The enzyme contains Zn2+ . The enzyme catalyses the stereoselective synthesis of aliphatic (R)-cyanohydrins . No activity towards mandelonitrile and 4-hydroxymandelonitrile . Natural substrates for the (R)-oxynitrilase from Linum usitatissimum are acetone and butan-2-one, which are the building blocks of the cyanogen glycosides in Linum, linamarin and lotaustralin, or linustatin and neolinustatin, respectively .
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The enzyme appears in viruses and cellular organisms
The enzyme contains Zn2+ [1]. The enzyme catalyses the stereoselective synthesis of aliphatic (R)-cyanohydrins [1]. No activity towards mandelonitrile and 4-hydroxymandelonitrile [5]. Natural substrates for the (R)-oxynitrilase from Linum usitatissimum are acetone and butan-2-one, which are the building blocks of the cyanogen glycosides in Linum, linamarin and lotaustralin, or linustatin and neolinustatin, respectively [4].
enantioselective transcyanation. Under optimum conditions, both acetyltrimethylsilane conversion to (R)-2-trimethylsilyl-2-hydroxy-ethylcyanide and enantiomeric excess of the product are above 99%. The silicon atom in acetyltrimethylsilane has a great effect on the eaction and both the substrate conversion and the product enantiomeric excess are much higher than those in its carbon counterpart 3,3-dimethyl-2-butanone
natural substrates for the (R)-oxynitrilase from Linum usitatissimum are acetone and butan-2-one, which are the building blocks of the cyanogen glycosides in Linum, linamarin and lotaustralin, or linustatin and neolinustatin, respectively
despite a short reaction time of 0.8 h, the conversion of methyl vinyl ketone results in a poor (38%) enantiomeric excess value. As in the same time there is almost no conversion without enzyme. This compound is one of the rare examples, where the enzyme exerts only a partial stereoselectivity for a defined substrate
natural substrates for the (R)-oxynitrilase from Linum usitatissimum are acetone and butan-2-one, which are the building blocks of the cyanogenic glycosides in Linum, linamarin and lotaustralin, or linustatin and neolinustatin, respectively
reaction with an immobilized form of the hydroxynitrile lyase as crosslinked enzyme aggregate with high specific activity and recovery on a preparative scale
synthesis of aromatic (S)-cyanohydrins. Most active towards derivatives of phenylacetone, converting 30-65% of the starting material to (S)-cyanohydrin with 55-95% enantiomeric excess in less than 1 day
the enzyme catalyzes the stereoselective synthesis of aliphatic (R)-cyanohydrins. Conversion of aromatic aldehydes (3-phenylpropionaldehyde or cinnamic aldehyde) and the aliphatic ketones is incomplete and gives poor enantiomeric excess-values, caused by the long reaction time
natural substrates for the (R)-oxynitrilase from Linum usitatissimum are acetone and butan-2-one, which are the building blocks of the cyanogenic glycosides in Linum, linamarin and lotaustralin, or linustatin and neolinustatin, respectively
natural substrates for the (R)-oxynitrilase from Linum usitatissimum are acetone and butan-2-one, which are the building blocks of the cyanogen glycosides in Linum, linamarin and lotaustralin, or linustatin and neolinustatin, respectively
LuHNL has significant homologies to members of the Zn2+-containing alcohol dehydrogenases. In particular, residues responsible for coordination of Zn2+ ions or fulfilling structural or functional tasks in Zn2+-alcohol dehydrogenases are conserved. Contains about 2-4 mol zinc per mol of recombinant enzyme. Hydroxynitrile lyase from Linum usitatissimum and Zn2+-alcohol dehydrogenases have similar structural requirements with respect to maintaining a catalytically active structure. Residues essentially involved in catalysis of Zn2+-ADHs are also of functional importance in hydroxynitrile lyase from Linum usitatissimum
development of an immobilized form of the hydroxynitrile lyase as crosslinked enzyme aggregate (CLEA) with high specific activity (303.5 U/g) and recovery (33%), 180.5 U/g LuCLEA (crosslinked enzyme aggregate) (using sat. (NH4)2SO4), 9.9 U/g LuEA (Enzyme aggregate of LuHNL) (using sat. (NH4)2SO4), 110.9 U/g LuCLEA (using tert-butanol), 221.9 U/g LuEA (using tert-butanol)
development of an immobilized form of the hydroxynitrile lyase as crosslinked enzyme aggregate (CLEA) with high specific activity (303.5 U/g) and recovery (33%), 180.5 U/g LuCLEA (crosslinked enzyme aggregate) (using sat. (NH4)2SO4), 9.9 U/g LuEA (Enzyme aggregate of LuHNL) (using sat. (NH4)2SO4), 110.9 U/g LuCLEA (using tert-butanol), 221.9 U/g LuEA (using tert-butanol)
cloning of a myc-His-tagged LuHNL-cDNA under control of the methanol-inducible AOX1 (alcohol oxidase) promotor of Pichia pastoris and introduction in the SMD1168 strain. Recombinant LuHNL is kinetically indistinguishable from the authentic flax enzyme
production of organosilicon compounds by enantioselective transcyanation. Under optimum conditions, both acetyltrimethylsilane conversion to (R)-2-trimethylsilyl-2-hydroxy-ethylcyanide and enantiomeric excess of the product are above 99%. the silicon atom in acetyltrimethylsilane has a great effect on the eaction and both the substrate conversion and the product enantiomeric excess are much higher than those in its carbon counterpart 3,3-dimethyl-2-butanone
Expression of the Zn2+-containing hydroxynitrile lyase from flax (Linum usitatissimum) in Pichia pastoris - utilization of the recombinant enzyme for enzymatic analysis and site-directed mutagenesis
Synthesis of optically active cyanohydrins from aromatic ketones: evidence of an increased substrate range and inverted stereoselectivity for the hydroxynitrile lyase from Linum usitatissimum