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Information on EC 4.1.2.10 - (R)-mandelonitrile lyase
for references in articles please use BRENDA:EC4.1.2.10
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IUBMB Comments
A variety of enzymes from different sources and with different properties. Some are flavoproteins, others are not. Active towards a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 4.1.2.10
- cyanohydrin
- prunus
- synthesis
- hcn
- cherry
-
enantioselective
- serotina
- lyases
-
r-mandelonitrile
-
enantiomeric
- amygdalus
-
diisopropyl
- prunasin
-
cyanogenesis
- hbhnl
-
hydrocyanic
-
hevea
-
s-selective
- pharmacology
- agriculture
showSynonyms
mandelonitrile lyase, athnl, (r)-oxynitrilase, (r)-(+)-mandelonitrile lyase, pahnl5, r-selective hnl, pahnl1, aphnl, (r)-hydroxynitrile lyase, pmhnl, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-(+)-Mandelonitrile lyase
(R)-HNL
(R)-hydroxynitrile lyase
(R)-Mandelonitrile lyase
(R)-Oxynitrilase
AciX9_0562
cupin 2 conserved barrel domain protein
D-alpha-hydroxynitrile lyase
-
-
-
-
D-Hydroxynitrile lyase
-
-
-
-
D-Oxynitrilase
-
-
-
-
EjHNL
HNL
HNL1
HNL2
HNL5
Hydroxynitrile lyase
hydroynitrile lyase
Lyase, mandelonitrile
-
-
-
-
MDL
-
-
-
-
Oxynitrilase
PaHNL
PaHNL5
PhaMDL
R-selective HNL
R-selective hydroxynitrile lyase
(R)-(+)-Mandelonitrile lyase
-
-
-
-
(R)-Mandelonitrile lyase
-
-
-
-
(R)-Oxynitrilase
-
-
-
-
Hydroxynitrile lyase
-
-
-
-
Oxynitrilase
-
-
-
-
PhaMDL
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-mandelonitrile = cyanide + benzaldehyde
based on the binding geometry, a reaction mechanism is proposed that involves one of the two conserved active site histidine residues acting as a general base abstracting the proton from the cyanohydrin hydroxyl group. Site-directed mutagenesis shows that both active site histidines are required for the reaction to occur
(R)-mandelonitrile = cyanide + benzaldehyde
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyanohydrin formation
cyanohydrin formation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
amygdalin and prunasin degradation, vicianin bioactivation
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SYSTEMATIC NAME
IUBMB Comments
(R)-mandelonitrile benzaldehyde-lyase (cyanide-forming)
A variety of enzymes from different sources and with different properties. Some are flavoproteins, others are not. Active towards a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
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CAS REGISTRY NUMBER
COMMENTARY
9024-43-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-4-hydroxymandelonitrile
cyanide + 4-hydroxybenzaldehyde
-
Substrates: -
Products: -
Products: -
r
2-chlorobenzaldehyde + HCN
(R)-2-chloromandelonitrile
-
Substrates: -
Products: after 96 h, 100% yield, 21% enantiomeric excess
Products: after 96 h, 100% yield, 21% enantiomeric excess
?
2-chlorobenzaldehyde + nitromethane
1-(2-chlorophenyl)-2-nitroethanol
Substrates: -
Products: 34% yield after 2 h
Products: 34% yield after 2 h
?
2-heptanone + HCN
(R)-2-heptanone cyanohydrin
-
Substrates: needs long reaction time (26 h), providing low enantiomeric exess (14%), which supports the fact that methyl ketones of long aliphatic chain are poor substrates
Products: -
Products: -
?
2-methoxybenzaldehyde + nitromethane
1-(2-methoxyphenyl)-2-nitroethanol
Substrates: -
Products: 13% yield after 2 h
Products: 13% yield after 2 h
?
2-methylbenzaldehyde + nitromethane
1-(2-methylphenyl)-2-nitroethanol
Substrates: -
Products: 12% yield after 2 h
Products: 12% yield after 2 h
?
3,4-dihydroxybenzaldehyde + HCN
(R)-3,4-dihydroxymandelonitrile
-
Substrates: -
Products: after 96 h, 100% yield, 99% enantiomeric excess
Products: after 96 h, 100% yield, 99% enantiomeric excess
?
3-(2-naphthyl)benzaldehyde + nitromethane
(1R)-1-[3-(naphthalen-2-yl)phenyl]-2-nitroethanol
Substrates: -
Products: 7% yield after 2 h
Products: 7% yield after 2 h
?
3-chlorobenzaldehyde + nitromethane
1-(3-chlorophenyl)-2-nitroethanol
Substrates: -
Products: 17% yield after 2 h
Products: 17% yield after 2 h
?
3-methoxybenzaldehyde + nitromethane
1-(3-methoxyphenyl)-2-nitroethanol
Substrates: -
Products: 17% yield after 2 h
Products: 17% yield after 2 h
?
3-methylbenzaldehyde + nitromethane
1-(3-methylphenyl)-2-nitroethanol
Substrates: -
Products: 12% yield after 2 h
Products: 12% yield after 2 h
?
3-phenylpropionaldehyde + HCN
(R)-2-hydroxy-4-phenylbutyronitrile
-
Substrates: -
Products: after 96 h, 83% yield, 91% enantiomeric excess
Products: after 96 h, 83% yield, 91% enantiomeric excess
?
4-bromobenzaldehyde + HCN
(R)-4-bromomandelonitrile
-
Substrates: -
Products: after 96 h, 100% yield, 99% enantiomeric excess
Products: after 96 h, 100% yield, 99% enantiomeric excess
?
4-bromobenzaldehyde + nitromethane
1-(4-bromophenyl)-2-nitroethanol
Substrates: -
Products: 20% yield after 2 h
Products: 20% yield after 2 h
?
4-chlorobenzaldehyde + nitromethane
1-(4-chlorophenyl)-2-nitroethanol
Substrates: -
Products: 9% yield after 2 h
Products: 9% yield after 2 h
?
4-fluorobenzaldehyde + HCN
(R)-4-fluoromandelonitrile
-
Substrates: -
Products: after 96 h, 100% yield, 72% enantiomeric excess
Products: after 96 h, 100% yield, 72% enantiomeric excess
?
4-fluorobenzaldehyde + nitromethane
1-(4-fluorophenyl)-2-nitroethanol
Substrates: -
Products: 9% yield after 2 h
Products: 9% yield after 2 h
?
4-methoxybenzaldehyde + nitromethane
1-(4-methoxyphenyl)-2-nitroethanol
Substrates: -
Products: 2% yield after 2 h
Products: 2% yield after 2 h
?
4-methylbenzaldehyde + nitromethane
1-(4-methylphenyl)-2-nitroethanol
Substrates: -
Products: 11% yield after 2 h
Products: 11% yield after 2 h
?
4-nitrobenzaldehyde + HCN
(R)-4-nitromandelonitrile
-
Substrates: -
Products: after 96 h, 100% yield, 14% enantiomeric excess
Products: after 96 h, 100% yield, 14% enantiomeric excess
?
acetyltrimethylsilane + acetone cyanohydrin
?
-
Substrates: both acetyltrimethylsilane conversion and enantiomeric excess of the product are above 99%
Products: -
Products: -
?
benzaldehyde + HCN
(R)-mandelonitrile
-
Substrates: -
Products: after 96 h, 100% yield, 99% enantiomeric excess
Products: after 96 h, 100% yield, 99% enantiomeric excess
?
benzaldehyde + nitromethane
(R)-2-nitro-1-phenylethanol
Substrates: -
Products: 30% yield after 2 h
Products: 30% yield after 2 h
?
cyanide + (2E)-3-methylpent-2-enal
(2R,3E)-2-hydroxy-4-methylhex-3-enenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + (2E)-hex-2-enal
(2R,3E)-2-hydroxyhept-3-enenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + (2E)-hex-2-enal
(3E)-2-hydroxyhept-3-enenitrile
Substrates: -
Products: 53% enantiomeric excess
Products: 53% enantiomeric excess
?
cyanide + (2E,4E)-hexa-2,4-dienal
(2R,3E,5E)-2-hydroxyhepta-3,5-dienenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + (4R)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde
(2S)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile + (2R)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
Substrates: -
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4R)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde is converted to 47.1% (2S)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 52.9% (2R)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4R)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde is converted to 47.1% (2S)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 52.9% (2R)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
?
cyanide + (4R,5S)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde
(2S)-hydroxy-[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile + (2R)-hydroxy-[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
-
Substrates: -
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4R,5S)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde is converted to 34.2% (2S)-hydroxy[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile and 65.8% (2R)-hydroxy[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4R,5S)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde is converted to 34.2% (2S)-hydroxy[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile and 65.8% (2R)-hydroxy[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
?
cyanide + (4R,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde
(2S)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile + (2R)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
Substrates: -
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4R,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde is converted to 48.2% (2S)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 51.8% (2R)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4R,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde is converted to 48.2% (2S)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 51.8% (2R)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
?
cyanide + (4S)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde
(2S)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile + (2R)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
Substrates: -
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4S)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde is converted to 66.4% (2S)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 33.6% (2R)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4S)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde is converted to 66.4% (2S)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 33.6% (2R)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
?
cyanide + (4S,5R)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde
(2S)-hydroxy-[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile + (2R)-hydroxy-[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
-
Substrates: -
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4S,5R)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde is converted to 52.6% (2S)-hydroxy[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile and 47.4% (2R)-hydroxy[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4S,5R)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde is converted to 52.6% (2S)-hydroxy[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile and 47.4% (2R)-hydroxy[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
?
cyanide + (4S,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde
(2S)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile + (2R)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
Substrates: -
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4S,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde is converted to 49.3% (2S)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 50.7% (2R)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4S,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde is converted to 49.3% (2S)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 50.7% (2R)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
?
cyanide + (benzyloxy)acetaldehyde
(2R)-3-(benzyloxy)-2-hydroxypropanenitrile + (2S)-3-(benzyloxy)-2-hydroxypropanenitrile
-
Substrates: -
Products: 43.9% (2S)-3-(benzyloxy)-2-hydroxypropanenitrile and 53.1% (2S)-3-(benzyloxy)-2-hydroxypropanenitrile
Products: 43.9% (2S)-3-(benzyloxy)-2-hydroxypropanenitrile and 53.1% (2S)-3-(benzyloxy)-2-hydroxypropanenitrile
?
cyanide + (naphthalen-1-yloxy)acetaldehyde
(2S)-2-hydroxy-3-(naphthalen-1-yloxy)propanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + (R)-4-methylsulfanylbenzaldehyde
(R)-4-methylsulfanyl-mandelonitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 1,3-benzodioxol-5-ylacetaldehyde
(2R)-1,3-benzodioxol-5-yl(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 1,3-benzodioxole-5-carbaldehyde
(2R)-1,3-benzodioxol-5-yl(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 1,4-dioxaspiro[4.5]decane-2-carbaldehyde
(S)-2-hydroxy-2-((R)-1,4-dioxaspiro[4.5]decan-2-yl)acetonitrile + (R)-2-hydroxy-2-((R)-1,4-dioxaspiro[4.5]decan-2-yl)acetonitrile + (S)-2-hydroxy-2-((S)-1,4-dioxaspiro[4.5]decan-2-yl)acetonitrile + (R)-2-hydroxy-2-((S)-1,4-dioxaspiro[4.5]decan-2-yl)acetonitrile
-
Substrates: -
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate 1,4-dioxaspiro[4.5]decane-2-carbaldehyde is converted to 21.8% (2S)-(2R)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile, 28.3% (2R)-(2R)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile, 30.3% (2S)-(2S)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile and 19.6% (2R)-(2S)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate 1,4-dioxaspiro[4.5]decane-2-carbaldehyde is converted to 21.8% (2S)-(2R)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile, 28.3% (2R)-(2R)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile, 30.3% (2S)-(2S)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile and 19.6% (2R)-(2S)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile
?
cyanide + 1-naphthaldehyde
(2R)-hydroxy-2-(naphthalen-1-yl)acetonitrile
Substrates: 30.3% conversion and 16.4% enantiomeric excess after 30 min incubation
Products: -
Products: -
?
cyanide + 1-naphthaldehyde
?
-
Substrates: 88% ee of the product
Products: -
Products: -
?
cyanide + 1-phenylethanone
2-hydroxy-2-phenylpropanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 2,2-dimethyl-3-phenoxypropanal
(2R)-2-hydroxy-3,3-dimethyl-4-phenoxybutanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 2,2-dimethyl-4H-1,3-benzodioxine-6-carbaldehyde
(2R)-(2,2-dimethyl-4H-1,3-benzodioxin-6-yl)(hydroxy)ethanenitrile
Substrates: 8.5% conversion assayed by 2-aminobenzamidoxime cycling method, 0.39% conversion assayed by chiral gas chromatography
Products: -
Products: -
?
cyanide + 2,3,4a,8a-tetrahydro-1,4-benzodioxine-6-carbaldehyde
(2R)-hydroxy(2,3,4a,8a-tetrahydro-1,4-benzodioxin-6-yl)acetonitrile
-
Substrates: isoenzyme HNL5
Products: -
Products: -
?
cyanide + 2-(benzyloxy)-3-phenylpropanal
(2S,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile + (2R,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile + (2S,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile + (2R,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile
-
Substrates: -
Products: 26.9% (2S,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile, 23.4% (2R,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile, 29.2% (2S,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile and 20.6% (2R,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile
Products: 26.9% (2S,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile, 23.4% (2R,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile, 29.2% (2S,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile and 20.6% (2R,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile
?
cyanide + 2-(benzyloxy)propanal
(2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile + (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile + (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile + (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile
-
Substrates: -
Products: 45.4% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile, 8.1% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile, 33.3% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile and 13.3% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile
Products: 45.4% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile, 8.1% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile, 33.3% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile and 13.3% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile
?
cyanide + 2-(naphthalen-2-yl)propanal
(2S,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile + (2S,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile + (2R,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile + (2R,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile
-
Substrates: -
Products: 30.4% (2S,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile, 24.0% (2S,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile, 20.0% (2R,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile and 25.6% (2R,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile
Products: 30.4% (2S,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile, 24.0% (2S,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile, 20.0% (2R,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile and 25.6% (2R,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile
?
cyanide + 2-bromobenzaldehyde
(2R)-(2-bromophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: 98% enantiomeric excess
Products: 98% enantiomeric excess
?
cyanide + 2-bromobenzaldehyde
(R)-2-bromomandelonitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 2-chlorobenzaldehyde
(2R)-2-(2-chlorophenyl)-2-hydroxyacetonitrile
Substrates: -
Products: -
Products: -
?
cyanide + 2-fluorobenzaldehyde
(2R)-(2-fluorophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: 99% enantiomeric excess
Products: 99% enantiomeric excess
?
cyanide + 2-fluorobenzaldehyde
(R)-2-fluoromandelonitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 2-furanaldehyde
(R)-2-furanmandelonitrile
Substrates: 52.4% conversion and 90.3% enantiomeric excess after 30 min incubation
Products: -
Products: -
?
cyanide + 2-iodobenzaldehyde
(2R)-(2-iodophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: more than 95% enantiomeric excess
Products: more than 95% enantiomeric excess
?
cyanide + 2-methoxy-3-phenylpropanal
(2S,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile + (2R,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile + (2S,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile + (2R,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile
-
Substrates: -
Products: 43.1% (2S,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile, 8.4 (2R,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile, 40.1% (2S,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile and 8.4% (2R,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile
Products: 43.1% (2S,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile, 8.4 (2R,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile, 40.1% (2S,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile and 8.4% (2R,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile
?
cyanide + 2-methoxybenzaldehyde
(R)-2-hydroxy-2-(2-methoxyphenyl)acetonitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 2-methoxybenzaldehyde
(R)-2-methoxymandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 2-methylbenzaldehyde
(R)-2-hydroxy-2-(2-methylphenyl)acetonitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 2-methylpropanal
(2R)-2-hydroxy-3-methylbutanenitrile
-
Substrates: activity is 67% of the activity with benzaldehyde
Products: 13% enentiomeric excess
Products: 13% enentiomeric excess
?
cyanide + 2-naphthaldehyde
(2R)-hydroxy-2-(naphthalen-2-yl)acetonitrile
Substrates: -
Products: -
Products: -
?
cyanide + 2-naphthaldehyde
(R)-2-hydroxy-2-(naphthalen-2-yl)acetonitrile
Substrates: -
Products: -
Products: -
?
cyanide + 2-naphthaldehyde
?
-
Substrates: 90% ee of the product
Products: -
Products: -
?
cyanide + 2-nitrobenzaldehyde
(R)-2-nitromandelonitrile
-
Substrates: lowest conversion
Products: -
Products: -
?
cyanide + 2-phenylpropanal
(2R,3S)-2-hydroxy-3-phenylbutanenitrile + (2S,3R)-2-hydroxy-3-phenylbutanenitrile + (2R,3R)-2-hydroxy-3-phenylbutanenitrile
-
Substrates: -
Products: 3.0% (2S,3S)-2-hydroxy-3-phenylbutanenitrile, 51.8% (2R,3S)-2-hydroxy-3-phenylbutanenitrile, 27.6% (2S,3R)-2-hydroxy-3-phenylbutanenitrile and + 17.6% (2R,3R)-2-hydroxy-3-phenylbutanenitrile
Products: 3.0% (2S,3S)-2-hydroxy-3-phenylbutanenitrile, 51.8% (2R,3S)-2-hydroxy-3-phenylbutanenitrile, 27.6% (2S,3R)-2-hydroxy-3-phenylbutanenitrile and + 17.6% (2R,3R)-2-hydroxy-3-phenylbutanenitrile
?
cyanide + 2-thiophenecarboxaldehyde
?
