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(1S)-1-furan-2-yl-2-nitroethanol
furan-2-carbaldehyde + CH3NO2
-
enantiomeric excess: ~90%, yield: 60-70%
-
-
r
(1S)-2-nitro-1-(4-nitrophenyl)ethanol
4-nitrobenzaldehyde + CH3NO2
-
enantiomeric excess: ~90%, yield: 60-70%
-
-
r
(1S)-2-nitro-1-phenylethanol
benzaldehyde + CH3NO2
-
enantiomeric excess: ~90%, yield: 60-70%
-
-
r
(1S,2R)-2-nitro-1-phenyl-propanol
benzaldehyde + C2H5NO2
-
4 diastereomers, enantiomeric excess: 95%, yield: 67%
-
-
r
(2S)-1-nitrooctan-2-ol
heptanal + CH3NO2
-
enantiomeric excess: ~90%, yield: 60-70%
-
-
r
(2S)-2,3-dimethyl-2-hydroxybutyronitrile
?
binding mode of the chiral substrates is identical to that observed for the biological substrate 2-hydroxy-2-methylpropanenitrile (i.e. acetone cyanohydrin). Three-point binding mode of the substrates: hydrophobic pocket, hydrogen bonds between the hydroxyl group and Ser80 and Thr11, electrostatic interaction of the cyano group with Lys236
-
-
?
(2S)-2-hydroxy-2-methylbutanenitrile
cyanide + butan-2-one
(2S)-2-hydroxy-2-methylpentanenitrile
cyanide + pentan-2-one
-
-
-
?
(2S)-hydroxy(3-phenoxyphenyl)ethanenitrile
cyanide + 3-phenoxybenzaldehyde
-
-
-
r
(R)-2-(2-furyl)-2-hydroxyacetonitrile
furan-2-carbaldehyde + HCN
-
enantiomeric excess: > 99%, yield: 90%
-
-
r
(R)-mandelonitrile
cyanide + benzaldehyde
low activity
-
-
r
(S)-2-nitro-1-phenylethanol
benzaldehyde + nitromethane
-
-
-
-
r
(S)-2-nitro-1-phenylethanol
nitromethane + benzaldehyde + (R)-2-nitro-1-phenylethanol
-
besides the native cyanohydrins reaction, the enzyme also catalyzes the asymmetric reversible Henry reaction yielding (S)-beta-nitroalcohols with high enantiomeric excess. The catalyst productivity achieved during the resolution is 10times higher than that in the HNL-catalyzed synthesis of (S)-2-nitro-1-phenylethanol
-
-
r
(S)-3-phenoxybenzaldehyde cyanohydrin
m-phenoxybenzaldyhyde + HCN
-
enantiomeric excess: > 98.5%, yield: 95.5%, used for insecticide synthesis
-
-
r
(S)-mandelonitrile
benzaldehyde + HCN
(S)-mandelonitrile
cyanide + benzaldehyde
(S)-mandelonitrile
HCN + benzaldehyde
2-furaldehyde cyanohydrin
2-furaldehyde + HCN
2-Furylaldehyde + cyanide
Furan-3-yl-hydroxyacetonitrile
-
-
-
-
?
2-hydroxy-2-methylpropanenitrile
acetone + HCN
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
2-hydroxy-2-methylpropanenitrile
cyanide + propan-2-one
-
-
-
r
2-hydroxy-2-methylpropanenitrile
HCN + acetone
2-hydroxyisobutyronitrile
HCN + acetone
-
-
-
?
2-Methyl-2-hydroxybutyronitrile
Butanone + cyanide
-
-
-
?
2-nitro-1-phenylethanol
?
2-nitro-1-phenylethanol
nitromethane + benzaldehyde
-
-
-
?
2-Pentanone + cyanide
3-Hydroxyhexanonitrile
-
-
-
-
?
2-Thienylaldehyde + cyanide
Hydroxythiophen-3-yl-acetonitrile
-
-
-
-
?
3,3-dimethyl-2-butanone + acetone cyanohydrin
(S)-2-hydroxy-2-methyl-3,3-dimethyl-butyronitrile
-
transcyanation
-
-
?
3-[(1S)-1-hydroxy-2-nitroethyl]phenol
3-hydroxybenzaldehyde + CH3NO2
-
enantiomeric excess: ~90%, yield: 60-70%
-
-
r
4-Methoxybenzaldehyde + cyanide
4-Methoxymandelonitrile
-
-
-
-
?
Acetone cyanhydrin
Cyanide + acetone
acetone cyanhydrin
HCN + acetone
acetone cyanohydrin
cyanide + acetone
acetone cyanohydrin
hydrocyanic acid + acetone
-
-
-
?
Acetophenone + cyanide
3-Hydroxy-3-phenylpropionitrile
-
-
-
-
?
acetyltrimethylsilane + acetone cyanohydrin
(S)-2-trimethylsilyl-2-hydroxyl-propionitrile + acetone
-
transcyanation
-
-
?
