(R)-Mandelonitrile lyase
(R)-Mandelonitrile lyase structure
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Common Name | (R)-Mandelonitrile lyase | ||
|---|---|---|---|---|
| CAS Number | 9024-43-5 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Investigation of the microheterogeneity and aglycone specificity-conferring residues of black cherry prunasin hydrolases.
Plant Physiol. 129(3) , 1252-64, (2002) In black cherry (Prunus serotina Ehrh.) seed homogenates, (R)-amygdalin is degraded to HCN, benzaldehyde, and glucose by the sequential action of amygdalin hydrolase (AH), prunasin hydrolase (PH), and mandelonitrile lyase. Leaves are also highly cyanogenic be... |
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Catalytic mechanism of hydroxynitrile lyase from Hevea brasiliensis: a theoretical investigation.
J. Phys. Chem. B 114(29) , 9622-8, (2010) Density functional theory (DFT) calculations using the hybrid functional B3LYP have been performed to investigate the catalytic mechanism of hydroxynitrile lyase from Hevea brasiliensis (Hb-HNL). This enzyme catalyzes the cleavage of acetone cyanohydrin to hy... |
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(R)-oxynitrilase-catalysed synthesis of chiral silicon-containing aliphatic (R)-ketone-cyanohydrins.
Biotechnol. Lett. 25(3) , 219-22, (2003) Optically active 2-trimethylsilyl-2-hydroxyl-ethylcyanide was prepared by enzymatic enantioselective transcyanation of acetyltrimethylsilane with acetone cyanohydrin in a biphasic system at 35 degrees C and pH 5. (R)-Oxynitrilase from apple seed meal was the ... |
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Synthesis of (R)-2-trimethylsilyl-2-hydroxyl-ethylcyanide catalyzed with (R)-oxynitrilase from loquat seed meal.
Biotechnol. Lett. 27(2) , 79-82, (2005) The synthesis of optically active (R)-2-trimethylsilyl-2-hydroxyl-ethylcyanide by asymmetric trans-cyanation of acetyltrimethylsilane with acetone cyanohydrin in a biphasic system was achieved using (R)-oxynitrilase from loquat seed meal. Diisopropyl ether wa... |
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Screening for new hydroxynitrilases from plants.
Biosci. Biotechnol. Biochem. 69 , 2349-57, (2005) We established a simple HPLC method to determine the activity and stereochemistry of the chiral mandelonitrile synthesized from benzaldehyde and cyanide, and applied it to screen for hydroxynitrile lyase (HNL) activity of plant origin. A total of 163 species ... |
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Conversion of sterically demanding α,α-disubstituted phenylacetonitriles by the arylacetonitrilase from Pseudomonas fluorescens EBC191.
Appl. Environ. Microbiol. 78 , 48 - 57, (2012) The nitrilase from Pseudomonas fluorescens EBC191 converted 2-methyl-2-phenylpropionitrile, which contains a quaternary carbon atom in the α-position toward the nitrile group, and also similar sterically demanding substrates, such as 2-hydroxy-2-phenylpropion... |
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Simultaneous expression of an arylacetonitrilase from Pseudomonas fluorescens and a (S)-oxynitrilase from Manihot esculenta in Pichia pastoris for the synthesis of (S)-mandelic acid.
Appl. Microbiol. Biotechnol. 80(1) , 87-97, (2008) The arylacetonitrilase of Pseudomonas fluorescens EBC191 catalyzes the conversion of (S)-mandelonitrile to (S)-mandelic acid and (S)-mandeloamide. This biotransformation is optimally performed under acidic pH values because (S)-mandelonitrile rapidly decompos... |
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Cross-linked aggregates of (R)-oxynitrilase: a stable, recyclable biocatalyst for enantioselective hydrocyanation.
Org. Lett. 7(2) , 327-9, (2005) [Reaction: see text] The (R)-oxynitrilase from almonds was immobilized as a cross-linked enzyme aggregate (CLEA) via precipitation with 1,2-dimethoxyethane and subsequent cross-linking using glutaraldehyde. The resulting preparation was a highly effective hyd... |
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Biochemical and structural characterization of a novel bacterial manganese-dependent hydroxynitrile lyase.
FEBS J. 280(22) , 5815-28, (2013) Hydroxynitrile lyases (HNLs), which catalyse the decomposition of cyanohydrins, are found mainly in plants. In vitro, they are able to catalyse the synthesis of enantiopure cyanohydrins, which are versatile building blocks in the chemical industry. Recently, ... |
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Cloning and expression of hydroxynitrile lyase gene from Eriobotrya japonica in Pichia pastoris.
J. Biosci. Bioeng. 112(4) , 321-5, (2011) Hydroxynitrile lyase gene (hnl) from Eriobotrya japonica was successfully amplified using the method of SEFA PCR (Self-Formed Adaptor PCR). The complete sequence was 5.5 kbp in length, including 3100 bp of the upstream promoter region, 1659 bp of the coding s... |