Substrates: -
Products: -
Products: -
?
cyanide + 3,4-dihydro-1H-isochromene-3-carbaldehyde
(S)-2-hydroxy-2-((S)-isochroman-3-yl)acetonitrile + (S)-2-hydroxy-2-((R)-isochroman-3-yl)acetonitrile + (R)-2-hydroxy-2-((S)-isochroman-3-yl)acetonitrile + (R)-2-hydroxy-2-((R)-isochroman-3-yl)acetonitrile
-
Substrates: -
Products: 28.6% (2S)-(3S)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile, 21.5% (2R)-(3S)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile, 28.7% (2S)-(3R)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile and 21.1% (2R)-(3R)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile
Products: 28.6% (2S)-(3S)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile, 21.5% (2R)-(3S)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile, 28.7% (2S)-(3R)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile and 21.1% (2R)-(3R)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile
?
cyanide + 3,4-dihydroxybenzaldehyde
(R)-3,4-dihydroxymandelonitrile
-
Substrates: -
Products: -
Products: -
?, r
cyanide + 3,4-dimethoxybenzaldehyde
(2R)-(3,4-dimethoxyphenyl)(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-bromobenzaldehyde
(2R)-(3-bromophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: 95% enantiomeric excess
Products: 95% enantiomeric excess
?
cyanide + 3-chloro-2,2-dimethylpropanal
(2R)-4-chloro-2-hydroxy-3,3-dimethylbutanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-fluorobenzaldehyde
(2R)-(3-fluorophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
?
cyanide + 3-hydroxy-2,2-dimethylpropanal
(2R)-2,4-dihydroxy-3,3-dimethylbutanenitrile
Substrates: 4.2% conversion assayed by 2-aminobenzamidoxime cycling method, 0.2% conversion assayed by chiral gas chromatography
Products: -
Products: -
?
cyanide + 3-hydroxy-2,2-dimethylpropanal
(2R)-2,5-dihydroxy-3,3-dimethylpentanenitrile
-
Substrates: i.e. hydroxypivaldehyde
Products: best enantiomeric excess is obtained at pH 2.5
Products: best enantiomeric excess is obtained at pH 2.5
?
cyanide + 3-iodobenzaldehyde
(2R)-(3-iodophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: 93% enantiomeric excess
Products: 93% enantiomeric excess
?
cyanide + 3-methoxy-2,2-dimethylpropanal
(2R)-2-hydroxy-4-methoxy-3,3-dimethylbutanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-methoxy-3-phenylpropanal
(2S,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile + (2R,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile + (2S,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile + (2R,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile
-
Substrates: -
Products: 6.5% (2S,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile, 45.2% (2R,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile, 14.0% (2S,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile, 34.3% (2R,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile
Products: 6.5% (2S,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile, 45.2% (2R,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile, 14.0% (2S,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile, 34.3% (2R,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile
?
cyanide + 3-methoxybenzaldehyde
(2R)-(3-methoxyphenyl)(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-methylbenzaldehyde
(2R)-(3-methylphenyl)(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-methylbutanal
(2R)-2-hydroxy-4-methylpentanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-phenoxybenzaldehyde
(2R)-2-hydroxy-2-(3-phenoxyphenyl)acetonitrile
Substrates: -
Products: more than 95% enantiomeric excess
Products: more than 95% enantiomeric excess
?
cyanide + 3-phenoxybenzaldehyde
(2R)-hydroxy(3-phenoxyphenyl)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-phenoxybenzaldehyde
(R)-2-hydroxy-2-(3-phenoxy-phenyl)-acetonitrile
-
Substrates: synthesis of (R)-2-hydroxy-2-(3-phenoxyphenyl)-acetonitrile with 93% enantiomeric excess
Products: -
Products: -
?
cyanide + 3-phenoxybenzaldehyde
(R)-3-phenoxymandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 3-phenoxypropanal
(2R)-2-hydroxy-5-phenylpentanenitrile
-
Substrates: -
Products: 74.3% (2R)-2-hydroxy-5-phenylpentanenitrile and 25.7% (2S)-2-hydroxy-5-phenylpentanenitrile
Products: 74.3% (2R)-2-hydroxy-5-phenylpentanenitrile and 25.7% (2S)-2-hydroxy-5-phenylpentanenitrile
?
cyanide + 3-phenylprop-2-enal
(2R)-2-hydroxy-4-phenylbut-3-enenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-phenylpropanal
(R)-2-hydroxy-4-phenylbutyronitrile
-
Substrates: isoenzyme HNL5
Products: -
Products: -
?
cyanide + 3-phenylpropionaldehyde
(R)-2-hydroxy-4-phenyl butyronitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 3-tetrahydrothiophenone
(S)-3-hydroxytetrahydrothiophene-3-carbonitrile
-
Substrates: the enzyme, that shows (R)-stereospecificity for its natural substrate shows S-stereselectivity with the heterocyclic ketone as substrate
Products: -
Products: -
?
cyanide + 4-(methylsulfanyl)benzaldehyde
(2R)-hydroxy[4-(methylsulfanyl)phenyl]ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 4-anisaldehyde
(R)-2-hydroxy-2-(4-methoxyphenyl)acetonitrile
-
Substrates: 99% ee of the product
Products: -
Products: -
?
cyanide + 4-bromoacetophenone
4-bromo-2-hydroxyphenylpropionitrile
-
Substrates: (R)-cyanohydrin is formed with 5% yield and 99% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
Products: -
Products: -
r
cyanide + 4-bromobenzaldehyde
(R)-4-bromomandelonitrile
-
Substrates: 99% ee of the product
Products: -
Products: -
?
cyanide + 4-chloroacetophenone
4-chloro-2-hydroxyphenylpropionitrile
-
Substrates: (R)-cyanohydrin is formed with 11% yield and 95% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
Products: -
Products: -
r
cyanide + 4-chlorobenzaldehyde
(2R)-(4-chlorophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
?
cyanide + 4-chlorobenzaldehyde
(R)-4-chloromandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 4-fluoroacetophenone
4-fluoro-2-hydroxyphenylpropionitrile
-
Substrates: (R)-cyanohydrin is formed with 20% yield and 84% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
Products: -
Products: -
r
cyanide + 4-fluorobenzaldehyde
(R)-4-fluoromandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 4-hydroxybenzaldehyde
(2R)-(4-hydroxyphenyl)(hydroxy)ethanenitrile
Substrates: -
Products: 97% enantiomeric excess
Products: 97% enantiomeric excess
?
cyanide + 4-hydroxybenzaldehyde
(2R)-hydroxy(4-hydroxyphenyl)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 4-hydroxybutanal
(R)-2,5-dihydroxypentanenitrile
-
Substrates: by varying the different reaction parameters it is possible to reduce the extension of the undesirable non-enzymatic competing reactions and optimize the optical purity of the cyanohydrin product. Best results are obtained at 15°C
Products: -
Products: -
?
cyanide + 4-iodoacetophenone
4-iodo-2-hydroxyphenylpropionitrile
-
Substrates: (R)-cyanohydrin is formed with 3% yield and 24% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
Products: -
Products: -
r
cyanide + 4-iodobenzaldehyde
(2R)-(4-iodophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: 92% enantiomeric excess
Products: 92% enantiomeric excess
?
cyanide + 4-methyl benzaldehyde
(2R)-(4-methylphenyl)(hydroxy)ethanenitrile
-
Substrates: (R)-cyanohydrin is formed with 85% yield and 79% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
Products: -
Products: -
r
cyanide + 4-phenylbutan-2-one
2-hydroxy-4-phenylbutyronitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 4-phenylbutanal
(2R)-2-hydroxy-5-phenylpentanenitrile
-
Substrates: -
Products: 88.9% (2R)-2-hydroxy-5-phenylpentanenitrile and 11.1% (2S)-2-hydroxy-5-phenylpentanenitrile
Products: 88.9% (2R)-2-hydroxy-5-phenylpentanenitrile and 11.1% (2S)-2-hydroxy-5-phenylpentanenitrile
?
cyanide + 5-hydroxypentanal
(R)-2,6-dihydroxyhexanenitrile
-
Substrates: by varying the different reaction parameters it is possible to reduce the extension of the undesirable non-enzymatic competing reaction and optimize the optical purity of the cyanohydrin product. Best results are obtained at 15°C
Products: -
Products: -
?
cyanide + 6-methylhept-5-en-2-one
(2R)-2-hydroxy-2,6-dimethylhept-5-enenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 7-ethyl-1-benzofuran-2-carbaldehyde
(2S)-(7-ethyl-1-benzofuran-2-yl)(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + acetophenone
(2R)-hydroxyphenylpropionitrile
-
Substrates: (R)-cyanohydrin is formed with 1% yield and 99% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
Products: -
Products: -
r
cyanide + cinnamaldehyde
(2R,3E)-2-hydroxy-4-phenylbut-3-enenitrile
-
Substrates: i.e. (2E)-3-phenylprop-2-enal
Products: -
Products: -
?
cyanide + cyclohexanecarbaldehyde
(2R)-cyclohexyl(hydroxy)acetonitrile
-
Substrates: activity is 41% of the activity with benzaldehyde
Products: 10% enentiomeric excess
Products: 10% enentiomeric excess
?
cyanide + cyclohexanecarbaldehyde
(2R)-cyclohexyl(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + cyclohexanone
1-hydroxycyclohexanecarbonitrile
Substrates: -
Products: -
Products: -
?
cyanide + decanal
(2R)-2-hydroxyundecanal
Substrates: -
Products: 56% enantiomeric excess
Products: 56% enantiomeric excess
?
cyanide + furan-2-carbaldehyde
(2R)-(furan-2-yl)(hydroxy)acetonitrile
-
Substrates: isoenzyme HNL5
Products: -
Products: -
?
cyanide + furan-2-carbaldehyde
(2S)-furan-2-yl(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + furan-2-carbaldehyde
(2S)-furan-2-yl-hydroxyacetonitrile
Substrates: -
Products: -
Products: -
?
cyanide + isobutyraldehyde
2-hydroxy-3-methylbutyronitrile
Substrates: -
Products: -
Products: -
?
cyanide + naphthalen-2-ylacetaldehyde
(2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
-
Substrates: -
Products: 3.5% (2S)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile and 96.5% (2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
Products: 3.5% (2S)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile and 96.5% (2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
?
cyanide + naphthalen-2-ylacetaldehyde
(2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile + (2S)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
-
Substrates: -
Products: 33.2% (2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile and 66.8% (2S)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
Products: 33.2% (2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile and 66.8% (2S)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
?
cyanide + naphthalene-1-carbaldehyde
(2R)-hydroxy(naphthalen-1-yl)acetonitrile
-
Substrates: isoenzyme HNL5
Products: -
Products: -
?
cyanide + naphthalene-2-carbaldehyde
(2R)-hydroxy(naphthalen-2-yl)acetonitrile
-
Substrates: isoenzyme HNL5
Products: -
Products: -
?
cyanide + octanal
(2R)-2-hydroxynonanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + p-anisaldehyde
(R)-2-hydroxy-2-(4-methoxyphenyl)acetonitrile
Substrates: -
Products: -
Products: -
?
cyanide + piperonal
(R)-2-hydroxy-2-(3,4-methylenedioxyphenyl)acetonitrile
Substrates: -
Products: -
Products: -
?
cyanide + pivaldehyde
pivaloyl cyanide
Substrates: -
Products: -
Products: -
?
cyanide + propanal
(2R)-2-hydroxybutanenitrile
-
Substrates: activity is 20% of the activity with benzaldehyde
Products: 7% enentiomeric excess
Products: 7% enentiomeric excess
?
cyanide + propionaldehyde
2-hydroxybutyronitrile
Substrates: -
Products: -
Products: -
?
cyanide + pyridine-3-carbaldehyde
(2R)-hydroxy(pyridin-3-yl)acetonitrile
-
Substrates: isoenzyme HNL5
Products: -
Products: -
?
cyanide + pyridine-3-carbaldehyde
(2R)-hydroxy(pyridin-3-yl)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + tetrahydro-2H-pyran-2-carbaldehyde
(2S)-hydroxy-[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile + (2R)-hydroxy-[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile + (2S)-hydroxy-[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile + (2R)-hydroxy-[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile
-
Substrates: -
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate tetrahydro-2H-pyran-2-carbaldehyde is converted to 47.6% (2S)-hydroxy[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile, 4.6% (2R)-hydroxy[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile, 42.6% (2S)-hydroxy[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile and 5.2% (2R)-hydroxy[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate tetrahydro-2H-pyran-2-carbaldehyde is converted to 47.6% (2S)-hydroxy[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile, 4.6% (2R)-hydroxy[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile, 42.6% (2S)-hydroxy[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile and 5.2% (2R)-hydroxy[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile
?
cyanide + tetrahydrofuran-2-carbaldehyde
(2S)-hydroxy-[(2R)-tetrahydrofuran-2-yl]ethanenitrile + (2R)-hydroxy-[(2R)-tetrahydrofuran-2-yl]ethanenitrile + (2S)-hydroxy-[(2S)-tetrahydrofuran-2-yl]ethanenitrile + (2R)-hydroxy-[(2S)-tetrahydrofuran-2-yl]ethanenitrile
-
Substrates: -
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate tetrahydrofuran-2-carbaldehyde is converted to 33.7% (2S)-hydroxy[(2R)-tetrahydrofuran-2-yl]ethanenitrile, 16.2% (2R)-hydroxy[(2R)-tetrahydrofuran-2-yl]ethanenitrile, 35.6% (2S)-hydroxy[(2S)-tetrahydrofuran-2-yl]ethanenitrile and 14.5% (2R)-hydroxy[(2S)-tetrahydrofuran-2-yl]ethanenitrile
Products: the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate tetrahydrofuran-2-carbaldehyde is converted to 33.7% (2S)-hydroxy[(2R)-tetrahydrofuran-2-yl]ethanenitrile, 16.2% (2R)-hydroxy[(2R)-tetrahydrofuran-2-yl]ethanenitrile, 35.6% (2S)-hydroxy[(2S)-tetrahydrofuran-2-yl]ethanenitrile and 14.5% (2R)-hydroxy[(2S)-tetrahydrofuran-2-yl]ethanenitrile
?
cyanide + thiophene-2-carbaldehyde
(2R)-hydroxy(thiophen-2-yl)acetonitrile
-
Substrates: isoenzyme HNL5
Products: -
Products: -
?
cyanide + thiophene-2-carbaldehyde
(2S)-hydroxy-2-(thiophen-2-yl)acetonitrile
Substrates: 82.2% conversion and 95.5% enantiomeric excess after 30 min incubation
Products: -
Products: -
?
cyanide + thiophene-2-carbaldehyde
hydroxy(thiophen-2-yl)ethanenitrile
Substrates: -
Products: separation of enantiomers not posible
Products: separation of enantiomers not posible
?
HCN + 1-naphthalenecarboxaldehyde
(R)-2-hydroxy-2-(1-naphthyl)acetonitrile
-
Substrates: 60% conversion
Products: 93% enantiomeric excess
Products: 93% enantiomeric excess
?
HCN + 2,3,4,5-tetrafluorobenzaldehyde
(R)-2-hydroxy-2-(2,3,4,5-tetrafluorophenyl)acetonitrile
-
Substrates: 26% conversion
Products: 23% enantiomeric excess
Products: 23% enantiomeric excess
?
HCN + 2,3,4-trimethoxybenzaldehyde
(R)-2-hydroxy-2-(2,3,4-trimethoxyphenyl)acetonitrile
-
Substrates: 14% conversion
Products: % enantiomeric excess
Products: % enantiomeric excess
?
HCN + 2,3,5,6-tetrafluorobenzaldehyde
(R)-2-hydroxy-2-(2,3,5,6-tetrafluorophenyl)acetonitrile
-
Substrates: 21% conversion
Products: 12% enantiomeric excess
Products: 12% enantiomeric excess
?
HCN + 2,3,5-trimethoxybenzaldehyde
(R)-2-hydroxy-2-(2,3,5-trimethoxyphenyl)acetonitrile
-
Substrates: 16% conversion
Products: 28% enantiomeric excess
Products: 28% enantiomeric excess
?
HCN + 2,3-dichlorobenzaldehyde
(R)-2-hydroxy-2-(2,3-dichlorophenyl)acetonitrile
-
Substrates: 11% conversion
Products: 22% enantiomeric excess
Products: 22% enantiomeric excess
?
HCN + 2,3-dimethoxybenzaldehyde
(R)-2-hydroxy-2-(2,3-dimethoxyphenyl)acetonitrile
-
Substrates: 7% conversion
Products: 37% enantiomeric excess
Products: 37% enantiomeric excess
?
HCN + 2,4-dichlorobenzaldehyde
(R)-2-hydroxy-2-(2,4-dichlorophenyl)acetonitrile
-
Substrates: 13% conversion
Products: 78% enantiomeric excess
Products: 78% enantiomeric excess
?
HCN + 2,4-dimethoxybenzaldehyde
(R)-2-hydroxy-2-(2,4-dimethoxyphenyl)acetonitrile
-
Substrates: 11% conversion
Products: 48% enantiomeric excess
Products: 48% enantiomeric excess
?
HCN + 2,4-dimethylbenzaldehyde
(R)-2-hydroxy-2-(2,4-dimethylphenyl)acetonitrile
-
Substrates: 5.8% conversion
Products: 86% enantiomeric excess
Products: 86% enantiomeric excess
?
HCN + 2,5-dichlorobenzaldehyde
(R)-2-hydroxy-2-(2,5-dichlorophenyl)acetonitrile
-
Substrates: 8.8% conversion
Products: 57% enantiomeric excess
Products: 57% enantiomeric excess
?
HCN + 2,5-dimethoxybenzaldehyde
(R)-2-hydroxy-2-(2,5-dimethoxyphenyl)acetonitrile
-
Substrates: 9% conversion
Products: 63% enantiomeric excess
Products: 63% enantiomeric excess
?
HCN + 2,6-dichlorobenzaldehyde
(R)-2-hydroxy-2-(2,6-dichlorophenyl)acetonitrile
-
Substrates: 10% conversion
Products: 12% enantiomeric excess
Products: 12% enantiomeric excess
?
HCN + 2,6-dimethoxybenzaldehyde
(R)-2-hydroxy-2-(2,6-dimethoxyphenyl)acetonitrile
-
Substrates: 6.5% conversion
Products: 32% enantiomeric excess
Products: 32% enantiomeric excess
?
