4.1.2.47: (S)-hydroxynitrile lyase
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For detailed information about (S)-hydroxynitrile lyase, go to the full flat file.
Word Map on EC 4.1.2.47
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4.1.2.47
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esculenta
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manihot
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brasiliensis
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hevea
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synthesis
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cassava
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ketone
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hcn
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lyases
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benzaldehyde
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s-mandelonitrile
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rubber
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athnl
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crantz
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hydrocyanic
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s-cyanohydrins
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r-selective
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arylacetonitrilase
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s-enantiomer
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cyanogenesis
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montanum
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s-mandelic
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pharmacology
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agriculture
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analysis
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drug development
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food industry
- 4.1.2.47
- esculenta
- manihot
- brasiliensis
- hevea
- synthesis
- cassava
- ketone
- hcn
- lyases
- benzaldehyde
-
s-mandelonitrile
- rubber
- athnl
- crantz
-
hydrocyanic
-
s-cyanohydrins
-
r-selective
- arylacetonitrilase
-
s-enantiomer
-
cyanogenesis
- montanum
-
s-mandelic
- pharmacology
- agriculture
- analysis
- drug development
- food industry
Reaction
Synonyms
(R)-LuHNL, (R)-Oxynitrilase, (S)-cyanohydrin producing hydroxynitrile lyase, (S)-Hb-HNL, (S)-HbHNL, (S)-HNL, (S)-Hydroxynitrile lyase, (S)-Me-HNL, (S)-MeHNL, (S)-Oxynitrilase, (S)-selective HNL, (S)-selective hydroxynitrile lyase, Acetone cyanohydrin lyase, ACL, alpha-Hydroxynitrile lyase, EC 4.1.2.37, EC 4.1.2.39, Hb-HNL, HbHNL, HNL, HNL1, Hydroxynitrile lyase, LuHNL, MeHNKL, MeHNL, mut-HNL1, Oxynitrilase, S-HnL, S-hydroxynitrile lyase, S-selective HnL, S-selective hydroxynitrile lyase, S-stereoselective HNL
ECTree
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Application
Application on EC 4.1.2.47 - (S)-hydroxynitrile lyase
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agriculture
analysis
cyanide-based high-throughput screening assay is developed. The assay is useful to detect activity and enantioselectivity of hydroxynitrile lyases theoretically towards any cyanohydrin substrate
food industry
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root-specific expression of cassava HNL not only increases total root protein levels 3fold approaching the target values for a nutritionally balanced meal but accelerates cyanogenesis during food processing resulting in a safer and more nutritious food product
pharmacology
synthesis
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enantiomerically pure cyanohydrins produced by enzyme-catalyzed synthesis are important synthetic intermediates for agrochemicals
agriculture
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enantiomerically pure cyanohydrins produced by enzyme-catalyzed synthesis are important synthetic intermediates for agrochemicals
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enantiomerically pure cyanohydrins produced by enzyme-catalyzed synthesis are important synthetic intermediates for pharmaceuticals
pharmacology
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enantiomerically pure cyanohydrins produced by enzyme-catalyzed synthesis are important synthetic intermediates for pharmaceuticals
synthesis
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biocatalyst for the enantiospecific addition of hydrogen cyanide to aldehydes in organic solvents
synthesis
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biocatalyst for the enantiospecific addition of hydrogen cyanide to aldehydes in organic solvents
synthesis
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catalyzes the industrially interesting formation of (S)-cyanohydrins from aldehydes or ketones and HCN
synthesis
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industrial important biocatalyst used in enantiospecific syntheses of alpha-hydroxynitriles from aldehydes and methyl-ketones
synthesis
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production of chiral ferrocene derivatives as ligands in asymmetric catalysis, to bioelectrochemistry and development of new pharmaceuticals against malaria
synthesis
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crude cell lysate containing a hydroxynitrile lyase can be used for the enantioselective synthesis of several cyanohydrins in a microchannel. These enzymatic reactions show a high initial reaction rate and enantioselectivity, which in a batchwise process can only be achieved by vigorous stirring
synthesis
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recombinant Pichia pastoris strains are constructed which simultaneously express the (S)-oxynitrilase of Manihot esculenta and the arylacetonitrilase of Pseudomonas fluorescens EBC191 each under the control of individual AOX1 promoters in order to obtain a whole cell catalyst for the synthesis of (S)-mandelic acid from benzaldehyde and cyanideproduction of optically active cyanohydrin compounds
synthesis
synthesis of enantiopure (S)-3-phenoxybenzaldehyde cyanohydrin (a useful intermediate in the pyrethroid synthesis) by applying a high pH two-phase system to reduce nonenzymatic reaction
synthesis
synthesis of optically active cyanohydrins that are interesting intermediates for the synthesis of alpha-hydroxy acids, alpha-hydroxy ketones, or beta-ethanolamines, all of which are important building blocks in organic synthesis
synthesis
the cyanohydrin reaction of formylferrocene catalysed by the hydroxynitrile lyase from Hevea brasiliensis provides an access to chiral ferrocene derivatives in high enantiomeric excess. Since cyanohydrins are versatile synthetic intermediates, the possibility for many preparative transformations is opened. This synthetic potential is enlarged even further with the transformation of 1,1'-diformylferrocene leading to biscyanohydrins
synthesis
the enzyme is a potent biocatalyst for the industrial production of chemicals
synthesis
the enzyme is a valuable catalysts for the synthesis of cyanohydrins, which are versatile chiral building blocks in the pharmaceutical and agrochemical industries
synthesis
hydroxynitrile lyase is a useful enzyme for production of optically active cyanohydrin compounds
synthesis
synthesis of pure 2-hydroxycarboxylic acids as valuable synthetic building blocks. Development of bienzymatic cascades to convert aldehydes, via hydrocyanation and subsequent hydration or hydrolysis, into the corresponding (S)-2-hydroxycarboxylic amides and acids. The biocatalysts comprise an (S)-specific hydroxynitrile lyase combined with a nonselective nitrile hydratase or nitrilase. The key to success is preventing racemisation of the intermediate (S)-2-hydroxynitrile while adequately protecting the nitrile-converting enzyme, either in a cross-linked enzyme aggregate (CLEA) or in resting cells.Two biocatalyst systems for the synthesis of (S)-mandelic acid are developed: a combined cross-linked enzyme aggregate (combi-CLEA) of an (S)-hydroxynitrile lyase and a nitrilase, as well as a whole-cell Escherichia coli biocatalyst expressing both enzymes. The nitrilase formed large amounts of mandelicamide, which was remedied by including an amidase in the combi-CLEA as well as by using nitrilasevariants obtained by directed mutagenesis in the whole-cell biocatalyst. Excellent results with more than 95% conversion of benzaldehyde into (S)-mandelic acid with near-quantitative enantiomeric purity are obtained with both biocatalyst systems. Directed mutagenesis of the nitrilase provides an amide-selective whole-cell biocatalyst, which produces (S)-mandelic amide in near-stoichiometric yields. (S)-2-hydroxylalkanoic carboxamides are synthesised in the presence of CLEAs of hydroxynitrile lyase and nitrile hydratase
synthesis
use of biocatalytic active static emulsions (BASE) for the hydroxynitrile lyase-catalyzed synthesis of enantiopure cyanohydrins. With this technique a full suppression of the undesired racemic non-enzymatic side reaction is facilitated, even at unusually high pH within the aqueous phase. BASE is an inclusion immobilization. It consists of a hydrophobic matrix, typically polydimethylsiloxane (PDMS), with dispersed domains of an aqueous phase