Benzaldehyde + cyanide
(S)-Mandelonitrile
-
-
-
-
?
benzaldehyde + HCN
(S)-mandelonitrile
-
-
-
?
cyanide + (2E)-3-(4-hydroxyphenyl)prop-2-enal
(2S,3E)-2-hydroxy-4-(4-hydroxyphenyl)but-3-enenitrile
-
wild-type enzyme: 95% enantiomeric excess, 80% conversion rate
-
?
cyanide + (2E)-but-2-enal
(3E)-2-hydroxypent-3-enenitrile
-
86% enantiomeric excess with crude enzyme preparation
-
?
cyanide + (2E)-but-2-enal
(3S,3E)-2-hydroxypent-3-enenitrile
-
92% enantiomeric excess
-
?
cyanide + (2E)-hex-2-enal
(2S,3E)-2-hydroxyhept-3-enenitrile
cyanide + (2Z)-hex-2-enal
(2S,3Z)-2-hydroxyhept-3-enenitrile
-
80% enantiomeric excess with crude enzyme preparation
-
?
cyanide + (4-hydroxyphenyl)acetaldehyde
(2S)-2-hydroxy-3-(4-hydroxyphenyl)propanenitrile
-
wild-type enzyme: 96% enantiomeric excess, 88% conversion rate
-
?
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
-
-
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
-
-
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 48.1% (2S)-hydroxy-[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile and 51.9% (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
-
-
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 52.7% (2S)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 47.3% (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
-
-
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 34.9% (2S)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 65.1% (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
-
-
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 35.1% (2S)-hydroxy-[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile and 64.9% (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
-
-
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 49.9% (2S)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 50.1% (2R)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
?
cyanide + 1,1'-diformylferrocene
(R,R)-1,1'-bis(cyanohydroxymethyl)ferrocene
a bulky organometallic compound, which does not occur in nature. S-hydroxynitrile lyase from Hevea brasieliensis catalyzes the formation of (R,R)-1,1'-bis(cyanohydroxymethyl)ferrocene at high yield and stereochemical purity
obtained at high yield and stereochemical purity
-
?
cyanide + 1,3-benzodioxole-5-carbaldehyde
(2S)-1,3-benzodioxol-5-yl(hydroxy)acetonitrile
-
86% enantiomeric excess
-
?
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
-
-
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 16.9% (2S)-(2R)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile, 33.0% (2R)-(2R)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile, 18.3% (2S)-(2S)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile and 31.8% (2R)-(2S)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile
-
?
cyanide + 1-naphthalene carboxaldehyde
?
cyanide + 1-phenylethanone
(2S)-2-hydroxy-2-phenylpropanenitrile
wild-type enzyme: 87% enantiomeric excess, 13% conversion rate
-
-
?
cyanide + 1-phenylpropan-2-one
(2S)-2-hydroxy-2-methyl-3-phenylpropanenitrile
wild-type enzyme: 97% enantiomeric excess, 82% conversion rate
-
-
?
cyanide + 2,2-dimethylpropanal
(2S)-2-hydroxy-3,3-dimethylbutanenitrile
cyanide + 2,4-dimethylbenzaldehyde
(2S)-(2,4-dimethylphenyl)(hydroxy)ethanenitrile
-
65% yield, 82% enantiomeric excess
-
?
cyanide + 2-bromobenzaldehyde
(2S)-(2-bromophenyl)(hydroxy)ethanenitrile
-
wild-type enzyme: 96% enantiomeric excess, 96% conversion rate
-
?
cyanide + 2-bromobenzaldehyde
(S)-2-bromomandelonitrile
the (S)-cyanohydrin is formed with more than 99.5% enantiomeric excess
-
-
r
cyanide + 2-chlorobenzaldehyde
(2S)-(2-chlorophenyl)(hydroxy)acetonitrile
-
92% enantiomeric excess
-
?
cyanide + 2-chlorobenzaldehyde
(2S)-(2-chlorophenyl)(hydroxy)ethanenitrile
-
wild-type enzyme: 98% enantiomeric excess, 96% conversion rate
-
?
cyanide + 2-chlorobenzaldehyde
(S)-2-chloromandelonitrile
the (S)-cyanohydrin is formed with more than 99.5% enantiomeric excess
-
-
r
cyanide + 2-flourobenzaldehyde
(S)-2-fluoromandelonitrile
the (S)-cyanohydrin is formed with more than 99.5% enantiomeric excess
-
-
r
cyanide + 2-hydroxybenzaldehyde
(2S)-(2-hydroxyphenyl)(hydroxy)ethanenitrile
-
wild-type enzyme: 91% enantiomeric excess, 47% conversion rate
-
?
cyanide + 2-methoxybenzaldehyde
(2S)-2-hydroxy-2-(2-methoxyphenyl)acetonitrile
-
77% enantiomeric excess
-
?
cyanide + 2-methylbenzaldehyde
(2S)-(2-methylphenyl)(hydroxy)ethanenitrile
-
76% yield, 47% enantiomeric excess
-
?