HCN + 2-allylcyclohexanone
cis-(1R,2S)-1-hydroxy-2-allylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-allylcyclohexanone
trans-(1R,2R)-1-hydroxy-2-allylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-allyloxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-allyloxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-allyloxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-allyloxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-butanone
(R)-2-hydroxy-2-methylbutyronitrile
-
Substrates: 48% conversion
Products: 72% enantiomeric excess
Products: 72% enantiomeric excess
?
HCN + 2-decanone
(R)-2-hydroxy-2-methyl-decanenitrile
-
Substrates: 18% conversion
Products: 52% enantiomeric excess
Products: 52% enantiomeric excess
?
HCN + 2-ethoxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-ethoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-ethoxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-ethoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-ethylcyclohexanone
cis-(1R,2S)-1-hydroxy-2-ethylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-ethylcyclohexanone
trans-(1R,2R)-1-hydroxy-2-methylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-furancarboxaldehyde
(S)-2-hydroxy-2-(2-furyl)acetonitrile
-
Substrates: 1.2% conversion
Products: 98% enantiomeric excess
Products: 98% enantiomeric excess
?
HCN + 2-heptanone
(R)-2-hydroxy-2-methyl-heptanenitrile
-
Substrates: 39% conversion
Products: 74% enantiomeric excess
Products: 74% enantiomeric excess
?
HCN + 2-hexanone
(R)-2-hydroxy-2-methyl-hexanenitrile
-
Substrates: 48% conversion
Products: 80% enantiomeric excess
Products: 80% enantiomeric excess
?
HCN + 2-methoxybenzaldehyde
(R)-2-hydroxy-2-(2-methoxyphenyl)acetonitrile
-
Substrates: 6.0% conversion
Products: 41% enantiomeric excess
Products: 41% enantiomeric excess
?
HCN + 2-methoxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-methoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-methoxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-methoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-methylbenzaldehyde
(R)-2-hydroxy-2-(2-methylphenyl)acetonitrile
-
Substrates: 6% conversion
Products: 61% enantiomeric excess
Products: 61% enantiomeric excess
?
HCN + 2-methylcyclohexanone
cis-(1R,2S)-1-hydroxy-2-methylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-methylcyclohexanone
trans-(1R,2R)-1-hydroxy-2-methylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-n-propoxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-n-propoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-n-propoxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-n-propoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-n-propylcyclohexanone
cis-(1R,2S)-1-hydroxy-2-n-propylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-n-propylcyclohexanone
trans-(1R,2R)-1-hydroxy-2-n-propylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 2-naphthalenecarboxaldehyde
(R)-2-hydroxy-2-(2-naphthyl)acetonitrile
-
Substrates: 58% conversion
Products: 98% enantiomeric excess
Products: 98% enantiomeric excess
?
HCN + 2-nonanone
(R)-2-hydroxy-2-methyl-nonanenitrile
-
Substrates: 20% conversion
Products: 65% enantiomeric excess
Products: 65% enantiomeric excess
?
HCN + 2-octanone
(R)-2-hydroxy-2-methyl-octanenitrile
-
Substrates: 22% conversion
Products: 67% enantiomeric excess
Products: 67% enantiomeric excess
?
HCN + 2-pentanone
(R)-2-hydroxy-2-methyl-pentanenitrile
-
Substrates: 46% conversion
Products: 81% enantiomeric excess
Products: 81% enantiomeric excess
?
HCN + 2-pyridinecarboxyaldehyde
(S)-2-hydroxy-2-(2-pyridyl)acetonitrile
-
Substrates: 89% conversion
Products: 22% enantiomeric excess
Products: 22% enantiomeric excess
?
HCN + 2-quinolinecarboxaldehyde
(S)-2-hydroxy-2-(2-quinolinyl)acetonitrile
-
Substrates: 38% conversion
Products: 21% enantiomeric excess
Products: 21% enantiomeric excess
?
HCN + 2-thiophenecarboxaldehyde
(S)-2-hydroxy-2-(2-thiophenyl)acetonitrile
-
Substrates: 31% conversion
Products: 88% enantiomeric excess
Products: 88% enantiomeric excess
?
HCN + 2-trifluoromethylbenzaldehyde
(R)-2-hydroxy-2-(2-trifluoromethylphenyl)acetonitrile
-
Substrates: 72% conversion
Products: 5% enantiomeric excess
Products: 5% enantiomeric excess
?
HCN + 2-undecanone
(R)-2-hydroxy-2-methyl-undecanenitrile
-
Substrates: 21% conversion
Products: 31% enantiomeric excess
Products: 31% enantiomeric excess
?
HCN + 3,3-dimethyl-2-butanone
(R)-2-hydroxy-2,3,3-trimethyl-butyronitrile
-
Substrates: 28% conversion
Products: 38% enantiomeric excess
Products: 38% enantiomeric excess
?
HCN + 3,4,5-trimethoxybenzaldehyde
(R)-2-hydroxy-2-(3,4,5-trimethoxyphenyl)acetonitrile
-
Substrates: 24% conversion
Products: 31% enantiomeric excess
Products: 31% enantiomeric excess
?
HCN + 3,4-dichlorobenzaldehyde
(R)-2-hydroxy-2-(3,4-dichlorophenyl)acetonitrile
-
Substrates: 7.9% conversion
Products: 94% enantiomeric excess
Products: 94% enantiomeric excess
?
HCN + 3,4-dimethoxybenzaldehyde
(R)-2-hydroxy-2-(3,4-dimethoxyphenyl)acetonitrile
-
Substrates: 13% conversion
Products: 78% enantiomeric excess
Products: 78% enantiomeric excess
?
HCN + 3,5-dichlorobenzaldehyde
(R)-2-hydroxy-2-(3,5-dichlorophenyl)acetonitrile
-
Substrates: 21% conversion
Products: 92% enantiomeric excess
Products: 92% enantiomeric excess
?
HCN + 3,5-dimethoxybenzaldehyde
(R)-2-hydroxy-2-(3,5-dimethoxyphenyl)acetonitrile
-
Substrates: 17% conversion
Products: 97% enantiomeric excess
Products: 97% enantiomeric excess
?
HCN + 3-chlorobenzaldehyde
(R)-2-hydroxy-2-(3-chlorophenyl)acetonitrile
-
Substrates: 38% conversion
Products: 92% enantiomeric excess
Products: 92% enantiomeric excess
?
HCN + 3-methoxybenzaldehyde
(R)-2-hydroxy-2-(3-methoxyphenyl)acetonitrile
-
Substrates: 31% conversion
Products: 92% enantiomeric excess
Products: 92% enantiomeric excess
?
HCN + 3-methoxycyclohexanone
cis-(1R,3S)-1-hydroxy-3-methoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 3-methoxycyclohexanone
trans-(1R,3R)-1-hydroxy-3-methoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 3-methyl-2-butanone
(R)-2-hydroxy-2,3-dimethyl-butyronitrile
-
Substrates: 39% conversion
Products: 42% enantiomeric excess
Products: 42% enantiomeric excess
?
HCN + 3-methylbenzaldehyde
(R)-2-hydroxy-2-(3-methylphenyl)acetonitrile
-
Substrates: 7.5% conversion
Products: 87% enantiomeric excess
Products: 87% enantiomeric excess
?
HCN + 3-methylcyclohexanone
cis-(1R,3S)-1-hydroxy-3-methylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 3-methylcyclohexanone
trans-(1R,3R)-1-hydroxy-3-methylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 3-nitrobenzaldehyde
(R)-2-hydroxy-2-(3-nitrophenyl)acetonitrile
-
Substrates: 87% conversion
Products: 65% enantiomeric excess
Products: 65% enantiomeric excess
?
HCN + 3-phenoxybenzaldehyde
(R)-2-hydroxy-2-(3-phenoxyphenyl)acetonitrile
-
Substrates: 42% conversion
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
?
HCN + 3-pyridinecarboxyaldehyde
(R)-2-hydroxy-2-(3-pyridyl)acetonitrile
-
Substrates: 90% conversion
Products: 75% enantiomeric excess
Products: 75% enantiomeric excess
?
HCN + 3-trifluoromethylbenzaldehyde
(R)-2-hydroxy-2-(3-trifluoro-methylphenyl)acetonitrile
-
Substrates: 91% conversion
Products: 68% enantiomeric excess
Products: 68% enantiomeric excess
?
HCN + 3-trifluoromethylcyclohexanone
cis-(1R,3S)-1-hydroxy-3-trifluoromethylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 3-trifluoromethylcyclohexanone
trans-(1R,3R)-1-hydroxy-3-trifluoromethylcyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + 4-allyloxybenzaldehyde
(R)-2-hydroxy-2-(4-allyloxyphenyl)acetonitrile
-
Substrates: 6.4% conversion
Products: 98% enantiomeric excess
Products: 98% enantiomeric excess
?
HCN + 4-benzyloxybenzaldehyde
(R)-2-hydroxy-2-(4-benzyloxyphenyl)acetonitrile
-
Substrates: 5.8% conversion
Products: 98% enantiomeric excess
Products: 98% enantiomeric excess
?
HCN + 4-bromobenzaldehyde
(R)-2-hydroxy-2-(4-bromophenyl)acetonitrile
-
Substrates: 22% conversion
Products: 99% enantiomeric excess
Products: 99% enantiomeric excess
?
HCN + 4-fluorobenzaldehyde
(R)-2-hydroxy-2-(4-fluorophenyl)acetonitrile
-
Substrates: 28% conversion
Products: % enantiomeric excess
Products: % enantiomeric excess
?
HCN + 4-methoxybenzaldehyde
(R)-2-hydroxy-2-(4-methoxyphenyl)acetonitrile
-
Substrates: 17% conversion
Products: 97% enantiomeric excess
Products: 97% enantiomeric excess
?
HCN + 4-methyl-2-pentanone
(R)-2-hydroxy-2,4-dimethyl-pentanenitrile
-
Substrates: 40% conversion
Products: 88% enantiomeric excess
Products: 88% enantiomeric excess
?
HCN + 4-methylbenzaldehyde
(R)-2-hydroxy-2-(4-methylphenyl)acetonitrile
-
Substrates: 7.0% conversion
Products: 95% enantiomeric excess
Products: 95% enantiomeric excess
?
HCN + 4-nitrobenzaldehyde
(R)-2-hydroxy-2-(4-nitrophenyl)acetonitrile
-
Substrates: 89% conversion
Products: 71% enantiomeric excess
Products: 71% enantiomeric excess
?
HCN + 4-phenoxybenzaldehyde
(R)-2-hydroxy-2-(4-phenoxyphenyl)acetonitrile
Substrates: -
Products: -
Products: -
?
HCN + 4-pyridinecarboxyaldehyde
(R)-2-hydroxy-2-(4-pyridyl)acetonitrile
-
Substrates: 65% conversion
Products: 41% enantiomeric excess
Products: 41% enantiomeric excess
?
HCN + 4-quinolinecarboxaldehyde
(R)-2-hydroxy-2-(4-quinolinyl)acetonitrile
-
Substrates: 73% conversion
Products: 28% enantiomeric excess
Products: 28% enantiomeric excess
?
HCN + 4-tert-butyldimethylsilyloxybenzaldehyde
(R)-2-hydroxy-2-(4-tert-butyldimethylsilyloxyphenyl)acetonitrile
-
Substrates: 4.8% conversion
Products: 97% enantiomeric excess
Products: 97% enantiomeric excess
?
HCN + 4-trifluoromethylbenzaldehyde
(R)-2-hydroxy-2-(4-trifluoromethylphenyl)acetonitrile
-
Substrates: 90% conversion
Products: 76% enantiomeric excess
Products: 76% enantiomeric excess
?
HCN + 5-methyl-2-hexanone
(R)-2-hydroxy-2,5-dimethyl-hexanenitrile
-
Substrates: 30% conversion
Products: 76% enantiomeric excess
Products: 76% enantiomeric excess
?
HCN + acetophenone
2-hydroxyphenylpropionitrile
-
Substrates: -
Products: -
Products: -
?
HCN + benzaldehyde
(R)-2-hydroxy-2-phenylacetonitrile
Substrates: -
Products: -
Products: -
?
HCN + butanal
(R)-2-hydroxy-pentanenitrile
-
Substrates: 51% conversion
Products: 84% enantiomeric excess
Products: 84% enantiomeric excess
?
HCN + cyclohexanecarboxaldehyde
(R)-2-hydroxy-2-cyclohexyl-acetonitrile
-
Substrates: 54% conversion
Products: 94% enantiomeric excess
Products: 94% enantiomeric excess
?
HCN + cyclopentanecarboxaldehyde
(R)-2-hydroxy-2-cyclopentyl-acetonitrile
-
Substrates: 51% conversion
Products: 91% enantiomeric excess
Products: 91% enantiomeric excess
?
HCN + decanal
(R)-2-hydroxyundecanenitrile
-
Substrates: reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
Products: -
Products: -
?
HCN + dodecanal
(R)-2-hydroxytridecanenitrile
-
Substrates: reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
Products: -
Products: -
?
HCN + hexanal
(R)-2-hydroxy-octanenitrile
-
Substrates: 38% conversion
Products: 81% enantiomeric excess
Products: 81% enantiomeric excess
?
HCN + iso-propoxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-iso-propoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + iso-propoxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-iso-propoxycyclohexanecarbonitrile
-
Substrates: -
Products: -
Products: -
?
HCN + isobutyraldehyde
(R)-2-hydroxy-3-methyl-butyronitrile
-
Substrates: 43% conversion
Products: 88% enantiomeric excess
Products: 88% enantiomeric excess
?
HCN + pentanal
(R)-2-hydroxy-hexanenitrile
-
Substrates: 36% conversion
Products: 85% enantiomeric excess
Products: 85% enantiomeric excess
?
HCN + piperonal
(R)-2-hydroxy-2-(3,4-methylenedioxyphenyl)acetonitrile
-
Substrates: 34% conversion
Products: 98% enantiomeric excess
Products: 98% enantiomeric excess
?
HCN + pivaldehyde
(R)-2-hydroxy-3,3-dimethyl-butyronitrile
-
Substrates: 29% conversion
Products: 92% enantiomeric excess
Products: 92% enantiomeric excess
?
HCN + propanal
(R)-2-hydroxy-butyronitrile
-
Substrates: 48% conversion
Products: 78% enantiomeric excess
Products: 78% enantiomeric excess
?
HCN + trimethylsilylmethylketone
(R)-2-hydroxy-2-trimethylsilyl-propanenitrile
-
Substrates: 62% conversion
Products: 72% enantiomeric excess
Products: 72% enantiomeric excess
?
HCN + undecanal
(R)-2-hydroxydodecanenitrile
-
Substrates: reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
Products: -
Products: -
?
nitromethane + 2-chlorobenzaldehyde
(1R)-1-(2-chlorophenyl)-2-nitroethanol
Substrates: -
Products: 34% yield, 68% enantiomeric excess
Products: 34% yield, 68% enantiomeric excess
?
nitromethane + 3-methoxybenzaldehyde
(1R)-1-(3-methoxyphenyl)-2-nitroethanol
Substrates: -
Products: 17% yield, 91% enantiomeric excess
Products: 17% yield, 91% enantiomeric excess
?
nitromethane + 4-fluorobenzaldehyde
(1R)-1-(4-fluorophenyl)-2-nitroethanol
Substrates: -
Products: 20% yield, 81% enantiomeric excess
Products: 20% yield, 81% enantiomeric excess
?
nitromethane + benzaldehyde
(1R)-2-nitro-1-phenylethanol
Substrates: 30% yield, 91% enantiomeric excess
Products: -
Products: -
?
propiophenone + HCN
(S)-1-phenylacetone cyanohydrin
-
Substrates: with 24% conversion and 46% enantiomeric exess
Products: -
Products: -
?
racemic mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
?
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
?
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
-
Substrates: high activity
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
-
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
-
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
-
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
-
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: in a large number of plant species hydroxynitrile lyases catalyzes the decomposition of cyanohydrins in order to generate hydrogen cyanide upon tissue damage. Hydrogen cyanide serves as a deterrent against herbivores and fungi
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
-
Substrates: modeling studies provide insights into the mechanism of cyanogenesis
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Prunus pseudoarmeniaca
-
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: in Prunus serotina Ehrh. macerates, the cyanogenic diglucoside (R)-amygdalin undergoes stepwise degradation to HCN catalyzed by amygdalin hydrolase, prunasin hydrolase, and (R)-(+)-mandelonitrile lyase
Products: -
Products: -
?
