A new (R)-hydroxynitrile lyase from Prunus mume: asymmetric synthesis of cyanohydrins

Nanda, Samik; Kato, Yasuo; Asano, Yasuhisa

doi:10.1016/j.tet.2005.08.105

Cited by 76 publications

(42 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Because millipedes exude defensive secretions of aromatic compounds, such as mandelonitrile and benzaldehyde (19), millipede HNLs seem likely to have substrate specificity toward aromatic compounds. Thus, we sought to synthesize cyanohydrins using ChuaHNL in a citrate buffer, using the aromatic aldehydes in our chemical library (26,27) as starting materials, and evaluated the chiral configuration and ee, which are important indices for fine chemical syntheses. ChuaHNL catalyzed the synthesis of cyanohydrins from monosubstituted, disubstituted, biphenyl, heteroaromatic, and bicyclic aldehydes with an almost exclusive R configuration and an ee range of 7.5-90% (Table S2).…”

Section: Substrate Specificity and Kinetic Studies In The Synthesis Omentioning

confidence: 99%

“…Overall, ChuaHNL displayed wide substrate specificity in cyanohydrin synthesis in an aqueous system at a mild temperature (22°C) and was shown to be a potent biocatalyst. Although other HNLs from almond or Japanese apricot showed a wide substrate spectrum, they required biphasic systems containing organic solvents (13,26).…”

Section: Substrate Specificity and Kinetic Studies In The Synthesis Omentioning

confidence: 99%

See 1 more Smart Citation

Discovery and molecular and biocatalytic properties of hydroxynitrile lyase from an invasive millipede,Chamberlinius hualienensis

Dadashipour

Ishida

Yamamoto

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

100

View full text Add to dashboard Cite

Hydroxynitrile lyase (HNL) catalyzes the degradation of cyanohydrins and causes the release of hydrogen cyanide (cyanogenesis). HNL can enantioselectively produce cyanohydrins, which are valuable building blocks for the synthesis of fine chemicals and pharmaceuticals, and is used as an important biocatalyst in industrial biotechnology. Currently, HNLs are isolated from plants and bacteria. Because industrial biotechnology requires more efficient and stable enzymes for sustainable development, we must continuously explore other potential enzyme sources for the desired HNLs. Despite the abundance of cyanogenic millipedes in the world, there has been no precise study of the HNLs from these arthropods. Here we report the isolation of HNL from the cyanide-emitting invasive millipede Chamberlinius hualienensis, along with its molecular properties and application in biocatalysis. The purified enzyme displays a very high specific activity in the synthesis of mandelonitrile. It is a glycosylated homodimer protein and shows no apparent sequence identity or homology with proteins in the known databases. It shows biocatalytic activity for the condensation of various aromatic aldehydes with potassium cyanide to produce cyanohydrins and has high stability over a wide range of temperatures and pH values. It catalyzes the synthesis of (R)-mandelonitrile from benzaldehyde with a 99% enantiomeric excess, without using any organic solvents. Arthropod fauna comprise 80% of terrestrial animals. We propose that these animals can be valuable resources for exploring not only HNLs but also diverse, efficient, and stable biocatalysts in industrial biotechnology.millipede hydroxynitrile lyase | bioresource exploration | biocatalysis | white biotechnology | arthropod

show abstract

Section: Substrate Specificity and Kinetic Studies In The Synthesis Omentioning

confidence: 99%

Section: Substrate Specificity and Kinetic Studies In The Synthesis Omentioning

confidence: 99%

Discovery and molecular and biocatalytic properties of hydroxynitrile lyase from an invasive millipede,Chamberlinius hualienensis

Dadashipour

Ishida

Yamamoto

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

100

View full text Add to dashboard Cite

show abstract

“…This new enzyme accepts a broad array of substrates, ranging from aromatic, heteroaromatic, of bicyclic to aliphatic carbonyl compounds, and it yields the corresponding cyanohydrins with excellent enantioselection. 27,28) Optically active cyanohydrins are building blocks for the total synthesis of several biologically active natural products. 29) If PmHNL can be prepared in sufficient amounts by the gene expressed in microbial hosts, it should be useful in the production of chiral synthetic, with potential for asymmetric synthesis.…”

mentioning

confidence: 99%

Characterization of a New (R)-Hydroxynitrile Lyase from the Japanese ApricotPrunus mumeand cDNA Cloning and Secretory Expression of One of the Isozymes inPichia pastoris

Fukuta

Nanda

Kato

et al. 2011

Bioscience, Biotechnology, and Biochemistry

Self Cite

View full text Add to dashboard Cite

“…Synthetic approach towards (R)-enantioenriched 2-hydroxy-2-methylbutyric acid (R)-I. [18,19] while the Linum usitatissimum HNL (LuHNL) was reported to give good to very good enantiopurities of the cyanohydrin intermediate. [20,21] We recently described that immobilizing the HNLs from Prunus amygdalus, Hevea brasiliensis and Manihot esculenta as cross-linked enzyme aggregates (CLEAs) can improve their stability and ease their recycling.…”

Section: Introductionmentioning

confidence: 99%

Linum usitatissimum Hydroxynitrile Lyase Cross‐Linked Enzyme Aggregates: A Recyclable Enantioselective Catalyst

et al. 2008

View full text Add to dashboard Cite

An immobilized form of the hydroxynitrile lyase from Linum usitatissimum (LuHNL) as crosslinked enzyme aggregate (CLEA) with high specific activity (303.5 U/g) and recovery (33%) was developed. Molecular imprinting using 2-butanone as additive in the immobilization process improved the synthetic activity of the biocatalyst. LuCLEA could be partially recycled for the synthesis of (R)-2-butanone cyanohydrin on a preparative scale over two batches. The enantioenriched cyanohydrin obtained was further hydrolyzed to give (R)-2-hydroxy-2-methylbutyric acid in 85% yield (from 2-butanone) and 87% ee.

show abstract

A new (R)-hydroxynitrile lyase from Prunus mume: asymmetric synthesis of cyanohydrins

Cited by 76 publications

References 50 publications

Discovery and molecular and biocatalytic properties of hydroxynitrile lyase from an invasive millipede,Chamberlinius hualienensis

Discovery and molecular and biocatalytic properties of hydroxynitrile lyase from an invasive millipede,Chamberlinius hualienensis

Characterization of a New (R)-Hydroxynitrile Lyase from the Japanese ApricotPrunus mumeand cDNA Cloning and Secretory Expression of One of the Isozymes inPichia pastoris

Linum usitatissimum Hydroxynitrile Lyase Cross‐Linked Enzyme Aggregates: A Recyclable Enantioselective Catalyst

Contact Info

Product

Resources

About