cyanide + 2-methylpropanal
(2S)-2-hydroxy-3-methylbutanenitrile
cyanide + 2-thiophene carboxaldehyde
?
cyanide + 3,3-dimethylbutan-2-one
(2S)-2-hydroxy-2,3,3-trimethylbutanenitrile
-
78% enantiomeric excess
-
?
cyanide + 3-(4-hydroxyphenyl)propanal
(2S)-2-hydroxy-4-(4-hydroxyphenyl)butanenitrile
-
wild-type enzyme: 67% enantiomeric excess, 90% conversion rate
-
?
cyanide + 3-bromobenzaldehyde
(S)-3-bromomandelonitrile
the (S)-cyanohydrin is formed with more than 96% enantiomeric excess
-
-
r
cyanide + 3-chlorobenzaldehyde
(S)-3-chloromandelonitrile
the (S)-cyanohydrin is formed with more than 96% enantiomeric excess
-
-
r
cyanide + 3-flourobenzaldehyde
(S)-3-fluoromandelonitrile
the (S)-cyanohydrin is formed with more than 99% enantiomeric excess
-
-
r
cyanide + 3-hydroxybenzaldehyde
(2S)-(3-hydroxyphenyl)(hydroxy)ethanenitrile
-
wild-type enzyme: 97% enantiomeric excess, 88% conversion rate
-
?
cyanide + 3-methoxybenzaldehyde
(2S)-(3-methoxyphenyl)(hydroxy)ethanenitrile
-
67% yield, 76% enantiomeric excess
-
?
cyanide + 3-methoxybenzaldehyde
(2S)-2-hydroxy-2-(3-methoxyphenyl)acetonitrile
-
99% enantiomeric excess
-
?
cyanide + 3-methylbenzaldehyde
(2S)-(3-methylphenyl)(hydroxy)ethanenitrile
-
76% yield, 76% enantiomeric excess
-
?
cyanide + 3-phenoxybenzaldehyde
(2S)-2-hydroxy-2-(3-phenoxyphenyl)acetonitrile
-
99% enantiomeric excess
-
?
cyanide + 3-phenoxybenzaldehyde
(2S)-hydroxy(3-phenoxyphenyl)acetonitrile
-
20% enantiomeric excess
-
?
cyanide + 3-phenoxybenzaldehyde
(S)-3-phenoxybenzaldehyde cyanohydrin
reaction in a high-pH two-phase system
97% enantiomeric excess
-
r
cyanide + 3-phenylpropanal
(2S)-2-hydroxy-4-phenylbutanenitrile
cyanide + 3-tetrahydrothiophenone
(S)-3-hydroxytetrahydrothiophene-3-carbonitrile
-
-
-
?
cyanide + 4-biphenyl carboxaldehyde
?
cyanide + 4-bromobenzaldehyde
(S)-4-bromomandelonitrile
the (S)-cyanohydrin is formed with more than 99.5% enantiomeric excess
-
-
r
cyanide + 4-chlorobenzaldehyde
(S)-4-chloromandelonitrile
the (S)-cyanohydrin is formed with 93% enantiomeric excess
-
-
r
cyanide + 4-fluorobenzaldehyde
(S)-4-fluoromandelonitrile
the (S)-cyanohydrin is formed with more than 99.5% enantiomeric excess
-
-
r
cyanide + 4-hydroxybenzaldehyde
(2S)-(4-hydroxyphenyl)(hydroxy)ethanenitrile
-
wild-type enzyme: 94% enantiomeric excess, 51% conversion rate
-
?
cyanide + 4-methoxybenzaldehyde
(2S)-(4-methoxyphenyl)(hydroxy)ethanenitrile
-
wild-type enzyme: 99% enantiomeric excess, 79% conversion rate
-
?
cyanide + 4-methoxybenzaldehyde
(2S)-2-hydroxy-2-(4-methoxyphenyl)acetonitrile
-
95% enantiomeric excess
-
?
cyanide + 4-methoxybenzaldehyde
(2S)-4-methoxymandelonitrile
-
-
-
-
?
cyanide + 4-methoxybenzaldehyde
(2S)-hydroxy(4-methoxyphenyl)acetonitrile
-
98% enantiomeric excess
-
?
cyanide + 4-methoxycyclohex-3-ene-1-carbaldehyde
(2S)-hydroxy[4-(methoxy)cyclohex-3-en-1-yl]ethanenitrile
-
-
-
r
cyanide + 4-methylbenzaldehyde
(2S)-(4-methylphenyl)(hydroxy)ethanenitrile
-
wild-type enzyme: 99% enantiomeric excess, 50% conversion rate
-
?
cyanide + 4-methylpentan-2-one
(2S)-2-hydroxy-2,4-dimethylpentanenitrile
-
28% enantiomeric excess
-
?