(R)-mandelonitrile
cyanide + benzaldehyde
-
Substrates: -
Products: -
Products: -
?, r
cyanide + 1-phenylethanone
(2R)-2-hydroxy-2-phenylpropanenitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 1-phenylethanone
(2R)-2-hydroxy-2-phenylpropanenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 2,2-dimethylpropanal
(2R)-2-hydroxy-3,3-dimethylbutanenitrile
-
Substrates: activity is 33% of the activity with benzaldehyde
Products: 9% enentiomeric excess
Products: 9% enentiomeric excess
?
cyanide + 2,2-dimethylpropanal
(2R)-2-hydroxy-3,3-dimethylbutanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 2,4-dimethylbenzaldehyde
(R)-2,4-dimethylmandelonitrile
-
Substrates: 2.44 activity compared to benzaldehyde, 43.3% enantiomeric excess
Products: -
Products: -
r
cyanide + 2,4-dimethylbenzaldehyde
(R)-2,4-dimethylmandelonitrile
-
Substrates: 99% ee of the product
Products: -
Products: -
?
cyanide + 2,4-dimethylbenzaldehyde
(R)-2-hydroxy-2-(2,4-dimethylphenyl)acetonitrile
Substrates: -
Products: -
Products: -
?
cyanide + 2,4-dimethylbenzaldehyde
(R)-2-hydroxy-2-(2,4-dimethylphenyl)acetonitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 2-chlorobenzaldehyde
(2R)-(2-chlorophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: 99% enantiomeric excess
Products: 99% enantiomeric excess
?
cyanide + 2-chlorobenzaldehyde
(2R)-(2-chlorophenyl)(hydroxy)ethanenitrile
-
Substrates: -
Products: 15.8% yield and 66% enantiomeric excess after 2 h
Products: 15.8% yield and 66% enantiomeric excess after 2 h
?
cyanide + 2-chlorobenzaldehyde
(2R)-(2-chlorophenyl)(hydroxy)ethanenitrile
Substrates: 27.7% conversion assayed by 2-aminobenzamidoxime cycling method, 32.2% conversion assayed by chiral gas chromatography
Products: -
Products: -
?
cyanide + 2-chlorobenzaldehyde
(R)-2-chloromandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 2-chlorobenzaldehyde
(R)-2-chloromandelonitrile
-
Substrates: 76% conversion with 90% ee of the product
Products: -
Products: -
?
cyanide + 2-chlorobenzaldehyde
(R)-2-chloromandelonitrile
Substrates: 60.8% conversion and 76.6% enantiomeric excess after 30 min incubation
Products: -
Products: -
?
cyanide + 2-chlorobenzaldehyde
(R)-2-chloromandelonitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 2-chlorobenzaldehyde
(R)-2-chloromandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 2-chlorobenzaldehyde
(R)-2-chloromandelonitrile
-
Substrates: -
Products: -
Products: -
?, r
cyanide + 2-methylbenzaldehyde
(R)-2-methylmandelonitrile
-
Substrates: 3.55 activity compared to benzaldehyde, 12.9% enantiomeric excess
Products: -
Products: -
r
cyanide + 2-methylbenzaldehyde
(R)-2-methylmandelonitrile
-
Substrates: 86% ee of the product
Products: -
Products: -
?
cyanide + 2-methylbenzaldehyde
(R)-2-methylmandelonitrile
Substrates: 48.3% conversion and 92% enantiomeric excess after 30 min incubation
Products: -
Products: -
?
cyanide + 2-methylbenzaldehyde
(R)-2-methylmandelonitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 3-chlorobenzaldehyde
(2R)-(3-chlorophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
?
cyanide + 3-chlorobenzaldehyde
(2R)-(3-chlorophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-chlorobenzaldehyde
(R)-3-chloromandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 3-chlorobenzaldehyde
(R)-3-chloromandelonitrile
Substrates: 46.5% conversion and 2.5% enantiomeric excess after 30 min incubation
Products: -
Products: -
?
cyanide + 3-chlorobenzaldehyde
(R)-3-chloromandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 3-methoxybenzaldehyde
(R)-3-methoxymandelonitrile
-
Substrates: 2.7 activity compared to benzaldehyde, 56.3% enantiomeric excess
Products: -
Products: -
r
cyanide + 3-methoxybenzaldehyde
(R)-3-methoxymandelonitrile
-
Substrates: 91% ee of the product
Products: -
Products: -
?
cyanide + 3-methoxybenzaldehyde
(R)-3-methoxymandelonitrile
Substrates: 30.7% conversion and 22% enantiomeric excess after 30 min incubation
Products: -
Products: -
?
cyanide + 3-methoxybenzaldehyde
(R)-3-methoxymandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 3-methylbenzaldehyde
(R)-3-methylmandelonitrile
-
Substrates: 94% ee of the product
Products: -
Products: -
?
cyanide + 3-methylbenzaldehyde
(R)-3-methylmandelonitrile
Substrates: 28% conversion and 53.3% enantiomeric excess after 30 min incubation
Products: -
Products: -
?
cyanide + 3-phenylpropanal
(2R)-2-hydroxy-4-phenylbutanenitrile
Substrates: -
Products: 68% enantiomeric excess
Products: 68% enantiomeric excess
?
cyanide + 3-phenylpropanal
(2R)-2-hydroxy-4-phenylbutanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 3-phenylpropanal
(2R)-2-hydroxy-4-phenylbutanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 4-biphenylcarboxaldehyde
?
Substrates: -
Products: -
Products: -
?
cyanide + 4-biphenylcarboxaldehyde
?
-
Substrates: 86% ee of the product
Products: -
Products: -
?
cyanide + 4-bromobenzaldehyde
(2R)-(4-bromophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
?
cyanide + 4-bromobenzaldehyde
(2R)-(4-bromophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 4-fluorobenzaldehyde
(2R)-(4-fluorophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
?
cyanide + 4-fluorobenzaldehyde
(2R)-(4-fluorophenyl)(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 4-hydroxybenzaldehyde
(R)-4-hydroxymandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 4-hydroxybenzaldehyde
(R)-4-hydroxymandelonitrile
-
Substrates: (R)-cyanohydrin is formed with 2% yield and 25% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
Products: -
Products: -
r
cyanide + 4-methoxybenzaldehyde
(2R)-(4-methoxyphenyl)(hydroxy)ethanenitrile
Substrates: -
Products: 68% enantiomeric excess
Products: 68% enantiomeric excess
?
cyanide + 4-methoxybenzaldehyde
(2R)-(4-methoxyphenyl)(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 4-methoxybenzaldehyde
(2R)-(4-methoxyphenyl)(hydroxy)ethanenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 4-methoxybenzaldehyde
(2R)-(4-methoxyphenyl)(hydroxy)ethanenitrile
-
Substrates: (R)-cyanohydrin is formed with 95% yield and 95% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
Products: -
Products: -
r
cyanide + 4-methoxybenzaldehyde
(2R)-hydroxy(4-methoxyphenyl)ethanenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 4-methoxybenzaldehyde
(2R)-hydroxy(4-methoxyphenyl)ethanenitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 4-methoxybenzaldehyde
(2R)-hydroxy(4-methoxyphenyl)ethanenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 4-methoxybenzaldehyde
(R)-4-methoxymandelonitrile
-
Substrates: 104% activity compared to benzaldehyde, 95.2% enantiomeric excess
Products: -
Products: -
r
cyanide + 4-methoxybenzaldehyde
(R)-4-methoxymandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + 4-methylbenzaldehyde
(2R)-(4-methylphenyl)(hydroxy)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + 4-methylbenzaldehyde
(2R)-(4-methylphenyl)(hydroxy)ethanenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + 4-methylbenzaldehyde
(R)-4-methylmandelonitrile
-
Substrates: 64.2 activity compared to benzaldehyde, 92.6% enantiomeric excess
Products: -
Products: -
r
cyanide + 4-methylbenzaldehyde
(R)-4-methylmandelonitrile
-
Substrates: 99% ee of the product
Products: -
Products: -
?
cyanide + 4-methylbenzaldehyde
(R)-4-methylmandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
?
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: wet EziG Opal-bound enzyme achieves 95% of conversion after 30 min of reaction time in batch and it was recycled up to 8times with a final conversion of 80% and excellent enantioselectivity
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: the enzyme catalyzes the synthesis of (R)-mandelonitrile from benzaldehyde with a 99% enantiomeric excess
Products: -
Products: -
?
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: CLEA-immobilized enzyme performs with 99% conversion and 98% enantiomeric excess
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: preference for (R)-product of 28%
Products: preference for (R)-product of 28%
?
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: both pH and temperature have a large effect on the initial velocity and enantiomeric excess (e.e.) of the product, (R)-mandelonitrile. High enantiomeric purity of the product is observed at low pH and temperature because the non-enzymatic reaction producing racemates of mandelonitrile is almost suppressed. The optimum pH and temperature to obtain high enantiomeric excess are pH 4.0 and 10°C, respectively. The best solvent for the highest initial velocity and enantiomeric excess is diethyl ether with an optimum aqueous phase content of 50% (v/v). The initial reaction rate increases as the aqueous phase content rises, but when the content is more than 50%, a reduction of enantiomeric excess is observed. Increasing the concentration of the substrates accelerates the initial velocity, but causes a slight decrease in the e.e. of the product. Under the optimized conditions, the conversion and enantiomeric excess of (R)-mandelonitrile for 3 h are 40 and 99%, respectively
Products: -
Products: -
?
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: -
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
?
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: 90% enantiomeric excess at 80% conversion using 0.5 M benzaldehyde in a biphasic reaction system with methyl tertiary butyl ether
Products: 90% enantiomeric excess at 80% conversion using 0.5 M benzaldehyde in a biphasic reaction system with methyl tertiary butyl ether
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: 90% enantiomeric excess at 80% conversion using 0.5 M benzaldehyde in a biphasic reaction system with methyl tertiary butyl ether
Products: 90% enantiomeric excess at 80% conversion using 0.5 M benzaldehyde in a biphasic reaction system with methyl tertiary butyl ether
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: 100% activity, 87.9% enantiomeric excess
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: 95% ee of the product
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: the enzyme shows high specific activity for (R)-mandelonitrile synthesis with 97.6% enantiomeric excess
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: several parameters influence the enantiomeric purity of the product and initial velocity of the reaction. Both pH and temperature are important parameters controlling the enantiomeric purity of the product. The optimum pH and temperature are pH 4 and 10°C, respectively. At the optimum pH and temperature, the spontaneous non-enzymatic reaction yielding the racemic mandelonitrile is almost completely suppressed. The initial velocity is markedly affected by the type of organic solvent in the biphasic system, while high enantiomeric purity is obtained when organic solvents having log P lower than 3.5 are used. The highest initial velocity of reaction and enantiomeric purity of (R)-mandelonitrile are obtained in the biphasic system of dibutyl ether with the aqueous phase content of 30% (v/v). The optimum substrate concentrations are 250 mM for benzaldehyde and 900 mM for acetone cyanohydrin, and the optimum enzyme concentration is 26.7 units/ml. The highest enantiomeric purity of (R)-mandelonitrile is successfully obtained with conversion and enantiomeric excess of 31.6% and 98.6%, respectively
Products: -
Products: -
?
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: the glycosylated enzyme efficiently performs transcyanation of (R)-mandelonitrile with a 98% enantiomeric excess in a biphasic system with diisopropyl ether
Products: -
Products: -
?
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
?
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: 72.2% conversion and 95.5% enantiomeric excess after 30 min incubation
Products: -
Products: -
?
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: -
Products: 82% yield, 99% enantiomeric excess
Products: 82% yield, 99% enantiomeric excess
?
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: -
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: the enzyme catalyses synthesis of (R)-mandelonitrile in methyl-tbutyl ether/citrate buffer biphasic system with more than 99% enantiomeric excess
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: synthesis of mandelonitrile is carried out with 89% molar conversion with 96% enantionmeric excess for R-mandelonitrile
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: 99% yield, 99% enantiomeric excess
Products: 99% yield, 99% enantiomeric excess
?
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: the formation of (R)-mandelonitrile from benzaldehyde and cyanide catalyzed by Prunus amygdalus hydroxynitrile lyase is chosen as a model reaction for the development and validation of a process model for production of (R)-cyanohydrins in an aqueous-organic biphasic-stirred tank reactor with an unknown interfacial area operated in batch mode. At 5°C and pH 5.5 the nonenzymatic reaction towards rac-mandelonitrile is largely suppressed
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: -
Products: 90.3% yield and 100% enantiomeric excess after 2 h
Products: 90.3% yield and 100% enantiomeric excess after 2 h
?
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase achieve the synthesis of (R)-mandelonitrile, (R)-cyanohydrin is formed with 93% yield and 99% enantiopurity
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: 27.7% conversion assayed by 2-aminobenzamidoxime cycling method, 32.2% conversion assayed by chiral gas chromatography
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
?
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: synthesis of (R)-mandelonitrile with 94% enantiomeric excess
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: -
Products: more than 99% enantiomeric excess
Products: more than 99% enantiomeric excess
?
cyanide + benzaldehyde
(R)-mandelonitrile
Prunus pseudoarmeniaca
-
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: (R)-specific
Products: -
Products: -
?
cyanide + benzaldehyde
(R)-mandelonitrile
-
Substrates: -
Products: -
Products: -
?, r
cyanide + butanal
(2R)-2-hydroxypentanenitrile
-
Substrates: -
Products: 42% yield, 55% enantiomeric excess
Products: 42% yield, 55% enantiomeric excess
?
cyanide + butanal
(2R)-2-hydroxypentanenitrile
Substrates: -
Products: 100% yield, 90% enantiomeric excess
Products: 100% yield, 90% enantiomeric excess
?
cyanide + furan-2-carbaldehyde
(2R)-furan-2-yl(hydroxy)ethanenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + furan-2-carbaldehyde
(2R)-furan-2-yl(hydroxy)ethanenitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + furan-2-carbaldehyde
(2R)-furan-2-yl(hydroxy)ethanenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + hexan-2-one
(2R)-2-hydroxy-2-methylhexanenitrile
Substrates: -
Products: 95% enantiomeric excess
Products: 95% enantiomeric excess
?
cyanide + hexan-2-one
(2R)-2-hydroxy-2-methylhexanenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + hexan-2-one
(2R)-2-hydroxy-2-methylhexanenitrile
-
Substrates: -
Products: -
Products: -
r
cyanide + hexan-2-one
(2R)-2-hydroxy-2-methylhexanenitrile
-
Substrates: -
Products: -
Products: -
?
cyanide + hexanal
(2R)-2-hydroxyheptanenitrile
Substrates: -
Products: 98% enantiomeric excess
Products: 98% enantiomeric excess
?
cyanide + hexanal
(2R)-2-hydroxyheptanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + hydroxypivaldehyde
(R)-hydroxypivaldehyde cyanohydrin
-
Substrates: crosslinked enzyme aggregates catalyze synthesis of (R)-hydroxypivaldehyde cyanohydrin under reaction conditions that immediately inactivated non-immobilized enzyme
Products: -
Products: -
r
cyanide + hydroxypivaldehyde
(R)-hydroxypivaldehyde cyanohydrin
-
Substrates: -
Products: -
Products: -
r
cyanide + naphthalene-2-carbaldehyde
(2R)-hydroxy(naphthalen-2-yl)ethanenitrile
-
Substrates: -
Products: 97.6% (2R)-hydroxy(naphthalen-2-yl)ethanenitrile and 2.4% (2S)-hydroxy(naphthalen-2-yl)ethanenitrile
Products: 97.6% (2R)-hydroxy(naphthalen-2-yl)ethanenitrile and 2.4% (2S)-hydroxy(naphthalen-2-yl)ethanenitrile
?
cyanide + naphthalene-2-carbaldehyde
(2R)-hydroxy(naphthalen-2-yl)ethanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + pentan-2-one
(2R)-2-hydroxy-2-methylpentanenitrile
-
Substrates: -
Products: 17% yield
Products: 17% yield
?
cyanide + pentan-2-one
(2R)-2-hydroxy-2-methylpentanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + phenylacetaldehyde
(2R)-2-hydroxy-3-phenylpropanenitrile
Substrates: -
Products: 96% enantiomeric excess
Products: 96% enantiomeric excess
?
cyanide + phenylacetaldehyde
(2R)-2-hydroxy-3-phenylpropanenitrile
-
Substrates: -
Products: 96.3% (2R)-2-hydroxy-3-phenylpropanenitrile and 3.7% (2S)-2-hydroxy-3-phenylpropanenitrile
Products: 96.3% (2R)-2-hydroxy-3-phenylpropanenitrile and 3.7% (2S)-2-hydroxy-3-phenylpropanenitrile
?
cyanide + phenylacetaldehyde
(2R)-2-hydroxy-3-phenylpropanenitrile
-
Substrates: isoenzyme HNL5
Products: -
Products: -
?
cyanide + phenylacetaldehyde
(2R)-2-hydroxy-3-phenylpropanenitrile
Substrates: -
Products: -
Products: -
?
cyanide + thiophene-2-carbaldehyde
(2R)-hydroxy(thiophen-2-yl)ethanenitrile
-
Substrates: -
Products: 87% yield, 99% enentiomeric excess
Products: 87% yield, 99% enentiomeric excess
?
cyanide + thiophene-2-carbaldehyde
(2R)-hydroxy(thiophen-2-yl)ethanenitrile
Substrates: -
Products: 48% yield, 87% enantiomeric excess
Products: 48% yield, 87% enantiomeric excess
?
cyanide + thiophene-2-carbaldehyde
(2S)-hydroxy(thiophen-2-yl)ethanenitrile
-
Substrates: activity is 2fold higher than with benzaldehyde
Products: 75% enentiomeric excess, The (S)-configuration is due to the Cahn-Ingold-Prelog rules
Products: 75% enentiomeric excess, The (S)-configuration is due to the Cahn-Ingold-Prelog rules
?
cyanide + thiophene-2-carbaldehyde
(2S)-hydroxy(thiophen-2-yl)ethanenitrile
Substrates: -
Products: -
Products: -
?
HCN + 2-chlorobenzaldehyde
(R)-2-hydroxy-2-(2-chlorophenyl)acetonitrile
Substrates: -
Products: -
Products: -
?
HCN + 2-chlorobenzaldehyde
(R)-2-hydroxy-2-(2-chlorophenyl)acetonitrile
-
Substrates: 37% conversion
Products: 56% enantiomeric excess
Products: 56% enantiomeric excess
?
HCN + 4-chlorbenzaldehyde
(R)-2-hydroxy-2-(4-chlorophenyl)acetonitrile
Substrates: -
Products: -
Products: -
?
HCN + 4-chlorbenzaldehyde
(R)-2-hydroxy-2-(4-chlorophenyl)acetonitrile
-
Substrates: 21% conversion
Products: 99% enantiomeric excess
Products: 99% enantiomeric excess
?
HCN + benzaldehyde
(R)-mandelonitrile
-
Substrates: reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
Products: -
Products: -
?
HCN + benzaldehyde
(R)-mandelonitrile
-
Substrates: 13% conversion
Products: 93% enantiomeric excess
Products: 93% enantiomeric excess
?
racemic 2-nitro-1-phenylethanol
(S)-2-nitro-1-phenylethanol + nitromethane + benzaldehyde
Substrates: 48% conversion and more than 97% enantiomeric excess
Products: -
Products: -
?
racemic 2-nitro-1-phenylethanol
(S)-2-nitro-1-phenylethanol + nitromethane + benzaldehyde
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: broad substrate range includes alphatic and aromatic aldehydes as well as ketones. Low activity with acetaldehyde, propionaldehyde and acetone cyanohydrin
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate range includes alphatic and aromatic aldehydes as well as ketones. Low activity with acetaldehyde, propionaldehyde and acetone cyanohydrin
Products: -
Products: -
?
additional information
?
-
-
Substrates: low activity towards acetone cyanohydrin
Products: -
Products: -
?
additional information
?
