its Mutant Enzymes

Li, Hongmei; Zhu, Dunming; Ling, Hua; Biehl, Edward R.

doi:10.1002/adsc.200900045

Cited by 72 publications

(31 citation statements)

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“…Numerous potentially interesting substrates were tested, including aryl γ,δ-unsaturated-β-ketoesters [2], various substituted β-ketoesters [3][4][5][6], diaryl ketones [7], and bicyclic ketones [8]. All KREDs require a reduced cofactor NAD(P)H, which increases the cost of their application.…”

Section: Introductionmentioning

confidence: 99%

Co-Immobilization of Ketoreductase and Glucose Dehydrogenase

et al. 2018

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Abstract:A two-enzyme system composed of immobilized ketoreductase (Hansenula polymorpha) and glucose dehydrogenase (Bacillus megaterium) was developed for the asymmetric reduction of keto esters to optically active hydroxy esters via immobilization in polyvinyl alcohol (PVA) gel particles. The concentration of enzymes was optimized, and the final particles were used 18 times in a row in a batch mode to achieve minimal loss of activity and complete conversion of the model substrate, β-ketoester ethyl-2-methylacetoacetate. Excellent stability was also achieved using new storage conditions of PVA particles, with 80% of activity being retained after almost 10 months.

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Section: Introductionmentioning

confidence: 99%

Co-Immobilization of Ketoreductase and Glucose Dehydrogenase

et al. 2018

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“…The group of red to pinkish yeasts is one of the most interesting biocatalysts [30][31][32][33] in the reduction of differently substituted arylketones and among them Sporobolomyces salmonicolor is the best known for this application. As expected, this yeast was able to produce the desired product 5a in a quantitative yield with 80% e.e.…”

Section: Resultsmentioning

confidence: 99%

Simple 1,3-diamines and their application as ligands in ruthenium(ii) catalysts for asymmetric transfer hydrogenation of aryl ketones

et al. 2015

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In this research work simple unsymmetrical 1,3-diamines were studied. The synthesis of the diamines started from non-commercial available compounds. S-5a and S,S-5c were obtained by biocatalysis with non conventional yeast, Rhodotorula rubra MIM 147, with excellent 99% e.e. and d.e. up to 90%. Different approaches of synthesis were applied to the same backbone to study both the steric and electronic effects of the ligands. The reactivity of the corresponding ruthenium complexes was evaluated in the asymmetric hydrogen transfer reduction of acetophenone as a standard substrate and of other different aryl ketones, highlighting the flexibility of the six membered chelating ring. A screening of the reaction conditions indicated aqueous media in the presence of HCOONa as a hydrogen donor to be the best system for overcoming the lack of stereocontrol thus allowing us to obtain 56% e.e. in the reduction of acetophenone with the complex in which the ligand was diamine 1, revealed as the best in terms of reactivity and stereoselectivity also in the reduction of the other different aryl ketones, in particular for a-tetralone, i (63% e.e.).

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“…Expanding on the acetophenone study, Zhu and coworkers tested the Gln-245 mutants against benzophenones, including 4methylbenzophenone and 4-chlorobenzophenone, as shown in Table 20. 46 The wild type SSCR gave the Ralcohol in high ee for each of the two substrates, but the Q245L mutant SSCR gave R alcohols with lower ee. Interestingly, the Q245P mutation shifted the preference towards the S alcohol for both 4-methylbenzophenone and 4-chlorobenzophenone in moderate ee.…”

Section: Sporobolomyces Salmonicolor Carbonyl Reductase (Sscr)mentioning

confidence: 96%

Controlling Substrate Specificity and Stereospecificity of Alcohol Dehydrogenases

et al. 2015

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The ability to control the substrate specificity and stereochemistry of enzymatic reactions is of increasing interest in biocatalysis. As this review highlights, this control can be achieved through various means, including mutagenesis of active site residues, alteration of physical variables like temperature and pressure, as well as through changing the reaction medium. While the focus of this article is on alcohol dehydrogenase reactions, each of these techniques can be readily applied towards other enzyme classes as well.In order to understand better the orientation of the substrate in the enzyme active site, it is important to have a map of the active site. In pioneering studies of the 1960's, Prelog proposed using a diamond lattice structure to visualize oxidoreductase active sites. 2 To validate his hypothesis, he tested the reaction with a series of increasingly larger substrates, and was able to determine the maximum spatial limits of the active site in each direction. By overlaying the molecules, which gave successful results, the active site was effectively mapped. It was important to have a means to map the active site, since this would give a measure of the limit of stereospecificity, and in the future, substrate specificity.In an extension of Prelog's diamond lattice model, Jones and coworkers further studied its utility towards horse liver alcohol dehydrogenase (HLADH) reactions. 3-7 In the early 1980's, Jones and Jakovac proposed a cubic space section model, due to the disadvantages of the diamond lattice for mapping an active site. 3 Among the disadvantages were the use of sp 3 hybridized carbon bond lengths and angles which could invariably limit researchers to use the diamond lattice model to choose substrates for analysis. With the cubic space section model, the cube sizes were flexible, which allowed researchers to use blocks that were as large or small as desired. The results for simpler examples, which worked adequately with Prelog's diamond lattice, also worked satisfactorily with the cubic model. Jones and coworkers highlighted further examples that fit nicely with the new cubic shaped model. [4][5][6][7] While mutagenesis can be accomplished routinely at present, it was not always the case. Hence, Jones studied the varying active sites of naturally occurring variants. Even though the cubic space model was useful, it was not widely adopted by other research groups due to the advent of more straightforward X-ray crystal structures, which give very clear information regarding the shape of the active site. Nonetheless, these early active site models have paved the way for

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Enantioselective Reduction of Diaryl Ketones Catalyzed by a Carbonyl Reductase from Sporobolomyces salmonicolor and its Mutant Enzymes

Cited by 72 publications

References 50 publications

Co-Immobilization of Ketoreductase and Glucose Dehydrogenase

Co-Immobilization of Ketoreductase and Glucose Dehydrogenase

Simple 1,3-diamines and their application as ligands in ruthenium(ii) catalysts for asymmetric transfer hydrogenation of aryl ketones

Controlling Substrate Specificity and Stereospecificity of Alcohol Dehydrogenases

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