cyanide + 4-oxocyclohexanecarbaldehyde
(2S)-hydroxy(4-oxocyclohexyl)ethanenitrile
-
-
-
r
cyanide + 4-phenoxybenzaldehyde
(2S)-(4-phenoxyphenyl)(hydroxy)ethanenitrile
-
wild-type enzyme: 96% enantiomeric excess, 47% conversion rate
-
?
cyanide + 4-phenylbutan-2-one
(2S)-2-hydroxy-2-methyl-4-phenylbutanenitrile
wild-type enzyme: 49% enantiomeric excess, 36% conversion rate
-
-
?
cyanide + 4-[(trimethylsilyl)oxy]cyclohex-3-ene-1-carbaldehyde
(2S)-hydroxy[4-((trimethylsilyl)oxy)cyclohex-3-en-1-yl]ethanenitrile
-
-
-
r
cyanide + 6-methylhept-5-en-2-one
(2S)-2-hydroxy-2,6-dimethylhept-5-enenitrile
wild-type enzyme: 61% enantiomeric excess, 78% conversion rate
-
-
?
cyanide + benzaldehyde
(2S)-2-hydroxy-2-phenylacetonitrile
-
i.e. (S)-mandelonitrile, more than 99% enantiomeric excess
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
cyanide + butan-2-one
(2S)-2-hydroxy-2-methylbutanenitrile
-
18% enantiomeric excess
-
?
cyanide + butanal
(2S)-2-hydroxypentanenitrile
-
80% enantiomeric excess
-
?
cyanide + cinnamaldehyde
(2S)-2-hydroxy-4-phenyl-(E)-but-3-enenitrile
-
95% enantiomeric excess
-
?
cyanide + cyclohex-3-ene-1-carbaldehyde
(2S)-2-(cyclohex-3-enyl)-2-hydroxyacetonitrile
-
99% enantiomeric excess
-
?
cyanide + cyclohexanecarbaldehyde
(2S)-2-cyclohexyl-2-hydroxyacetonitrile
-
99% enantiomeric excess
-
?
cyanide + cyclohexanecarbaldehyde
(2S)-cyclohexyl(hydroxy)acetonitrile
-
92% enantiomeric excess
-
?
cyanide + decanal
(2S)-2-hydroxyundecanenitrile
-
wild-type enzyme: 78% enantiomeric excess, 65% conversion rate
-
?
cyanide + dodecanal
(2S)-2-hydroxytridecanenitrile
-
wild-type enzyme: 71% enantiomeric excess, 80% conversion rate
-
?
cyanide + ferrocenecarboxaldehyde
(R)-(cyanohydroxymethyl)ferrocene
i.e. bis(cyclopentadienyl)iron, a bulky organometallic compound, which does not occur in nature. S-hydroxynitrile lyase from Hevea brasiliensis catalyzes the formation of (R)-(cyanohydroxymethyl)ferrocene at high yield and stereochemical purity
obtained at high yield and stereochemical purity
-
?
cyanide + heptan-2-one
(2S)-2-hydroxy-2-methylheptanenitrile
-
92% enantiomeric excess
-
?
cyanide + heptan-3-one
(2S)-2-ethyl-2-hydroxyhexanenitrile
wild-type enzyme: 46% enantiomeric excess, 14% conversion rate
-
-
?
cyanide + hexan-2-one
(2S)-2-hydroxy-2-methylhexanenitrile
-
80% enantiomeric excess
-
?
cyanide + hexanal
2-hydroxyheptanenitrile
-
84% enantiomeric excess
-
?
cyanide + nonanal
(2S)-2-hydroxydecanenitrile
-
wild-type enzyme: 80% enantiomeric excess, 99% conversion rate
-
?
cyanide + nonanal
2-hydroxydecanenitrile
-
85% enantiomeric excess
-
?
cyanide + octan-3-one
(2S)-2-ethyl-2-hydroxyheptanenitrile
wild-type enzyme: 61% enantiomeric excess, 24% conversion rate
-
-
?
cyanide + octanal
(2S)-2-hydroxynonanenitrile
-
wild-type enzyme: 79% enantiomeric excess, 96% conversion rate
-
?
cyanide + pentan-2-one
(2S)-2-hydroxy-2-methylpentanenitrile
-
69% enantiomeric excess
-
?
cyanide + pentanal
(2S)-2-hydroxyhexanenitrile
-
91% enantiomeric excess
-
?
cyanide + phenylacetaldehyde
(2S)-2-hydroxy-3-phenylpropanenitrile
-
99% enantiomeric excess
-
?
cyanide + phenylacetaldehyde
2-hydroxy-3-phenylpropanenitrile
-
wild-type enzyme: 98% enantiomeric excess, 99% conversion rate
-
?
cyanide + piperonal
?