-
-
Substrates: biocatalyst to synthesize a series of chiral methyl ketone cyanohydrins with satisfactory conversion and conspicuous enantiomeric excess. 2',6'-dimethylacetophenone, a compound with steric hindrance on the phenyl group is unsuitable as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also catalyzes transcyanation of benzaldehyde and acetone cyanohydrin to (R)-mandelonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: synthesis of optically active (R)-2-trimethylsilyl-2-hydroxyl-ethylcyanide by asymmetric transcyanation of acetyltrimethylsilane with acetone cyanohydrin in a biphasic system. The substrate conversion and the product enantiomeric excess are 95% and 98% under the optimized conditions. Acetyltrimethylsilane was a better substrate of the enzyme than its carbon counterpart
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is active towards aromatic and aliphatic aldehydes and shows a preference for small substrates over bulky one
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme activity toward 2-methylbenzaldehyde, 2,4-dimethylbenzaldehyde and 3-methoxybenzaldehyde is very low
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is less than 5% of the activity with benzaldehyde: 4-methoxybenzaldehyde, naphthalene-1-carbaldehyde, naphthalene-2-carbaldehyde and 1,3-benzodioxole-5-carbaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: aliphatic carbonyls are poorly converted
Products: -
Products: -
?
additional information
?
-
-
Substrates: naphthyl and alkoxy substituents in the alpha- and also in the beta-position to the aldehyde group significantly influence the stereochemical outcome of the oxynitrilase-catalyzed transformation. No activity with methoxy(phenyl)acetaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrates having ortho substituents are poor substrates in terms of enantioselectivity of the resulting cyanohydrins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not accept 3,3-dimethyl-2-butanone as substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
?
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
-
Substrates: high activity
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
-
Substrates: -
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: in a large number of plant species hydroxynitrile lyases catalyzes the decomposition of cyanohydrins in order to generate hydrogen cyanide upon tissue damage. Hydrogen cyanide serves as a deterrent against herbivores and fungi
Products: -
Products: -
r
(R)-mandelonitrile
cyanide + benzaldehyde
Substrates: in Prunus serotina Ehrh. macerates, the cyanogenic diglucoside (R)-amygdalin undergoes stepwise degradation to HCN catalyzed by amygdalin hydrolase, prunasin hydrolase, and (R)-(+)-mandelonitrile lyase
Products: -
Products: -
?
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
r
cyanide + benzaldehyde
(R)-mandelonitrile
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
FAD-dependent enzyme, the FAD cofactor is deeply buried within the molecule and is completely isolated from bulk solvent
FAD
there is no evidence that the flavin cofactor directly participates in the reaction
FAD
-
absolute requirement of oxidized FAD as cofactor. Enzyme activity requires the FAD cofactor to be bound in its oxidized form. The observed inactivation upon cofactor reduction is largely caused by the reversal of the electrostatic potential within the active site
FAD
benzyl alcohol is bound too far away from the FAD cofactor in order to be oxidized
FAD
thee structure of PaHNL5 in complex with benzyl alcohol shows that this compound binds too far away from the FAD cofactor in order to directly participate in the redox mechanism proposed for aryl-alcohol oxidases
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
metal ions are not required for its activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-Iodoacetamide
1 mM, 9% residual activity; 9.0% residual activity at 1 mM
diisopropylether
the activity of the wild type enzyme is reduced from 90 to 50% as the diisopropylether concentration increased from 20 to 50% (v/v), and the enzyme is almost inactive at a high diisopropylether concentration of 70 to 80% (v/v)
diethyldicarbonate
-
68.4 and 62.5% remaining activity for recombinant enzymes from Escherichia coli and Pichia pastoris, respectively, at 1 mM
iodoacetamide
-
26.5 and 30.2% remaining activity for recombinant enzymes from Escherichia coli and Pichia pastoris, respectively, at 1 mM
iodoacetic acid
-
18.3 and 21.3% remaining activity for recombinant enzymes from Escherichia coli and Pichia pastoris, respectively, at 1 mM
iodoacetic acid
1 mM, 8% residual activity; 8.0% residual activity at 1 mM
additional information
-
the enzyme is not inhibited by sulfhydryl- or hydroxyl-modifying reagents
-
additional information
-
not inhibited by EDTA, EGTA, sodium fluoride, o-phenanthroline, 2,4-dinitro-1-thiocyanate, NaN3, dithiothreitol, phenylhydrazine, Triton X-100, 2,2'-bipyridyl, N-ethylmaleimide, and D-cycloserine
-
additional information
not inhibited by EDTA, EGTA, sodium fluoride, o-phenanthroline, 2,4-dinitro-1-thiocyanate, NaN3, dithiothreitol, phenylhydrazine, Triton X-100, 2,2'-bipyridyl, N-ethylmaleimide, and D-cycloserine
-
additional information
not inhibited by EDTA, EGTA, sodium fluoride, o-phenanthroline, 2,4-dinitro-1-thiocyanate, NaN3, dithiothreitol, phenylhydrazine, Triton X-100, 2,2'-bipyridyl, N-ethylmaleimide, and D-cycloserine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remained good
-
additional information
-
best solvents are diisopropylether, tert-butylmethylether or di-n-butylether. With all the three solvents more than 95% enantioselectivity is observed. However, the rate of the reaction is very slow
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
The apoplastic antioxidant system in Prunus: response to long-term plum pox virus infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
estimation of kinetic parameters by progress curve analysis
-
0.3
(R)-mandelonitrile
pH 5.0, temperature not specified in the publication, enzyme form DtHNL1
0.45
(R)-mandelonitrile
pH 5.0, temperature not specified in the publication, enzyme form DtHNL2
0.63
(R)-mandelonitrile
pH 5.0, temperature not specified in the publication, enzyme form DtHNL4
0.75
(R)-mandelonitrile
pH 5.0, temperature not specified in the publication, enzyme form DtHNL3
0.9
(R)-mandelonitrile
mutant enzyme Y40F, at pH 4.2 and 22°C
0.95
(R)-mandelonitrile
-
enzyme immobilized onto Eupergit C250 L, pH 5.5, 25°C
1
(R)-mandelonitrile
mutant enzyme Y103F, at pH 4.2 and 22°C
1.03
(R)-mandelonitrile
Prunus pseudoarmeniaca
-
enzyme immobilized onto Eupergit C 250L, in 50 mM citrate buffer, pH 6.0, 25°C
1.3
(R)-mandelonitrile
-
enzyme immobilized onto Eupergit CM, pH 5.5, 25°C
1.3
(R)-mandelonitrile
mutant enzyme D56E, at pH 4.2 and 22°C
1.6
(R)-mandelonitrile
Prunus pseudoarmeniaca
-
enzyme immobilized onto Eupergit C, in 50 mM citrate buffer, pH 6.0, 25°C
2.23
(R)-mandelonitrile
Prunus pseudoarmeniaca
-
free enzyme, in 50 mM citrate buffer, pH 6.0, 25°C
2.93
(R)-mandelonitrile
mutant enzyme K117R, at pH 4.2 and 22°C
8.7
(R)-mandelonitrile
wild type enzyme, at pH 4.2 and 22°C
1.6
benzaldehyde
mutant enzyme Y40F, at pH 4.2 and 22°C
2 - 5
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA112, at pH 4.0 and 25°C
2 - 3.4
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA117, at pH 4.0 and 25°C
4.9
benzaldehyde
mutant enzyme Y103F, at pH 4.2 and 22°C
7.1
benzaldehyde
mutant enzyme D56E, at pH 4.2 and 22°C
13
benzaldehyde
25°C, pH 4, hydroxynitrile lyase expressed in Pichia pastoris
13.7
benzaldehyde
native enzyme from yellow cultivar, at pH 4.0 and 25°C
14
benzaldehyde
pH 4.0, 10°C, enzyme form DtHNL1
19.2
benzaldehyde
native enzyme from purple cultivar, at pH 4.0 and 25°C
19.8
benzaldehyde
25°C, pH 4, hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris
25.2
benzaldehyde
recombinant enzyme from purple cultivar, at pH 4.0 and 25°C
26.1
benzaldehyde
25°C, pH 4, hydroxynitrile lyase expressed in Escherichia coli
26.1
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA109, at pH 4.0 and 25°C
26.3
benzaldehyde
recombinant enzyme from yellow cultivar, at pH 4.0 and 25°C
26.6
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA107, at pH 4.0 and 25°C
33
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA105, at pH 4.0 and 25°C
40
benzaldehyde
mutant enzyme K117R, at pH 4.2 and 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
estimation of kinetic parameters by progress curve analysis
-
0.15
(R)-mandelonitrile
mutant enzyme K117R, at pH 4.2 and 22°C
1.4
(R)-mandelonitrile
mutant enzyme Y103F, at pH 4.2 and 22°C
4.8
(R)-mandelonitrile
mutant enzyme D56E, at pH 4.2 and 22°C
20.4
(R)-mandelonitrile
mutant enzyme Y40F, at pH 4.2 and 22°C
142
(R)-mandelonitrile
wild type enzyme, at pH 4.2 and 22°C
144
(R)-mandelonitrile
pH 5.0, temperature not specified in the publication, enzyme form DtHNL1
156
(R)-mandelonitrile
pH 5.0, temperature not specified in the publication, enzyme form DtHNL2
272
(R)-mandelonitrile
pH 5.0, temperature not specified in the publication, enzyme form DtHNL4
356
(R)-mandelonitrile
pH 5.0, temperature not specified in the publication, enzyme form DtHNL3
14
benzaldehyde
mutant enzyme Y103F, at pH 4.2 and 22°C
24.1
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA105, at pH 4.0 and 25°C
33.6
benzaldehyde
recombinant enzyme from purple cultivar, at pH 4.0 and 25°C
35.7
benzaldehyde
native enzyme from purple cultivar, at pH 4.0 and 25°C
36.4
benzaldehyde
recombinant enzyme from yellow cultivar, at pH 4.0 and 25°C
37.2
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA107, at pH 4.0 and 25°C
38.4
benzaldehyde
25°C, pH 4, hydroxynitrile lyaseexpressed in Escherichia coli
39
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA109, at pH 4.0 and 25°C
39.7
benzaldehyde
25°C, pH 4, hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris
50.4
benzaldehyde
native enzyme from yellow cultivar, at pH 4.0 and 25°C
52.1
benzaldehyde
25°C, pH 4, hydroxynitrile lyase expressed in Pichia pastoris
53.4
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA117, at pH 4.0 and 25°C
63.1
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA112, at pH 4.0 and 25°C
102
benzaldehyde
mutant enzyme D56E, at pH 4.2 and 22°C
141
benzaldehyde
mutant enzyme K117R, at pH 4.2 and 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
(R)-mandelonitrile
mutant enzyme K117R, at pH 4.2 and 22°C
1.4
(R)-mandelonitrile
mutant enzyme Y103F, at pH 4.2 and 22°C
4.8
(R)-mandelonitrile
mutant enzyme D56E, at pH 4.2 and 22°C
5
(R)-mandelonitrile
pH 5.0, temperature not specified in the publication, enzyme form DtHNL1
16.4
(R)-mandelonitrile
wild type enzyme, at pH 4.2 and 22°C
20.4
(R)-mandelonitrile
mutant enzyme Y40F, at pH 4.2 and 22°C
0.73
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA105, at pH 4.0 and 25°C
1.33
benzaldehyde
recombinant enzyme from purple cultivar, at pH 4.0 and 25°C
1.4
benzaldehyde
recombinant enzyme from yellow cultivar, at pH 4.0 and 25°C
1.4
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA107, at pH 4.0 and 25°C
1.47
benzaldehyde
25°C, pH 4, hydroxynitrile lyase expressed in Escherichia coli
1.5
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA109, at pH 4.0 and 25°C
1.86
benzaldehyde
native enzyme from purple cultivar, at pH 4.0 and 25°C
2
benzaldehyde
25°C, pH 4, hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris
2.3
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA117, at pH 4.0 and 25°C
2.53
benzaldehyde
recombinant C-terminally truncated enzyme HNLDELTA112, at pH 4.0 and 25°C
3.6
benzaldehyde
mutant enzyme K117R, at pH 4.2 and 22°C
3.7
benzaldehyde
native enzyme from yellow cultivar, at pH 4.0 and 25°C
4
benzaldehyde
25°C, pH 4, hydroxynitrile lyase expressed in Pichia pastoris
14.6
benzaldehyde
mutant enzyme D56E, at pH 4.2 and 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
129
133.6
134
25°C, pH 4, hydroxynitrile lyase expressed in Pichia pastoris
140
25°C, pH 4, hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris
220
(R)-HNL after 24.4fold purification, in 0.3 mM citrate buffer, at pH 5.0 and 25°C
54.1
25°C, pH 4, hydroxynitrile lyase expressed in Escherichia coli
9
(R)-HNL from crude extract, in 0.3 mM citrate buffer, at pH 5.0 and 25°C
additional information
129
isoform HNL2 after purification, in 0.3 mM citrate buffer, at pH 5.0 and 25°C
additional information
-
the purified enzyme has a specific activity of 1997 units/mg at pH 4.2 and 22°C
additional information
-
the purified enzyme has a specific activity of 1945 units/mg at pH 4.2 and 22°C
additional information
-
the purified recombinant enzyme has a specific activity of 2741 units/mg at pH 4.2 and 22°C
additional information
-
the purified enzyme has a specific activity of 2140 units/mg at pH 4.2 and 22°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
-
at low pH very low amounts of crude enzyme catalyse stereoselective hydroxypivalaldehyde cyanohydrin formation in water based reaction systems
3.5 - 7
-
because of the base-catalyzed decomposition of mandelonitrile, pH dependence is only determined below pH 7.5. Activity increases from pH 3.5 to 6.2 and levels off between pH 6.2 and 7 for both isoforms
4.25
1.4 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme, immobilized on cellulosic carrier materials Avicel)
4.5
4.5 - 4.8
4.75
pH-dependent half-lives: 4.4 min (wild-type enzyme), 5.5 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme), 30.6 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme, immobilized on cellulosic carrier materials Avicel)
4.75 - 5
-
the enzyme shows maximum activity in 0.1 M sodium-citrate buffer having pH 4.75 at 25°C
5.5
4
-
selected as the optimum temperature for the reaction to avoid the non-enzymatic reaction producing racemates of mandelonitrile
4
-
selected as the assay temperature for the reaction to avoid the non-enzymatic reaction producing racemates of mandelonitrile
4.5
pH-dependent half-lives: 1.5 min (wild-type enzyme), 1.5 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme), 2.1 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme, immobilized on cellulosic carrier materials Avicel)
5.5
-
mandelonitrile cleavage reaction, enzyme immobilized onto Eupergit CM and Eupergit C 250 L supports
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 4
3.5 - 4.5
-
pH 3.5: about 70% of maximal activity, pH 4.5: about 75% of maximal activity, synthesis of (R)-mandelonitrile
4 - 5
-
the activity is significantly decreased at pH levels higher than 5.0 due to a rapidly increasing nonenzymatic reaction, yielding the racemic mixture containing both of the enantiomers
4 - 8
-
4.0 pH: about 60% of maximal activity, pH 8.0: about 50% of maximal activity
4.3 - 5.3
pH 4.3: about 45% of maximal activity, pH 5.3: about 50% of maximal activity
4.5 - 6
pH 4.5: about 40% of maximal activity, pH 6.0: about 30% of maximal activity
4.5 - 7.5
-
the enzyme shows no activity for mandelonitrile degradation below pH 4.5 and over pH 7.5, as well as no activity over pH 6.0 for mandelonitrile synthesis
5 - 6.5
-
pH 5.0: about 70% of maximal activity, pH 6.5: about 50% of maximal activity, degradation of (R)-mandelonitrile
2.5 - 4
active at pH 2.5, about 80% of maximal activity at pH 4.0
2.5 - 4
active at pH 2.5, about 80% of maximal activity at pH 4.0<
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
15
25
30
30 - 40
35
40
10
-
selected as the optimum temperature for the reaction to avoid the non-enzymatic reaction producing racemates of mandelonitrile
10
-
selected as the optimum temperature for the reaction to avoid the non-enzymatic reaction producing racemates of mandelonitrile
25
-
soluble enzyme and enzyme immobilized onto Eupergit CM and Eupergit C 250 L supports
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 70
-
10°C: about 70% of maximal activity, 70°C: about 60% of maximal activity
20 - 50
20 - 60
20°C: about 50% of maximal activity, 60°C: about 40% of maximal activity
5 - 40
-
5°C: about 80% of maximal activity, 40°C: about 50% of maximal activity, synthesis of (R)-mandelonitrile
50
Prunus pseudoarmeniaca
-
free enzyme retains about 57% of its maximum activity at 50°C whereas immobilized enzymes onto Eupergit C and Eupergit C 250 L retain about 75 and 82% of their maximum activities, respectively, at 50°C
20 - 50
20°C: about 35% of maximal activity, 50°C: about 60% of maximal activity
20 - 50
-
20°C: about 55% of maximal activity, 50°C: about 25% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
5.2
calculated from sequence, mature protein without signal peptide
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
cultivars forma flavicarpa (yellow passion fruit) and Sims (purple passion fruit)
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
temporal and spatial expression patterns in flowers and mature seeds. Highest expression levels are detected during floral development. High level of expression in parenchymal cells, both in petals and in the style of the carpe
brenda
temporal expression of amygdalin hydrolase and (R)-(+)-mandelonitrile lyase in ripening fruit. Expression may be under transcriptional control during fruit maturation. (R)-(+)-mandelonitrile lyase transcripts are localized within cotyledonary parenchyma cell
brenda
-
the specific activity of young leaves is significantly higher than that of mature leaves
brenda
-
the enzyme's specific activity in young leaves is significantly higher than that of mature leaves
brenda
temporal and spatial expression patterns in flowers and mature seeds
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme is involved in the cyanogenic pathway, a widespread defense mechanism against herbivores and pathogens. Plants produce cyanogenic glycosides e.g. prunasin or amygdalin, store these compounds in different tissues, and enzymatically degrade them upon tissue disruption, in order to finally release toxic hydrogen cyanide
metabolism
the enzyme is involved in a process called cyanogenesis. They possess an important biological role in plant defense against herbivoral and fungal attack due to the bitter taste and the release of toxic hydrogen cyanide upon tissue disruption
physiological function
the enzyme is involved in the cyanogenic pathway, a widespread defense mechanism against herbivores and pathogens. Plants produce cyanogenic glycosides e.g. prunasin or amygdalin, store these compounds in different tissues, and enzymatically degrade them upon tissue disruption, in order to finally release toxic hydrogen cyanide
physiological function
the enzyme is involved in aprocess called cyanogenesis. They possess an important biological role in plant defense against herbivoral and fungal attack due to the bitter taste and the release of toxic hydrogen cyanide upon tissue disruption
physiological function
the enzyme gene participates in Arabidopsis defense against Tetranychus urticae. After mite infestation, mandelonitrile content increases in wild type and overexpressing plants, while hydrogen cyanide accumulates. The reduced leaf damage detected in the enzyme overexpressing lines reflects the mite's reduced ability to feed on leaves, which consequently restricts mite fecundity
Show AA Sequence and Transmembrane Helices (274 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
13000
14067
calculated from sequence, mature protein without signal peptide
17000
hydroxynitrile lyase expressed in Pichia pastoris, SDS-PAGE
20000
46000 - 47000
52400
58100
61000
62000
62751
13000
hydroxynitrile lyase expressed in Escherichia coli, SDS-PAGE
13000
hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris, SDS-PAGE
46000 - 47000
-
gel filtration, hydroxynitrile lyase S, hydroxynitrile lyase L
62000
x * 62751, calculated, x * 62000, SDS-PAGE of deglycosylated protein
62751
x * 62751, calculated, x * 62000, SDS-PAGE of deglycosylated protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
?
