Enzymkatalysierte Synthese von (<i>S</i>)‐Cyanhydrinen

Niedermeyer, Uwe; Kula, Maria‐Regina

doi:10.1002/ange.19901020420

Cited by 43 publications

(5 citation statements)

References 10 publications

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“…Initial investigations were performed on the natural substrate 4-hydroxybenzaldehyde, and rather promising results concerning the enantiomeric excess were found [83]. As already mentioned, the (S)-hydroxynitrile lyase from Sorghum bicolor adds HCN only to aromatic and heteroaromatic aldehydes.…”

Section: Enzymatic Synthesis Of Cyanohydrinsmentioning

confidence: 97%

Formation of CC Bonds: Enzymatic Synthesis of Cyanohydrins

Fechter¹,

Griengl²

2002

Enzyme Catalysis in Organic Synthesis

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Section: Enzymatic Synthesis Of Cyanohydrinsmentioning

confidence: 97%

Formation of CC Bonds: Enzymatic Synthesis of Cyanohydrins

Fechter¹,

Griengl²

2002

Enzyme Catalysis in Organic Synthesis

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“…Its major drawback is the limited substrate tolerance, only aromatic and heteroaromatic aldehydes are accepted, while aliphatic aldehydes or ketones are not converted. For a wide range of 3‐ and 4‐substituted aromatic aldehydes excellent selectivities were obtained 140d. 148…”

Section: Enzymes Used For Carbon‐carbon Bond Formationmentioning

confidence: 98%

Biocatalytic Methods for CC Bond Formation

2013

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Carbon‐carbon bond formation is among the most challenging transformations in the organic synthetic chemistry. Enzymes capable to perform this reaction are of great interest. The enzymes for stereoselective CC bond formations have been investigated very intensively during the last two decades. New recombinant DNA technologies have paved the way for improved catalysts and broaden the application scope of the already known enzymes and reactions. On the other side new discoveries have brought more enzyme players in the arena of CC bond formation reactions. Novel enzymatic CC bond formation reactions have been applied, implying the most important benefit of biocatalysis, namely the high selectivity.

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“…In the presence of an immobilized oxynitrilase a highly enantioselective process has been achieved. Another strategy to suppress the undesired reaction is conducting the enzymatic hydrocyanation at low pH values as demonstrated by the Kula group [58]. In recent years a range of recombinant oxynitrilases have been developed and utilized typically in an isolated form.…”

Section: Oxynitrilase-catalyzed Hydrocyanation Of Aldehydesmentioning

confidence: 99%

Asymmetric Synthesis with Recombinant Whole‐Cell Catalysts

2016

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c h a p t e r 2 3 INTRODUCTIONAsymmetric catalytic transformations play a central role in the field of organic chemistry and are of great interest for applications in the chemical and pharmaceutical industry. Among those, hydrolytic and reverse reactions to form carboxylate deriva tives as well as C─C bond-forming and redox reactions are of particular importance. For a long time this field was dominated by the use of chemocatalysts [1]. For example, numerous chiral heavy-metal complexes have been found to be highly efficient cat alysts, on a technical scale, in particular, for the asymmetric reduction of imines, ketones, and enamides. A representative success story is imine reduction for the man ufacture of metolachlor as one of the largest industrially applied asymmetric chemo catalytic processes to date, and the widely technically applied hydrogenation technology for the reduction of ketones and enamides, for which Noyori and Knowles were awarded the Nobel Prize [2]. An alternative for the production of chiral building blocks, with a continuously increasing number of examples, also on an industrial scale, is biocatalysis. Known for a long time, the use of biocatalytic alternatives has also been limited for a long time, which has been due to-among others-the following two reasons: (i) wild-type whole cells such as baker's yeast require a large amount of biomass (due to the forma tion of the desired enzymes in the cell only in low amounts) and often give unsatisfy ing enantioselectivities (due to the action of more than one enzyme), and (ii) the use of isolated enzymes requires additional costs for cell disruption and enzyme isolation as well as the addition of an external amount of cofactor. Due to impressive progress in the field of molecular biology, these limitations have often been overcome. High overexpression of the desired enzyme in recombinant host organism and high cell density fermentation technology provide efficient and economically attractive access to these microorganisms (so-called designer cells), which contain exclusively the desired biocatalyst (enzyme) in large amounts. Such designer cells can be used directly in organic synthetic reactions without the need to isolate the enzyme in additional downstream operation steps. The presence of the cofactor in the cells requires no addition of an external amount of cofactors or supply thereof in very low amount only. Due to these advantages, recombinant whole cells overexpressing cofactor dependent enzymes have become very attractive catalysts for asymmetric synthesis. This is underlined by an increasing number of recent organic biotransformations based on the use of such "designer cells."

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Enzymkatalysierte Synthese von (S)‐Cyanhydrinen

Cited by 43 publications

References 10 publications

Formation of CC Bonds: Enzymatic Synthesis of Cyanohydrins

Formation of CC Bonds: Enzymatic Synthesis of Cyanohydrins

Biocatalytic Methods for CC Bond Formation

Asymmetric Synthesis with Recombinant Whole‐Cell Catalysts

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