-
47% yield, 74% enantiomeric excess
-
?
cyanide + prop-2-enal
(2S)-2-hydroxy-3-methylbutanenitrile
-
-
-
-
?
cyanide + prop-2-enal
(2S)-2-hydroxybut-3-enenitrile
cyanide + prop-2-enal
2-hydroxybut-3-enenitrile
-
84% enantiomeric excess
-
?
cyanide + propanal
(2S)-2-hydroxybutanenitrile
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
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate tetrahydro-2H-pyran-2-carbaldehyde is converted to 5.4% (2S)-hydroxy-[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile, 45.9% (2R)-hydroxy-[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile, 3.9% (2S)-hydroxy[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile and 44.9% (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
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate tetrahydrofuran-2-carbaldehyde is converted to 17.1% (2S)-hydroxy-[(2R)-tetrahydrofuran-2-yl]ethanenitrile, 32.9% (2R)-hydroxy-[(2R)-tetrahydrofuran-2-yl]ethanenitrile, 18.9% (2S)-hydroxy[(2S)-tetrahydrofuran-2-yl]ethanenitrile and 31.1% (2R)-hydroxy[(2S)-tetrahydrofuran-2-yl]ethanenitrile
-
?
cyanide + thiophene-2-carbaldehyde
(2S)-hydroxy(thiophen-2-yl)ethanenitrile
-
-
-
-
?
cyclohexanone cyanohydrin
?
-
-
-
?
DL-mandelonitrile
benzaldehyde + HCN
-
-
-
?
ferrocenyl aldehyde + HCN
ferrocenyl-cyanohydrin
-
-
-
?
furan-3-carbaldehyde + HCN
(2S)-hydroxy(furan-3-yl)ethanenitrile
-
92% enantiomeric excess
-
?
HCN + (2E)-oct-2-enal
(2S,3E)-2-hydroxynon-3-enenitrile
-
-
-
?
HCN + (benzyloxy)acetaldehyde
3-(benzyloxy)-(2S)-2-hydroxy-propanenitrile + 3-(benzyloxy)-(2R)-2-hydroxy-propanenitrile
-
-
50% 3-(benzyloxy)-(2S)-2-hydroxy-propanenitrile and 50% 3-(benzyloxy)-(2R)-2-hydroxy-propanenitrile
?
HCN + (E)-2-butenal
(3E)-2-hydroxypent-3-enenitrile
-
-
-
?
HCN + 1,1'-diformylferrocene
(R,R)-1,1-bis(cyanohydroxymethyl)ferrocene
-
-
-
?
HCN + 2,2-dimethylpropanal
2-hydroxy-3,3-dimethylbutyronitrile
-
-
-
?
HCN + 2-allyloxybutanal
3-allyloxy-2-hydroxypentanenitrile
-
-
-
?
HCN + 2-allyloxyheptanal
(2R,3RS)-3-allyloxy-2-hydroxyoctanenitrile
-
-
-
?
HCN + 2-allyloxyhexanal
(2R,3RS)-3-allyloxy-2-hydroxyheptanenitrile
-
-
-
?
HCN + 2-allyloxypentanal
(2R,3RS)-3-allyloxy-2-hydroxyhexanenitrile
-
-
-
?
HCN + 2-allyloxypropanal
3-allyloxy-2-hydroxybutanenitrile
-
-
-
?
HCN + 2-benzyloxypropanal
3-benzyloxy-2-hydroxybutanenitrile
-
-
-
?
HCN + 2-chlorobenzaldehyde
(2-chlorophenyl)(hydroxy)acetonitrile
-
-
-
?
HCN + 2-hexenal
2-hydroxyhept-3-enenitrile
-
-
-
?
HCN + 2-methoxymethoxypropanal
3-methoxymethoxy-2-hydroxybutanenitrile
-
-
-
?
HCN + 2-methylallyloxyacetaldehyde
3-(2-methylallyloxy)-2-hydroxypropionitrile
-
-
-
?
HCN + 2-methyldihydrofuran
3-hydroxy-2-methyltetrahydrofuran-3-carbonitrile
-
analysis of diastereomeric distribution of the products, depending on different reaction conditions such as pH, reaction time, and solvent properties
-
?
HCN + 2-methyldihydrothiophen-3(2H)-one
3-hydroxy-2-methyltetrahydrothiophen-3-carbonitrile
-
analysis of diastereomeric distribution of the products, depending on different reaction conditions such as pH, reaction time, and solvent properties
-
?
HCN + 2-naphthaldehyde
(2S)-2-hydroxynaphthalen-2-yl-acetonitrile + (2R)-2-hydroxynaphthalen-2-yl-acetonitrile
-
-
83% (2S)-2-hydroxynaphthalen-2-yl-acetonitrile and 17% (2R)-2-hydroxynaphthalen-2-yl-acetonitrile
?
HCN + 2-naphthylacetaldehyde
(2S)-2-hydroxy-3-naphthalen-1-yl-propionitrile + (2R)-2-hydroxy-3-naphthalen-1-yl-propionitrile
-
-
84.3% (2S)-2-hydroxy-3-naphthalen-1-yl-propionitrile and 15.6% (2R)-2-hydroxy-3-naphthalen-1-yl-propionitrile
?
HCN + 2-propenal
2-hydroxybut-3-enenitrile
-
-
-
?