x * 62751, calculated, x * 62000, SDS-PAGE of deglycosylated protein
homodimer
-
2 * 20000, recombinant enzyme from Escherichia coli, SDS-PAGE
homodimer
-
2 * 24000, recombinant enzyme from Pichia pastoris, SDS-PAGE
monomer
1 * 62751, isoform HNL2, calculated from amino acid sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
flavoprotein
enzyme shows a typical flavoprotein spectrum with absorption maxima at 389 nm nd 463 nm
glycoprotein
glycoprotein
glycosylation sites at position N109 and N123
glycoprotein
-
the recombinant enzyme from Pichia pastoris is glycosylated
glycoprotein
hydroxynitrile lyase from leaves and that expressed in Pichia pastoris are glycosylated, whereas that expressed in Escherichia coli is not. Predicted mature enzyme has a N-glycosylation site on the asparagine residue at 105
glycoprotein
the mass difference between the glycosylated and deglycosylated form of the recombinant protein expressed in Aspergillus niger averages to 25 kDa, which indicates that more than one sugar unit is attached to the glycosylated Asn residues
glycoprotein
molecular mass 97000 Da, mass of deglycosylated protein 62000 Da
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure at a crystallographic resolution of 2.5 A and comparison with the S-selective HNL from Hevea brasiliensis. The structures exhibit an alpha/beta-hydrolase fold and a Ser-His-Asp catalytic triad. Modeling of complexes of the enzymes with both (R)- and (S)-mandelonitrile leads to a catalytic mechanism, in which His236 from the catalytic triad acts as a general base and the emerging negative charge on the cyano group is stabilized by main-chain amide groups and an alpha-helix dipole very similar to alpha/beta-hydrolases
ligand-free enzyme and in complexes with acetate, cyanide ion, and thiocyanate or iodoacetate hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M sodium acetate (pH 5.0), 28-32 % (w/v) PEG monomethyl ether 2000, and 0.3 M NDSB-195
sitting drop vapor-diffusion method
to 2.5 A resolution, Structure exhibits a cupin fold, and manganese is bound to three histidine and one glutamine residue
hanging drop vapor diffusion method, using 0.1 M Bis-Tris-HCl (pH 6.0-7.0), 0.15 M potassium thiocyanate, 8-11% (w/v) PEG 8000, and 8% (w/v) PEG 1500
-
crystals of the His6-tagged hydroxynitrile lyase are prepared using vapor diffusion sitting drop method at 20°C. The crystal structures of Passiflora edulis hydroxynitrile lyase and its C-terminal peptide depleted derivative are determined by molecular replacement method using the template structure of a heat stable protein, SP1, from Populus tremula at 2.8 and 1.8 A resolution, respectively. Passiflora edulis hydroxynitrile lyase belongs to dimeric alpha+beta barrel superfamily consisting of a central beta-barrel in the middle of a dimer. The structure of Passiflora edulis hydroxynitrile lyase complexed with (R)-mandelonitrile is also determined. The hydroxyl group of (R)-mandelonitrile forms hydrogen bonds with His8 and Tyr30 in the active site, whereas the nitrile group is oriented toward the carboxyl group of Glu54, unlike other hydroxynitrile lyases, where it interacts with basic residues typically
3D structural data of the enzyme with the reaction product benzaldehyde bound within the active site, which allow unambiguous assignment of the location of substrate binding
crystal structuture of mutant V317A of hydroxynitrile lyase isoenzyme 5 in complex with benzyl alcohol. The structure of is determined at a resolutionof 2.3 A by molecular replacement
hanging drop vapor diffusion using polyethylene glycol 4000 and isopropanol as coprecipitants. The crystals belong to the monoclinic space group P2(1) with unit cell parameters a = 69.9, b = 95.1, c = 95.6 A, and beta = 118.5 degrees. A complete set of diffraction data collected to 2.6 A resolution on native crystals of isoenzyme III
-
triclinic crystals grown in hanging drops, 1.5 A resolution, space group P1 with cell parameters a = 56.2 A, b = 67.5 A, c = 79.8
vapor diffusion method, high resolution X-ray structure of the highly glycosylated Prunus amygdalus HNL isoenzyme 5 (PaHNL5 V317A) expressed in Aspergillus niger and its complex with benzyl alcohol. In PaHNLs benzyl alcohol is bound too far away from the FAD cofactor in order to be oxidized
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F179A
the variant has about 12fold increased selectivity towards the retro-nitroaldol reaction over cyanogenesis (the wild type reaction)
F179N
the variant improves about 2.4fold kcat/Km value and E value to 138 versus 81 by wild type
D56E
the mutation results in preferential recognition of (R)-mandelonitrile exhibiting the lower Km value than that of the wild type enzyme and retains 4.2% activity of the wild type
K117R
the enzyme activity is significantly decreased as compared with the wild type enzyme. The mutation results in preferential recognition of (R)-mandelonitrile exhibiting the lower Km value than that of the wild type enzyme
R38A
the cleavage activity of the variant is completely lost
Y103F
the enzyme activity is significantly decreased as compared with the wild type enzyme. The mutant shows improved (R)-mandelonitrile binding affinity compared to the wild type enzyme
Y40F
the mutant shows improved (R)-mandelonitrile binding affinity compared to the wild type enzyme and retains 12.6% activity of the wild type
N85E
-
the mutant shows lower specific activity with 2-chlorobenzaldehyde plus cyanide than the wild type at pH 3.5 and 25 C for 30 min of incubation
N85H
-
the mutant shows lower specific activity with 2-chlorobenzaldehyde plus cyanide than the wild type at pH 3.5 and 25 C for 30 min of incubation
N85H/T95A
-
the mutant shows lower specific activity with 2-chlorobenzaldehyde plus cyanide than the wild type at pH 3.5 and 25 C for 30 min of incubation
N85Q
-
the mutant shows lower specific activity with 2-chlorobenzaldehyde plus cyanide than the wild type at pH 3.5 and 25 C for 30 min of incubation
N85Y
-
the mutant shows lower specific activity with 2-chlorobenzaldehyde plus cyanide (91% conversion with 98.2% ee of the product) than the wild type at pH 3.5 and 25 C for 30 min of incubation
N85Y/T95A
-
the mutant shows lower specific activity with 2-chlorobenzaldehyde plus cyanide than the wild type at pH 3.5 and 25 C for 30 min of incubation
T95A
-
the mutant shows higher specific activity with 2-chlorobenzaldehyde plus cyanide than the wild type at pH 3.5 and 25 C for 30 min of incubation
W109H
-
the mutant shows lower specific activity with 2-chlorobenzaldehyde plus cyanide than the wild type at pH 3.5 and 25 C for 30 min of incubation
N105Q
the mutant enzyme shows much lower thermostability, pH stability, and organic solvent tolerance than the hydroxynitrile lyase from leaves and that expressed in Pichia pastoris. kcat of the mutant enzyme is 1.3fold lower than the kcat of the wild-type enzyme, kcat/Km of the mutant enzyme is 2.3fold lower than the kcat/Km of the wild type enzyme from leaves
I108M/A111G
-
mutant with improved catalytic properties: recovery of a 89.9% yield of (R)-2-chloromandelonitrile with an enantiomeric excess of 97.6% enantiomeric excess, about 4% residual aldehyde. The mutant also contains two silent mutations at position 85 and position 432
L1Q/A111G
-
activity is similar to wild-type enzyme with its preferred substrate benzaldehyde. Directed evolution of PaHNL5/L1Q/A11G
L1Q/N3I/I108M/A111G
-
mutant with improved catalytic properties: recovery of a 92.7% yield of (R)-2-chloromandelonitrile with an ee of 98.6% enantiomeric excess, about 2% residual aldehyde, the mutant also contains two silent mutations at position 85 and position 432
L331A
the mutant shows increased conversion of 2,2-dimethyl-4H-1,3-benzodioxine-6-carbaldehyde compared to the wild type enzyme
L343F
the mutant shows significantly enhanced acid tolerance and higher specific activity than the wild type enzyme. L343F exhibits a half-life of 112 h at pH 2.5, showing stability much higher than that of the wild type (19.7 h)
L343I
the mutant shows significantly enhanced acid tolerance and higher specific activity than the wild type enzyme. L343I exhibits a half-life of 43 h at pH 2.5, showing stability higher than that of the wild type (19.7 h)
additional information
additional information
fusion of enzyme to different fluorescent reporter proteins. All fusion constructs retain enzymatic activity and fluorescence in vivo and in vitro, but show significant differences in activity and pH stability. Flavin-based fluorescent reporter fusions show almost 2 orders of magnitude-increased half-lives in the weakly acidic pH range compared to findings for the wild-type enzyme. This increased stability is apparently caused by oligomerization mediated via the flavin-based tag. The increased stability of the fusion proteins enables the efficient synthesis of (R)-mandelonitrile in an aqueous-organic two-phase system at a pH below 5
additional information
-
fusion of enzyme to different fluorescent reporter proteins. All fusion constructs retain enzymatic activity and fluorescence in vivo and in vitro, but show significant differences in activity and pH stability. Flavin-based fluorescent reporter fusions show almost 2 orders of magnitude-increased half-lives in the weakly acidic pH range compared to findings for the wild-type enzyme. This increased stability is apparently caused by oligomerization mediated via the flavin-based tag. The increased stability of the fusion proteins enables the efficient synthesis of (R)-mandelonitrile in an aqueous-organic two-phase system at a pH below 5
additional information
design of a surface-modified variant incorporating 11 changes in the amino acids on the protein surface to stabilze the protein at acidic pH. Mutant shows a broadened pH optimum towards the acidic range, along with enhancement of activity by up to twofold and significantly increased pH- and thermostabilities. The effect is probably due to a shift of the isoelectic point from pH 5.1 to 4.8. Mutant is applicable in aqueous/organic two-phase systems
additional information
-
design of a surface-modified variant incorporating 11 changes in the amino acids on the protein surface to stabilze the protein at acidic pH. Mutant shows a broadened pH optimum towards the acidic range, along with enhancement of activity by up to twofold and significantly increased pH- and thermostabilities. The effect is probably due to a shift of the isoelectic point from pH 5.1 to 4.8. Mutant is applicable in aqueous/organic two-phase systems
additional information
-
directed evolution of PaHNL5/L1Q/A11G (a mutant with activity is similar to wild-type enzyme with its preferred substrate benzaldehyde). 10000 transformants are screened for cleavage or synthesis of (R)-2-chloromandelonitrile
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.4
-
at pH 2.4 the free enzyme loses activity within hours, whereas the activity of CLEA-immobilized enzyme is retained for at least 504 h (3 weeks)
2.5
2.5 - 5.5
-
in the pH range of 2.5-3.5, recombinant enzyme from Pichia pastoris is more stable than the one expressed in E. coli (55-60% retaining activity), displaying 80% remaining activity after 1 h of incubation. Recombinant enzyme from Pichia pastoris shows stable activity compared to recombinant enzyme from Escherichia coli in the pH range of 4.0-5.5
3 - 10.5
-
after 1h incubation at 2°C, the enzyme retains activity over the pH range of 3.0-10.5
3.5 - 10
3.5 - 8
4.75
wild-type, half-life 2.2 min, flavin-based fluorescent reporter fusion protein half-life 55-95 min
5.4
-
half-life time: 2 h, the deactivation of the enzyme at slightly acidic pH is a result of pronounced structural unfolding
6
20°C, wild-type, half-life 60 h, surface-modified mutant, half-life 52.2 h
2.5
8°C, 72 h, more than 50% of activity retains
2.5
8°C, 72 h, more than 50% of activity retained
2.5
8°C, 72 h, more than 50% of activity is retained
3.5 - 10
activities of all the hydroxynitrile lyase are broadly stable over the range from pH 3.5 to 10.0, although the activity of hydroxynitrile lyase expressed in Escherichia coli is reduced to 60% and 70% at pH 7.0 and 10.0, respectively
3.5 - 10
the enzyme is broadly stable over the range of 3.5 to 10 after preincubation at 30°C for 1 h without substrate
3.5 - 8
-
isoform HNL-L shows high stability in the pH range of 3.5-8.0 for 30 min
4
8°C, 72 h, more than 50% of activity retains
4
8°C, 72 h, more than 50% of activity retained
4
8°C, 72 h, more than 50% of activity is retained
4
Prunus pseudoarmeniaca
-
increasing the pH value above 4.0, the yield and ee are dramatically decreased due to the spontaneous chemical decomposition of the product
5
20°C, wild-type, half-life 0.16 h, surface-modified mutant, half-life 2.23 h
5
8°C, 72 h, more than 65% of activity retains
5
8°C, 72 h, more than 65% of activity retained
5
8°C, 72 h, more than 65% of activity is retained
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
pH 5.0, wild-type, half-life 18 min, surface-modified mutant, half-life 137 min
10
15 - 95
-
after 1 h incubation in 10 mM potassium phosphate buffer (pH 7.0), the enzyme retains full activity between 15°C and 60°C. The enzyme almost loses its activity after 1 h incubation at 95°C
20
22
-
the relative activity of free enzyme decreases rapidly and depletes at the end of 15 days storage time while the immobilized hydroxynitrile lyases are very active at the same conditions with retained initial activities of 67% and 83% for hydroxynitrile lyase immobilized onto Eupergit CM and hydroxynitrile lyase immobilized onto Eupergit C 250 L, respectively. At the end of 30 days storage time, the corresponding retained activities are 48% and 71% for hydroxynitrile lyase immobilized onto Eupergit CM and hydroxynitrile lyase immobilized onto Eupergit C 250 L
25 - 50
Prunus pseudoarmeniaca
-
the half lives of free enzyme at 25 and 50°C are 49.9 and 30.5 h, respectively and these correspondingly are 96.3 and 43.6 h for immobilized enzyme onto Eupergit C, and 138.6 and 50.2 h for immobilized enzyme onto Eupergit C 250 L
30
30 - 50
1 h, stable, hydroxynitrile lyase from leaves, hydroxynitrile lyase expressed in Pichia pastoris, hydroxynitrile lyase expressed in Escherichia coli, hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris
30 - 80
-
both recombinant enzymes show 100% remaining activity at 30-55 C after 1 h of preincubation. In direct comparisons at 80 C, recombinant enzyme from Pichia pastoris exhibits 100% remaining activity and displays more stability than recombinant enzyme from Escherichia coli, which loses 50% of its activity under these conditions
37
4
-
the enzyme does not show any significant loss of activity at 4°C, hence it has good potential for industrial application
5 - 20
Prunus pseudoarmeniaca
-
free and immobilized enzyme preparations show optimal carboligation activity at 5°C. As the temperature is increased from 5 to 20°C, the yields decrease, however enantiomeric excess values (99%) unchange
5 - 55
-
isoform HNL-L shows high stability below 55°C for 30 min with more than 80% of the original activity retained
50
55
60
65
70
76
80
additional information
the hydroxynitrile lyase from leaves and that expressed in Pichia pastoris show much better thermostability, pH stability, and organic solvent tolerance than the deglycosylated enzyme expressed in Escherichia coli and the deglycosylated mutant N105Q expressed in Pichia pastoris
10
pH 5.0, wild-type, half-life 23.6 min, surface-modified mutant, half-life 136 min
20
pH 5.0, wild-type, half-life 9.6 min, surface-modified mutant, half-life 134 min
55
-
30 min, pH 6.0, without substrate, more than 80% of the original activity is retained
55
1 h, 10% loss of activity, hydroxynitrile lyase from leaves and hydroxynitrile lyase expressed in Pichia pastoris
60
1h, hydroxynitrile lyase from leaves loses 20% of its activity. Hydroxynitrile lyase expressed in Pichia pastoris loses 40% of its activity. Hydroxynitrile lyase expressed in Escherichia coli and hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris completely lose activity
60
the activity the enzyme from yellow cultivar remains above 80% after 1 h incubation at 60°C. The activity the enzyme from purple cultivar remains 40% after 1 h incubation at 60°C
65
in the pH-range 4-8 the Tm is constant at 76°C. At pH 9 and 10 the Tm values are slightly lower, 70°C and the lowest Tm of 65°C is measured at pH 3
70
1 h, hydroxynitrile lyase from leaves loses 60% of its activity, Hydroxynitrile lyase expressed in Pichia pastoris, completely loses activity
70
in the pH-range 4-8 the Tm is constant at 76°C. At pH 9 and 10 the Tm values are slightly lower, 70°C and the lowest Tm of 65°C is measured at pH 3
76
in the pH-range 4-8 the Tm is constant at 76°C. At pH 9 and 10 the Tm values are slightly lower, 70°C and the lowest Tm of 65°C is measured at pH 3
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
(R)-oxynitrilase immobilized as a cross-linked enzyme aggregate via precipitation with 1,2-dimethoxyethane and subsequent cross-linking using glutaraldehyde is stable and recyclable
-
at pH 4.5, the celite545-immobilized enzyme has reasonably good activity with 62% ee and 41% conversion of (S)-2-nitro-1-phenylethanol
both of immobilized enzymes (Eupergit C and Eupergit C250L) are used repeatedly 20times and the residual activities are about 97% of their initial activities
Prunus pseudoarmeniaca
-
C-terminally truncated enzyme HNLDELTA107 expressed in Escherichia coli is not glycosylated, and shows improved thermostability, solvent stability, and reusability similar to that of the wild-type glycosylated form of enzyme expressed in Pichia pastoris
crosslinked enzyme aggregates result in significant enhancement of the biocatalyst stability under acidic conditions (activity is retained after 168 h at pH 2.4)
-
enzyme immobilized on wet EziG Opal remains stable for 7 reaction cycles. Conversion of 74% and enantioselectivity of 89% respectively are achieved after 12 h of continuous operation
the cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase can be reused several times without loss of enantioselectivity
-
the enzyme is stable without the substrate but is remarkably unstable upon incubation with benzaldehyde and KCN
-
the fusion protein of Arabidopsis thaliana hydroxynitrile lyase and a family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi and a fluorescent reporter module protein shows increases stability at weakly acidic pH values, which is further increased by immobilization
the immobilized enzyme preparations (immobilized onto Eupergit CM and Eupergit C 250 L supports) are successfully reused 10times without loss of activity and enantioselectivity
-
the presence of glycan can prevent the self-degradation of this enzyme at 10°C
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
butyl acetate
dibutyl ether
diethyl ether
diisopropyl ether
Ethyl acetate
hexane
methyl-tert-butylether
toluene
the highest enenatiomeric excess is observed in toluene, i.e., 99% and about 38% conversion
additional information
-
effect of different organic solvents on the hydrocyanation of acetophenone tested
butyl acetate
synthesis of (R)-beta-nitro alcohols, highest enantioselectivity is obtained with n-butyl acetate as solvent with an optimum aqueous phase content of 50% (v/v)
butyl acetate
the highest 42.2% conversion is observed in n-butyl acetate with 98% ee of (S)-2-nitro-1-phenylethanol. The highest conversion and enantiomeric excess is obtained in 55% (w/v) n-butyl acetate, while it decreases beyond 75% (w/v)
dibutyl ether
-
EjHNL is very stable in ethyl acetate, diethyl ether, methyl-tert-butyl ether, diisopropyl ether, dibutyl ether and hexane for 12 h. The best solvent for the highest initial velocity and enantiomeric excess is diethyl ether with an optimum aqueous phase content of 50% (v/v)
dibutyl ether
-
more than 80% residual activity after incubation for 12 h in the system of methyl-tert-butyl ether, dibutyl ether, hexane, and diisopropyl ether while diethyl ether and ethyl acetate are not suitable solvents
diethyl ether
-
EjHNL is very stable in ethyl acetate, diethyl ether, methyl-tert-butyl ether, diisopropyl ether, dibutyl ether and hexane for 12 h. The best solvent for the highest initial velocity and enantiomeric excess is diethyl ether with an optimum aqueous phase content of 50% (v/v)
diethyl ether
-
more than 80% residual activity after incubation for 12 h in the system of methyl-tert-butyl ether, dibutyl ether, hexane, and diisopropyl ether while diethyl ether and ethyl acetate are not suitable solvents
diisopropyl ether
-
EjHNL is very stable in ethyl acetate, diethyl ether, methyl-tert-butyl ether, diisopropyl ether, dibutyl ether and hexane for 12 h. The best solvent for the highest initial velocity and enantiomeric excess is diethyl ether with an optimum aqueous phase content of 50% (v/v)
diisopropyl ether
-
more than 80% residual activity after incubation for 12 h in the system of methyl-tert-butyl ether, dibutyl ether, hexane, and diisopropyl ether while diethyl ether and ethyl acetate are not suitable solvents
Ethyl acetate
-
EjHNL is very stable in ethyl acetate, diethyl ether, methyl-tert-butyl ether, diisopropyl ether, dibutyl ether and hexane for 12 h. The best solvent for the highest initial velocity and enantiomeric excess is diethyl ether with an optimum aqueous phase content of 50% (v/v)
Ethyl acetate
-
more than 80% residual activity after incubation for 12 h in the system of methyl-tert-butyl ether, dibutyl ether, hexane, and diisopropyl ether while diethyl ether and ethyl acetate are not suitable solvents
hexane
-
EjHNL is very stable in ethyl acetate, diethyl ether, methyl-tert-butyl ether, diisopropyl ether, dibutyl ether and hexane for 12 h. The best solvent for the highest initial velocity and enantiomeric excess is diethyl ether with an optimum aqueous phase content of 50% (v/v)
hexane
-
more than 80% residual activity after incubation for 12 h in the system of methyl-tert-butyl ether, dibutyl ether, hexane, and diisopropyl ether while diethyl ether and ethyl acetate are not suitable solvents
methyl-tert-butylether
-
EjHNL is very stable in ethyl acetate, diethyl ether, methyl-tert-butyl ether, diisopropyl ether, dibutyl ether and hexane for 12 h. The best solvent for the highest initial velocity and enantiomeric excess is diethyl ether with an optimum aqueous phase content of 50% (v/v)
methyl-tert-butylether
-
more than 80% residual activity after incubation for 12 h in the system of methyl-tert-butyl ether, dibutyl ether, hexane, and diisopropyl ether while diethyl ether and ethyl acetate are not suitable solvents
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
10°C, 12 h, the stabilities of hydroxynitrile lyase from leaves and hydroxynitrile lyase expressed in Pichia pastoris are comparable, with remaining enzyme activities of 60-94%. The activities of hydroxynitrile lyase mutant N105Q expressed in Pichia pastor and hydroxynitrile lyase expressed in Escherichia coli vary between 70% and 0% in all biphasic systems apart from those with DEE and DIPE. The nonglycosylated hydroxynitrile lyase expressed in Escherichia coli and hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris both lose 50% of their activity in aqueous buffer with shaking at 1500 rpm at 10°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Ni Sepharose column chromatography
ammonium sulfate precipitation, DEAE Toyopearl column chromatography, phenyl Toyopearl column chromatography, and Superdex 200 gel filtration
ammonium sulfate precipitation, DEAE-Toyopearl column chromatography, butyl-Toyopearl column chromatography, and GigaCapQ-Toyopearl column chromatography
-
butyl-Toyopearl column chromatography, Toyopearl DEAE-650M column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
partly, as crosslinked enzyme aggregates. Optimal conditions are initial glutaraldehyde concentration of 25% w/v, ammonium sulfate saturation concentration of 43% w/v, and crosslinking time of 18 h
-
the fused family 2 carbohydrate-binding module enables the purification and simultaneous immobilization of Arabidopsis thaliana hydroxynitrile lyase on various cellulosic carrier materials
to homogeneity. The final yield, of 36% with 49fold purification, is obtained by 30-80% (NH4)2SO4 fractionation and column chromatography on DEAE-Toyopearl and concanavalin A Sepharose 4B, which suggests the presence of a carbohydrate side chain
Toyopearl butyl-650M column chromatography, Mono Q column chromatography, and Resource phenyl column chromatography
-
Toyopearl butyl-650M column chromatography, MonoQ column chromatography, and Superdex 200 gel filtration
-
Toyopearl butyl-650M column chromatography, Toyopearl DEAE-650M column chromatography, Q Sepharose column chromatography, and Superdex 75gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Arabidopsis thaliana hydroxynitrile lyase fused to family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi and to a fluorescent reporter module
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli SHuffle T7 and Pichia pastoris GS115 cells
-
expressed in Escherichia coli Shuffle T7 cells
expressed in Pichia pastoris strain GS115
expression in Escherichia coli
expression in Escherichia coli. Recombinant production of DtHNL1 in Komagataella phaffii under control of the strong and tightly regulated AOX1 promoter. Two different shuttle vectors are used, pPpT4_S and pPpB1, to obtain strains with optimal gene copy numbers for efficient heterologous expression
-
heterologously expression of the His-tagged hydroxynitrile lyase isoenzymes (HNL1, HNL2, HNL4 and HNL5) in Pichia pastoris
-
mutant V317A of hydroxynitrile lyase isoenzyme 5 is expressed in Aspergillus niger
the enzyme is cloned and expressed in Escherichia coli BL21(DE3) and Pichia pastoris GS115 cells without a signal peptide sequence
the highly glycosylated Prunus amygdalus HNL isoenzyme 5 (PaHNL5 V317A) is expressed in Aspergillus niger. The recombinant protein is highly glycosylated as confirmed by SDS-page and mass spectrometry
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced in response to spider mite (Tetranychus urticae) infestation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
pharmacology
synthesis
agriculture
-
hydroxynitrile lyases are involved in the synthesis of enantiomerically pure cyanohydrins which are important intermediates in the production of pharmaceuticals and agrochemicals. The enzyme synthesizes (R)-mandelonitrile in both, batch reaction and fed-batch reaction and can be effectively used in the synthesis of (R)-mandelonitrile
agriculture
-
the enzyme has very high potential for synthesis of cyanohydrins and can be used for the production of enantiopure cyanohydrins. Cyanohydrins are important intermediates in the production of pharmaceuticals and agrochemicals
pharmacology
-
hydroxynitrile lyases are involved in the synthesis of enantiomerically pure cyanohydrins which are important intermediates in the production of pharmaceuticals and agrochemicals. The enzyme synthesizes (R)-mandelonitrile in both, batch reaction and fed-batch reaction and can be effectively used in the synthesis of (R)-mandelonitrile
pharmacology
-
the enzyme has very high potential for synthesis of cyanohydrins and can be used for the production of enantiopure cyanohydrins. Cyanohydrins are important intermediates in the production of pharmaceuticals and agrochemicals
synthesis
-
(R)-oxynitrilase immobilized as a cross-linked enzyme aggregate via precipitation with 1,2-dimethoxyethane and subsequent cross-linking using glutaraldehyde is stable and recyclable. Application in microaqueous medium, superior biocatalyst for the enantioselective hydrocyanation of slow-reacting aldehydes
synthesis
-
used as a catalyst in the preparation of optically active cyanohydrins
synthesis
-
production of (R)-hydroxypivalaldehyde cyanohydrin, the chiral key precursor in hydroxynitrile lyase based (R)-pantlactone synthesis
synthesis
development and validation of a process model for production of (R)-cyanohydrins in an aqueous-organic biphasic-stirred tank reactor with an unknown interfacial area operated in batch mode. The formation of (R)-mandelonitrile from benzaldehyde and cyanide catalyzed by Prunus amygdalus hydroxynitrile lyase is chosen as a model reaction. Methyl tert-butyl ether is selected as the organic solvent and the reaction conditions are 5°C and pH 5.5 at which the nonenzymatic reaction towards rac-mandelonitrile is largely suppressed
synthesis
hydroxynitrile lyases are proficient biocatalysts for the stereospecific synthesis of cyanohydrins
synthesis
-
optically active cyanohydrins are expedient starting materials for preparation of alpha-hydroxyketones, alpha-hydroxy acids, beta-aminoalcohols, aminonitriles and aziridines
synthesis
-
optically active cyanoydrins are expedient starting materials for preparation of alpha-hydroxyketones, alpha-hydroxy acids, beta-aminoalcohols, aminonitriles and aziridines
synthesis
synthesis of (R)-beta-nitro alcohols using nitromethane as donor. Highest enantioselectivity is obtained with n-butyl acetate as solvent with an optimum aqueous phase content of 50% (v/v)
synthesis
-
the immobilization of partially purified hydroxynitrile lyase from Prunus dulcis as crosslinked enzyme aggregate is a very promising tool owing to its ease of preparation, cheapness, and efficiency in the preparation of enantiopure cyanohydrins. Response surface methodology provides an effective way for the optimization of the preparation of PdHNL-crosslinked enzyme aggregate. The synthesis of (R)-mandelonitrile, (R)-2-chloromandelonitrile, (R)-3,4-dihydroxymandelonitrile, (R)-2-hydroxy-4-phenyl butyronitrile, (R)-4-bromomandelonitrile, (R)-4-fluoromandelonitrile, and (R)-4-nitromandelonitrile is achieved with high yield and enantiomeric excess
synthesis
fusion of enzyme to different fluorescent reporter proteins. Flavin-based fluorescent reporter fusions convert 95% benzaldehyde to (R)-mandelonitrile within 60 min at pH 4.75, with 96% enantiomeric excess
synthesis
the high specific activity toward benzaldehyde along with wide temperature, pH stabilities and high enantioselectivity in the synthesis of various cyanohydrins make this enzyme suitable as an industrial biocatalyst
synthesis
-
the enzyme is a powerful and cheap biocatalyst in the synthesis of (R)-mandelonitrile and may be used in combination with nitrilases to produce enantiopure mandelic acids
synthesis
an easy one-step immobilization of a complex Arabidopsis thaliana hydroxynitrile lyase fusion protein is possible starting from an Escherichia coli crude cell extract (producing a carbohydrate-binding module-containing fusion protein) and cost efficient cellulosic carrier materials. Highly-specific site-selective immobilization of the target protein is achieved by fusing the family 2 carbohydrate-binding module of the exoglucanase/xylanase Cex from Cellulomonas fimi to the target enzyme. This yields a cheap, active, stable and recyclable immobilizate, which can be employed in micro-aqueous reaction systems to enable enantiopure cyanohydrin synthesis
synthesis
-
the enzyme may find application as a biocatalyst for the synthesis of enantiomerically pure cyanohydrins. DtHNL1-CLEA preparation results in a more robust biocatalyst under acidic conditions, which is an interesting feature for the efficient production of enantiomerically pure cyanohydrins
synthesis
-
Amygdalus pedunculata hydroxynitrile lyase is an excellent biocatalyst and has very high potential for synthesis of enantiopure cyanohydrins
synthesis
-
hydroxynitrile lyases are involved in the synthesis of enantiomerically pure cyanohydrins which are important intermediates in the production of pharmaceuticals and agrochemicals. The enzyme synthesizes (R)-mandelonitrile in both, batch reaction and fed-batch reaction and can be effectively used in the synthesis of (R)-mandelonitrile
synthesis
-
the enzyme has very high potential for synthesis of cyanohydrins and can be used for the production of enantiopure cyanohydrins. Cyanohydrins are important intermediates in the production of pharmaceuticals and agrochemicals
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wajant, H.; Foerster, S.; Selmar, D.; Effenberger, F.; Pfizenmaier, K.
Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum
Plant Physiol.
109
1231-1238
1995
Phlebodium aureum, Prunus dulcis (O24243)
brenda
Lauble, H.; Mueller, K.; Schindellin, H.; Foerster, S.; Effenberger, F.
Crystallization and preliminary X-ray diffraction studies of mandelonitrile lyase from almonds
Proteins Struct. Funct. Genet.
19
343-347
1994
Prunus dulcis
brenda
Zheng, L.; Poulton, J.E.
Temporal and spatial expression of amygdalin hydrolase and (R)-(+)-mandelonitrile lyase in black cherry seeds
Plant Physiol.
109
31-39
1995
Prunus serotina (P52706), Prunus serotina
brenda
Effenberger, F.; Foerster, S.; Wajant, H.
Hydroxynitrile lyases in stereoselective catalysis
Curr. Opin. Biotechnol.
11
532-539
2000
Prunus sp.
brenda
Willeman, W.F.; Hanefeld, U.; Straathof, A.J.J.; Heijnen, J.J.
Estimation of kinetic parameters by progress curve analysis for the synthesis of (R)-mandelonitrile by Prunus amygdalus hydroxynitrile lyase
Enzyme Microb. Technol.
27
423-433
2000
Prunus dulcis
brenda
de Gonzalo, G.; Brieva, R.; Gotor, V.
(R)-Oxynitrilase-catalyzed transformation of omega-hydroxyalkanals
J. Mol. Catal. B
19-20
223-230
2002
Prunus dulcis
-
brenda
Dreveny, I.; Kratky, C.; Gruber, K.
The active site of hydroxynitrile lyase from Prunus amygdalus: modeling studies provide new insights into the mechanism of cyanogenesis
Protein Sci.
11
292-300
2002
Prunus dulcis
brenda
Dreveny, I.; Gruber, K.; Glieder, A.; Thompson, A.; Kratky, C.
The hydroxynitrile L-lyase from almond: A lyase that looks like an oxidoreductase
Structure
9
803-815
2001
Prunus dulcis (O24243), Prunus dulcis
brenda
Lin, G.; Han, S.; Li, Z.
Enzymic synthesis of (R)-cyanohydrins by three (R)-oxynitrilase sources in micro-aqueous organic medium
Tetrahedron
55
3531-3540
1999
Prunus armeniaca, Prunus persica, Eriobotrya japonica
-
brenda
Bianchi, P.; Roda, G.; Riva, S.; Danieli, B.; Zabelinskaja-Mackova, A.; Griengl, H.
On the selectivity of oxynitrilases towards alpha-oxygenated aldehydes
Tetrahedron
57
2213-2220
2001
Prunus dulcis
-
brenda
Huang, S.R.; Liu, S.L.; Zong, M.H.; Xu, R.
Synthesis of (R)-2-trimethylsilyl-2-hydroxyl-ethylcyanide catalyzed with (R)-oxynitrilase from loquat seed meal
Biotechnol. Lett.
27
79-82
2005
Eriobotrya japonica
brenda
Weis, R.; Poechlauer, P.; Bona, R.; Skranc, W.; Luiten, R.; Wubbolts, M.; Schwab, H.; Glieder, A.
Biocatalytic conversion of unnatural substrates by recombinant almond R-HNL isoenzyme 5
J. Mol. Catal. B
29
211-218
2004
Prunus dulcis
-
brenda
van Langen, L.M.; Selassa, R.P.; van Rantwijk, F.; Sheldon, R.A.
Cross-linked aggregates of (R)-oxynitrilase: a stable, recyclable biocatalyst for enantioselective hydrocyanation
Org. Lett.
7
327-329
2005
Prunus dulcis
brenda
Gaisberger, R.P.; Fechter, M.H.; Griengl, H.