HCN + 3-furaldehyde
(2R)-3-furyl(hydroxy)acetonitrile
-
-
-
?
HCN + 3-furylcarbaldehyde
hydroxy(fur-3yl)acetonitrile
-
-
-
?
HCN + 3-phenoxybenzaldehyde
(2S)-hydroxy(3-phenoxyphenyl)acetonitrile
-
-
-
?
HCN + 3-phenoxypropanal
(2S)-2-hydroxy-4-phenoxybutanenitrile + (2S)-2-hydroxy-4-phenoxybutanenitrile
-
-
95.8% (2S)-2-hydroxy-4-phenoxybutanenitrile and 4.2% (2R)-2-hydroxy-4-phenoxybutanenitrile
?
HCN + 3-phenylpropionaldehyde
(2S)-2-hydroxy-4-phenylbutanenitrile
HCN + 4-methoxybenzaldehyde
(4-methoxyphenyl) (hydroxy)acetonitrile
-
-
-
?
HCN + acrolein
(2S)-2-hydroxybut-3-enenitrile
HCN + allyloxy-2-hydroxypropionitrile
3-allyloxy-2-hydroxypropionitrile
-
-
-
?
HCN + benzaldehyde
(R)-mandelonitrile
HCN + benzaldehyde
(S)-mandelonitrile
HCN + benzene-1,2,4-tricarbaldehyde
?
-
-
-
?
HCN + benzyloxyacetaldehyde
3-benzyloxy-2-hydroxypropionitrile
-
-
-
?
HCN + cyclohexanecarbaldehyde
(2R)-cyclohexyl(hydroxy)acetonitrile
-
-
-
?
HCN + decanal
(S)-2-hydroxyundecanenitrile
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. Compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
-
-
?
HCN + dodecanal
(S)-2-hydroxytridecanenitrile
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. Compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
-
-
?
HCN + ferrocene aldehyde
?
-
-
-
?
HCN + formylferrocene
(R)-(cyanohydroxymethyl)ferrocene
-
-
-
?
HCN + furaldehyde
(2R)-furan-2-yl(hydroxy)ethanenitrile
-
enzyme encapsulated in sol-gel matrix
-
-
?
HCN + hexanal
(S)-2-hydroxyoctanenitrile
-
enzyme encapsulated in sol-gel matrix
-
-
?
HCN + isobutyraldehyde
2-hydroxy-3-methylbutyronitrile
-
-
-
?
HCN + m-phenoxybenzaldehyde
(S)-hydroxy-(3-phenoxy-phenyl)acetonitrile
-
enzyme encapsulated in sol-gel matrix
-
-
?
HCN + methoxymethoxyacetaldehyde
2-hydroxy-3-methoxymethoxypropionitrile
-
-
-
?
HCN + methyl isopropyl ketone
(S)-2-hydroxy-2,3-dimethylbutanenitrile
-
enzyme encapsulated in sol-gel matrix
-
-
?
HCN + pentanal
2-hydroxyhexanenitrile
-
-
-
?
HCN + phenylacetaldehyde
(2R)-2-hydroxy-3-phenylpropanenitrile
-
-
-
?
HCN + propanal
2-hydroxybutanenitrile
-
-
-
?
HCN + rac-2-methyl-3-phenylpropionaldehyde
(2S,3R)-2-hydroxy-3-methyl-4-phenylbutyronitrile
-
-
wild-type and mutant enzymes Y128Y, W128L, W128C, W128A are (S)-selective
-
?
HCN + rac-2-phenylbutyraldehyde
2-hydroxy-3-phenylpentanenitrile
-
-
diastereomer composition. (2R,3R): 0.5% (wild-type), 0.7% (mutant W128Y), 0.8% (mutant W128L), 0.4% (mutant W128L), 0.6% (mutant W128C), 0% (mutant W128A). (2R,3S): 4.5% (wild-type), 4.6% (mutant W128Y), 24.3% (mutant W128L), 23.4% (mutant W128C), 34.1% (mutant W128A), 35.5% (mutant W128V). (2S,3S): 45.8% (wild-type), 45.6% (mutant W128Y), 25.1% (mutant W128L), 26.1% (mutant W128C), 15.0% (mutant W128A), 13.7% (mutant W128V). (2S,3R): 49.2% (wild-type), 49.1% (mutant W128Y), 49.8% (mutant W128L), 50.1% (mutant W128C), 50.3% (mutant W128A), 50.8% (mutant W128V)
-
?
HCN + rac-2-phenylpropionaldehyde
2-hydroxy-3-phenylbutyronitrile
-
-
diastereomer composition. (2R,3R): 0.1% (wild-type), 0.2% (mutant W128Y), 0.3% (mutant W128L), 0.5% (mutant W128C), 1% (mutant W128A). (2R,3S): 5.2% (wild-type), 24.4% (mutant W128Y), 37.5% (mutant W128L), 43.4% (mutant W128C), 46.2% mutant (W128A). (2S,3S): 44.4% (wild-type), 25.4% (mutant W128Y), 12.2% (mutant W128C), 6.1% (mutant W128L), 3.4% (mutant W128A). (2S,3R): 50.3% (wild-type), 50.2% (mutant W128Y), 50.0% (mutant W128L), 50.0% (mutant W128C), 49.4% (mutant W128A)
-
?
HCN + rac-3-phenylbutyraldehyde
(2S,3R)-2-hydroxy-4-phenylpentanenitrile
-
-
wild-type and mutant enzymes Y128Y, W128L, W128C, W128A are (S)-selective
-
?
HCN + tetrahydro-2H-3-pyranone
(3R)-3-hydroxytetrahydro-2H-pyran-3-carbonitrile
-
-
enantiomeric excess at pH 4.75 is 48.3%
?
HCN + tetrahydro-3-furanone
(3R)-3-hydroxytetrahydrofuran-3-carbonitrile
-
-
81% enantiomeric excess
?
HCN + thiophen-2-carbaldehyde
hydroxy(thien-2-yl)acetonitrile
-
-
-
?
HCN + thiophen-3-carbaldehyde
hydroxy(thien-3-yl)acetonitrile
-
-
-
?
HCN + undecanal
(S)-2-hydroxydodecanenitrile
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. Compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
-
-
?
hexanal cyanohydrin
hexanal + HCN
Isobutyraldehyde + cyanide
2-Hydroxy-3-methylbutyronitrile
-
-
-
-
?
lactonitrile
?
poor substrate
-
-
?
m-phenoxybenzaldehyde cyanohydrin
m-phenoxybenzaldehyde + cyanide
2-phenoxybenzaldehyde cyanohydrin is converted with lower activity than (S)-mandelonitrile and cyclohexanone cyanohydrile
-
-
?
m-phenoxybenzaldehyde cyanohydrin
m-phenoxybenzaldehyde + HCN
mandelonitrile
benzaldehyde + HCN
mandelonitrile
cyanide + benzaldehyde
-
-
-
?
mandelonitrile
HCN + benzaldehyde
n-Butyraldehyde + cyanide
(S)-2-Hydroxyvaleronitrile
-
-
-
?
nitromethane + benzaldehyde
(S)-2-nitro-1-phenylethanol
-
-
-
-
r
p-hydroxymandelonitrile
?
phydroxymandelonitrile is converted with lower activity than (S)-mandelonitrile and cyclohexanone cyanohydrile
-
-
?
propionaldehyde cyanohydrin
propionaldehyde + cyanide
poor substrate
-
-
?
rac-2-nitro-1-phenylethanol
nitromethane + benzaldehyde
-
-
-
?
rac-mandelonitrile
benzaldehyde + HCN
-
-
-
?
rac-mandelonitrile
HCN + benzaldehyde
-
-
-
?
thiophene-2-carbaldehyde + HCN
(2S)-hydroxy(thiophen-2-yl)ethanenitrile
-
96% enantiomeric excess
-
?
thiophene-3-carbaldehyde + HCN
(2S)-hydroxy(thiophen-3-yl)ethanenitrile
-
98% enantiomeric excess
-
?
additional information
?
-
(2S)-2-hydroxy-2-methylbutanenitrile
cyanide + butan-2-one
-
-
-
?
(2S)-2-hydroxy-2-methylbutanenitrile
cyanide + butan-2-one
the liberation of HCN serves as a defense mechanism against herbivores and microbial attack in plants
-
-
?
(S)-mandelonitrile
benzaldehyde + HCN
-
enantiomeric excess: > 99%, yield: 90%
-
-
r
(S)-mandelonitrile
benzaldehyde + HCN
-
-
-
-
?
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
r
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
-
?
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
-
r
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
?
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
r
(S)-mandelonitrile
cyanide + benzaldehyde
binding mode of the chiral substrate is identical to that observed for the biological substrate acetone cyanohydrin. Three-point binding mode of the substrates: hydrophobic pocket, hydrogen bonds between the hydroxyl group and Ser80 and Thr11, electrostatic interaction of the cyano group with Lys236
-
-
?
(S)-mandelonitrile
cyanide + benzaldehyde
enzyme kinetics in both directions is studied on a model system with mandelonitrile, benzaldehyde, and HCN using two different methods: initial rate measurements and progress curve analysis. Ordered Uni bi mechanism with the formation of a dead-end complex of enzyme, (S)-mandelonitrile and HCN. HCN is the first product released from the enzyme followed by benzaldehyde while in the synthesis reaction, benzaldehyde is the first substrate bond to the enzyme followed by HCN
-
-
r
(S)-mandelonitrile
cyanide + benzaldehyde
the enzymatic reversible conversion of (S)-mandelonitrile to HCN and benzaldehyde can be adequately described by a three-step, reversible-ordered UniBi reaction scheme
-
-
r
(S)-mandelonitrile
cyanide + benzaldehyde
the enzyme is a member of the alpha/beta hydrolase fold protein family, containing a catalytic triad with C-C cleaving and ligating activity
-
-
r
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
-
?