The first hydroxynitrile lyase catalysed cyanohydrin formation in ionic liquids
Tetrahedron
15
2959-2963
2004
Prunus dulcis
-
brenda
Kobler, C.; Bohrer, A.; Effenberger, F.
Hydroxynitrile lyase-catalyzed addition of HCN to 2- and 3-substituted cyclohexanones
Tetrahedron
60
10397-10410
2004
Prunus dulcis
-
brenda
Solis, A.; Luna, H.; Manjarrez, N.; Perez, H.I.
Study on the (R)-oxynitrilase activity of Pouteria sapota
Tetrahedron
60
10427-10431
2004
Pouteria sapota
-
brenda
Nanda, S.; Kato, Y.; Asano, Y.
A new (R)-hydroxynitrile lyase from Prunus mume: asymmetric synthesis of cyanohydrins
Tetrahedron
61
10908-10916
2005
Prunus mume
-
brenda
Ueatrongchit, T.; Kayo, A.; Komeda, H.; Asano, Y.; H-Kittikun, A.
Purification and characterization of a novel (R)-hydroxynitrile lyase from Eriobotrya japonica (Loquat)
Biosci. Biotechnol. Biochem.
72
1513-1522
2008
Eriobotrya japonica (B7VF77)
brenda
Liu, Z.; Pscheidt, B.; Avi, M.; Gaisberger, R.; Hartner, F.S.; Schuster, C.; Skranc, W.; Gruber, K.; Glieder, A.
Laboratory evolved biocatalysts for stereoselective syntheses of substituted benzaldehyde cyanohydrins
Chembiochem
9
58-61
2008
Prunus dulcis
brenda
Pscheidt, B.; Avi, M.; Gaisberger, R.; Hartner, F.S.; Skranc, W.; Glieder, A.
Screening hydroxynitrile lyases for (R)-pantolactone synthesis
J. Mol. Catal. B
52-53
183-188
2008
Prunus dulcis
-
brenda
Fang, F.; Ji, A.; Meng, Z.
Biosynthesis of chiral methyl ketone cyanohydrins catalyzed by oxynitrilase in Chaenomeles speciosa seed meal
React. Kinet. Catal. Lett.
93
233-239
2008
Chaenomeles speciosa
-
brenda
Andexer, J.; von Langermann, J.; Mell, A.; Bocola, M.; Kragl, U.; Eggert, T.; Pohl, M.
An R-selective hydroxynitrile lyase from Arabidopsis thaliana with an alpha/beta-hydrolase fold
Angew. Chem. Int. Ed. Engl.
46
8679-8681
2007
Arabidopsis thaliana (Q9LFT6), Arabidopsis thaliana
brenda
Dreveny, I.; Andryushkova, A.S.; Glieder, A.; Gruber, K.; Kratky, C.
Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity
Biochemistry
48
3370-3377
2009
Prunus dulcis (O24243)
brenda
Willeman, W.F.; Gerrits, P.J.; Hanefeld, U.; Brussee, J.; Straathof, A.J.; van der Gen, A.; Heijnen, J.J.
Development of a process model to describe the synthesis of (R)-mandelonitrile by Prunus amygdalus hydroxynitrile lyase in an aqueous-organic biphasic reactor
Biotechnol. Bioeng.
77
239-247
2002
Prunus dulcis (O24243)
brenda
Fechter, M.H.; Gruber, K.; Avi, M.; Skranc, W.; Schuster, C.; Pchlauer, P.; Klepp, K.O.; Griengl, H.
Stereoselective biocatalytic synthesis of (S)-2-hydroxy-2-methylbutyric acid via substrate engineering by using "thio-disguised" precursors and oxynitrilase catalysis
Chemistry
13
3369-3376
2007
Prunus dulcis
brenda
Ueatrongchit, T.; Tamura, K.; Ohmiya, T.; H-Kittikun, A.; Asano, Y.
Hydroxynitrile lyase from Passiflora edulis. Purification, characteristics and application in asymmetric synthesis of (R)-mandelonitrile
Enzyme Microb. Technol.
46
456-465
2010
Passiflora edulis
brenda
Guterl, J.K.
Andexer, J.N.; Sehl, T.; von Langermann, J.; Frindi-Wosch, I.; Rosenkranz, T.; Fitter, J.; Gruber, K.; Kragl, U.; Eggert, T.; Pohl, M.: Uneven twins: comparison of two enantiocomplementary hydroxynitrile lyases with alpha/beta-hydrolase fold
J. Biotechnol.
141
166-173
2009
Arabidopsis thaliana
brenda
Ueatrongchit, T.; Komeda, H.; Asano, Y.; H-Kittikun, A.
Parameters influencing asymmetric synthesis of (R)-mandelonitrile by a novel (R)-hydroxynitrile lyase from Eriobotrya japonica
J. Mol. Catal. B
56
208-214
2009
Eriobotrya japonica
-
brenda
Suelves, M.; Puigdomenech, P.
Molecular cloning of the cDNA coding for the (R)-(+)-mandelonitrile lyase of Prunus amygdalus: temporal and spatial expression patterns in flowers and mature seeds
Planta
206
388-393
1998
Prunus dulcis (O24243), Prunus dulcis
brenda
Roda, G.; Riva, S.; Danieli, B.
Almond oxynitrilase-catalyzed transformation of aldehydes is strongly influenced by naphthyl and alkoxy substituents
Tetrahedron
10
3939-3949
1999
Prunus dulcis
-
brenda
Fukuta, Y.; Nanda, S.; Kato, Y.; Yurimoto, H.; Sakai, Y.; Komeda, H.; Asano, Y.
Characterization of a new (R)-hydroxynitrile lyase from the Japanese apricot Prunus mume and cDNA cloning and secretory expression of one of the isozymes in Pichia pastoris
Biosci. Biotechnol. Biochem.
75
214-220
2011
Prunus mume, Prunus mume (B9X0I2), Prunus mume (B9X0I1)
brenda
Fuhshuku, K.; Asano, Y.
Synthesis of (R)-beta-nitro alcohols catalyzed by R-selective hydroxynitrile lyase from Arabidopsis thaliana in the aqueous-organic biphasic system
J. Biotechnol.
153
153-159
2011
Arabidopsis thaliana, Arabidopsis thaliana (Q9LFT6)
brenda
Tuekel, S.; Yildirim, D.; Alagoez, D.; Alptekin, O.; Yuecebilgi, G.; Bilgin, R.
Partial purification and immobilization of a new (R)-hydroxynitrile lyase from seeds of Prunus pseudoarmeniaca
J. Mol. Catal. B
66
161-165
2010
Prunus pseudoarmeniaca
-
brenda
Liu, S.; Zong, M.
(R)-oxynitrilase from Prunus salicina catalysed synthesis of (R)-ketone-cyanohydrin by enantioselective transcyanation
Prog. Biochem. Biophys.
37
1212-1216
2010
Prunus salicina
-
brenda
Hussain, Z.; Wiedner, R.; Steiner, K.; Hajek, T.; Avi, M.; Hecher, B.; Sessitsch, A.; Schwab, H.
Characterization of two bacterial hydroxynitrile lyases with high similarity to cupin superfamily proteins
Appl. Environ. Microbiol.
78
2053-2055
2012
endophytic bacterium Psm-BT4509 (G9DE15)
brenda
Scholz, K.E.; Kopka, B.; Wirtz, A.; Pohl, M.; Jaeger, K.E.; Krauss, U.
Fusion of a flavin-based fluorescent protein to hydroxynitrile lyase from Arabidopsis thaliana improves enzyme stability
Appl. Environ. Microbiol.
79
4727-4733
2013
Arabidopsis thaliana (Q9LFT6), Arabidopsis thaliana
brenda
Yildirim, D.; Tuekel, S.S.; Alagoez, D.
Crosslinked enzyme aggregates of hydroxynitrile lyase partially purified from Prunus dulcis seeds and its application for the synthesis of enantiopure cyanohydrins
Biotechnol. Prog.
30
818-827
2014
Prunus dulcis
brenda
Andexer, J.N.; Staunig, N.; Eggert, T.; Kratky, C.; Pohl, M.; Gruber, K.
Hydroxynitrile lyases with alpha/beta-hydrolase fold: two enzymes with almost identical 3D structures but opposite enantioselectivities and different reaction mechanisms
ChemBioChem
13
1932-1939
2012
Arabidopsis thaliana (Q9LFT6), Arabidopsis thaliana
brenda
Okrob, D.; Metzner, J.; Wiechert, W.; Gruber, K.; Pohl, M.
Tailoring a stabilized variant of hydroxynitrile lyase from Arabidopsis thaliana
ChemBioChem
13
797-802
2012
Arabidopsis thaliana (Q9LFT6), Arabidopsis thaliana
brenda
Hajnal, I.; Lyskowski, A.; Hanefeld, U.; Gruber, K.; Schwab, H.; Steiner, K.
Biochemical and structural characterization of a novel bacterial manganese-dependent hydroxynitrile lyase
FEBS J.
280
5815-5828
2013
Granulicella tundricola (E8WYN5), Granulicella tundricola MP5ACTX9 (E8WYN5)
brenda
Alagz, D.; Tkel, S.; Yildirim, D.
Purification, immobilization and characterization of (R)-hydroxynitrile lyase from Prunus amygdalus turcomanica seeds and their applicability for synthesis of enantiopure cyanohydrins
J. Mol. Catal. B
101
40-46
2014
Prunus turcomanica
-
brenda
Zheng, Y.; Xu, J.; Wang, H.; Lin, G.; Hong, R.; Yu, H.
Hydroxynitrile lyase isozymes from Prunus communis identification, characterization and synthetic applications
Adv. Synth. Catal.
359
1185-1193
2017
Prunus dulcis
-
brenda
Alagoez, D.; Tuekel, S.S.; Yildirim, D.
Enantioselective synthesis of various cyanohydrins using covalently immobilized preparations of hydroxynitrile lyase from Prunus dulcis
Appl. Biochem. Biotechnol.
177
1348-1363
2015
Prunus dulcis
brenda
Isobe, K.; Kitagawa, A.; Kanamori, K.; Kashiwagi, N.; Matsui, D.; Yamaguchi, T.; Fuhshuku, K.I.; Semba, H.; Asano, Y.
Characterization of a novel hydroxynitrile lyase from Nandina domestica Thunb
Biosci. Biotechnol. Biochem.
82
1760-1769
2018
Nandina domestica
brenda
Kopka, B.; Diener, M.; Wirtz, A.; Pohl, M.; Jaeger, K.E.; Krauss, U.
Purification and simultaneous immobilization of Arabidopsis thaliana hydroxynitrile lyase using a family 2 carbohydrate-binding module
Biotechnol. J.
10
811-819
2015
Arabidopsis thaliana (Q9LFT6)
brenda
Asif, M.; Bhalla, T.C.
Hydroxynitrile lyase of wild apricot (Prunus armeniaca L.) purification, characterization and application in synthesis of enantiopure mandelonitrile
Catal. Lett.
146
1118-1127
2017
Prunus armeniaca
-
brenda
Asif, M.; Bhalla, T.C.
Enantiopure synthesis of (R)-mandelonitrile Using Hydroxynitrile lyase of wild apricot (Prunus armeniaca L.) [ParsHNL] in aqueous/organic biphasic system
Catal. Lett.
147
1592-1597
2017
Prunus armeniaca
-
brenda
Nuylert, A.; Ishida, Y.; Asano, Y.
Effect of glycosylation on the biocatalytic properties of hydroxynitrile lyase from the Passion Fruit, Passiflora edulis A comparison of natural and recombinant enzymes
ChemBioChem
18
257-265
2017
Passiflora edulis (A0A1L7NZN4)
brenda
Lanfranchi, E.; Grill, B.; Raghoebar, Z.; Van Pelt, S.; Sheldon, R.A.; Steiner, K.; Glieder, A.; Winkler, M.
Production of hydroxynitrile Lyase from Davallia tyermannii (DtHNL) in Komagataella phaffii and its immobilization as a CLEA to generate a robust biocatalyst
ChemBioChem
19
312-316
2018
Davallia tyermanii
brenda
Motojima, F.; Nuylert, A.; Asano, Y.
The crystal structure and catalytic mechanism of hydroxynitrile lyase from passion fruit, Passiflora edulis
FEBS J.
285
313-324
2018
Passiflora edulis (A0A1L7NZN4), Passiflora edulis
brenda
Yao, L.; Li, H.; Yang, J.; Li, C.; Shen, Y.
Purification and characterization of a hydroxynitrile lyase from Amygdalus pedunculata Pall
Int. J. Biol. Macromol.
118
189-194
2018
Prunus pedunculata
brenda
Pavkov-Keller, T.; Bakhuis, J.; Steinkellner, G.; Jolink, F.; Keijmel, E.; Birner-Gruenberger, R.; Gruber, K.
Structures of almond hydroxynitrile lyase isoenzyme 5 provide a rationale for the lack of oxidoreductase activity in flavin dependent HNLs
J. Biotechnol.
235
24-31
2016
Prunus dulcis (O24243), Prunus dulcis
brenda
Dadashipour, M.; Ishida, Y.; Yamamoto, K.; Asano, Y.
Discovery and molecular and biocatalytic properties of hydroxynitrile lyase from an invasive millipede, Chamberlinius hualienensis
Proc. Natl. Acad. Sci. USA
112
10605-10610
2015
Chamberlinius hualienensis (A0A0H5BR52)
brenda
Lanfranchi, E.; Pavkov-Keller, T.; Koehler, E.M.; Diepold, M.; Steiner, K.; Darnhofer, B.; Hartler, J.; Van Den Bergh, T.; Joosten, H.J.; Gruber-Khadjawi, M.; Thallinger, G.G.; Birner-Gruenberger, R.; Gruber, K.; Winkler, M.; Glieder, A.
Enzyme discovery beyond homology a unique hydroxynitrile lyase in the Bet v1 superfamily
Sci. Rep.
7
46738
2017
Davallia tyermanii (A0A1C9V3S9), Davallia tyermanii (A0A1C9V3R0), Davallia tyermanii (A0A1C9V3R4), Davallia tyermanii (A0A1C9V3R6)
brenda
Nuylert, A.; Nakabayashi, M.; Yamaguchi, T.; Asano, Y.
Discovery and structural analysis to improve the enantioselectivity of hydroxynitrile lyase from Parafontaria laminata millipedes for (R)-2-chloromandelonitrile synthesis
ACS Omega
5
27896-27908
2020
Parafontaria laminata
brenda
Rao, D.H.S.; Shivani, K.; Padhi, S.K.
Immobilized Arabidopsis thaliana hydroxynitrile lyase-catalyzed retro-Henry reaction in the synthesis of (S)-beta-nitroalcohols
Appl. Biochem. Biotechnol.
193
560-576
2021
Arabidopsis thaliana (Q9LFT6)
brenda
Solis, A.; Cano, A.; Martinez-Casares, R.; Solis-Oba, M.; Castro-Rivera, R.; Velazquez Flores, O.
Preparation of optically active cyanohydrins from 2-substituted benzaldehydes using a hydroxynitrile lyase from Pouteria sapota seeds immobilized on celite
Biocatal. Biotransform.
41
344-352
2022
Pouteria sapota
-
brenda
Vishnu Priya, B.; Sreenivasa Rao, D.H.; Gilani, R.; Lata, S.; Rai, N.; Akif, M.; Kumar Padhi, S.
Enzyme engineering improves catalytic efficiency and enantioselectivity of hydroxynitrile lyase for promiscuous retro-nitroaldolase activity
Bioorg. Chem.
120
105594
2022
Arabidopsis thaliana (Q9LFT6)
brenda
Mueller, E.; Sosedov, O.; Groening, J.A.D.; Stolz, A.
Synthesis of (R)-mandelic acid and (R)-mandelic acid amide by recombinant E. coli strains expressing a (R)-specific oxynitrilase and an arylacetonitrilase
Biotechnol. Lett.
43
287-296
2021
Arabidopsis thaliana
brenda
Coloma, J.; Lugtenburg, T.; Afendi, M.; Lazzarotto, M.; Bracco, P.; Hagedoorn, P.; Gardossi, L.; Hanefeld, U.
Immobilization of Arabidopsis thaliana hydroxynitrile lyase (AtHNL) on EziG opal
Catalysts
10
1-14
2020
Arabidopsis thaliana (Q9LFT6)
-
brenda
Nuylert, A.; Motojima, F.; Khanongnuch, C.; Hongpattarakere, T.; Asano, Y.
Stabilization of hydroxynitrile lyases from two variants of passion fruit, Passiflora edulis Sims and Passiflora edulis forma flavicarpa, by C-terminal truncation
ChemBioChem
21
181-189
2020
Passiflora edulis (A0A1L7NZN4)
brenda
Zheng, Y.C.; Ding, L.Y.; Jia, Q.; Lin, Z.; Hong, R.; Yu, H.L.; Xu, J.H.
A high-throughput screening method for the directed evolution of hydroxynitrile lyase towards cyanohydrin synthesis
ChemBioChem
22
996-1000
2021
Prunus dulcis (O24243)
brenda
Motojima, F.; Izumi, A.; Nuylert, A.; Zhai, Z.; Dadashipour, M.; Shichida, S.; Yamaguchi, T.; Nakano, S.; Asano, Y.
R-hydroxynitrile lyase from the cyanogenic millipede, Chamberlinius hualienensis - A new entry to the carrier protein family Lipocalines
FEBS J.
288
1679-1695
2021
Chamberlinius hualienensis (A0A0H5BR52)
brenda
Arnaiz, A.; Santamaria, M.E.; Rosa-Diaz, I.; Garcia, I.; Dixit, S.; Vallejos, S.; Gotor, C.; Martinez, M.; Grbic, V.; Diaz, I.
Hydroxynitrile lyase defends Arabidopsis against Tetranychus urticae
Plant Physiol.
189
2244-2258
2022
Arabidopsis thaliana (Q9LFT6)
brenda
Yamaguchi, T.; Nuylert, A.; Ina, A.; Tanabe, T.; Asano, Y.
Hydroxynitrile lyases from cyanogenic millipedes molecular cloning, heterologous expression, and whole-cell biocatalysis for the production of (R)-mandelonitrile
Sci. Rep.
8
3051
2018
Oxidus gracilis, Parafontaria tonominea, Nedyopus tambanus tambanus, Nedyopus tambanus mangaesinus
brenda
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