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
r
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
-
r
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
?
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
-
?
(S)-mandelonitrile
cyanide + benzaldehyde
-
-
-
r
(S)-mandelonitrile
cyanide + benzaldehyde
high selectivity towards the (S)-enentiomer
-
-
?
(S)-mandelonitrile
HCN + benzaldehyde
-
-
-
-
?
(S)-mandelonitrile
HCN + benzaldehyde
-
highly (S)-selective
-
?
(S)-mandelonitrile
HCN + benzaldehyde
-
-
-
-
?
2-furaldehyde cyanohydrin
2-furaldehyde + HCN
-
aqua gel, 30 min, conversion ratio: 89%, enantiomeric excess: 94%
-
-
r
2-furaldehyde cyanohydrin
2-furaldehyde + HCN
-
free enzyme, 30 min, conversion ratio: 89%,enantiomeric excess: 94%
-
-
r
2-hydroxy-2-methylpropanenitrile
acetone + HCN
-
-
-
?
2-hydroxy-2-methylpropanenitrile
acetone + HCN
-
-
-
-
r
2-hydroxy-2-methylpropanenitrile
acetone + HCN
-
release of HCN serves as a defense against herbivores and microbial attack of the plant
-
?
2-hydroxy-2-methylpropanenitrile
acetone + HCN
-
-
-
-
?
2-hydroxy-2-methylpropanenitrile
acetone + HCN
-
-
-
?
2-hydroxy-2-methylpropanenitrile
acetone + HCN
acetone cyanohydrin spontaneously decomposes to acetone and cyanide at pH above 5.0 or temperatures above 35 C
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
-
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
i.e. acetone cyanohydrin, three-point binding mode of the substrates: hydrophobic pocket, hydrogen bonds between the hydroxyl group and Ser80 and Thr11, electrostatic interaction of the cyano group with Lys236
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
-
-
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
-
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
-
-
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
-
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
i.e. acetone cyanohydrin
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
-
i.e. acetone cyanohydrin
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
i.e. acetone cyanohydrin, catalyzes the decomposition of the achiral alpha-hydroxynitrile 2-hydroxy-2-methylpropanenitrile into HCN and acetone during cyanogenesis of damaged plants
-
-
?
2-hydroxy-2-methylpropanenitrile
cyanide + acetone
the liberation of HCN serves as a defense mechanism against herbivores and microbial attack in plants
-
-
?
2-hydroxy-2-methylpropanenitrile
HCN + acetone
-
-
-
?
2-hydroxy-2-methylpropanenitrile
HCN + acetone
-
liberation of HCN by degradation of acetone cyanohydrin is considerably faster than the consumption of HCN by the formation of (S)-mandelonitrile
-
?
2-hydroxy-2-methylpropanenitrile
HCN + acetone
-
release of HCN serves as a defense against herbivores and microbial attack of the plant
-
?
2-hydroxy-2-methylpropanenitrile
HCN + acetone
-
-
-
?
2-nitro-1-phenylethanol
?
-
-
-
-
?
2-nitro-1-phenylethanol
?
-
very low turnover number
-
-
?
Acetone cyanhydrin
Cyanide + acetone
-
-
-
?
Acetone cyanhydrin
Cyanide + acetone
-
-
-
?
Acetone cyanhydrin
Cyanide + acetone
-
-
-
?
acetone cyanhydrin
HCN + acetone
-
-
-
?
acetone cyanhydrin
HCN + acetone
-
S-specific
-
?
acetone cyanohydrin
cyanide + acetone
-
-
-
-
?
acetone cyanohydrin
cyanide + acetone
-
-
-
?
cyanide + (2E)-hex-2-enal
(2S,3E)-2-hydroxyhept-3-enenitrile
-
95% enantiomeric excess with crude enzyme preparation
-
?
cyanide + (2E)-hex-2-enal
(2S,3E)-2-hydroxyhept-3-enenitrile
-
97% enantiomeric excess
-
?
cyanide + (2E)-hex-2-enal
(2S,3E)-2-hydroxyhept-3-enenitrile
-
wild-type enzyme: 97% enantiomeric excess, 58% conversion rate
-
?
cyanide + 1-naphthalene carboxaldehyde
?
-
-
-
?
cyanide + 1-naphthalene carboxaldehyde
?
-
-
-
?
cyanide + 2,2-dimethylpropanal
(2S)-2-hydroxy-3,3-dimethylbutanenitrile
-
67% enantiomeric excess
-
?
cyanide + 2,2-dimethylpropanal
(2S)-2-hydroxy-3,3-dimethylbutanenitrile
-
94% enantiomeric excess
-
?
cyanide + 2-methylpropanal
(2S)-2-hydroxy-3-methylbutanenitrile
-
81% enantiomeric excess
-
?
cyanide + 2-methylpropanal
(2S)-2-hydroxy-3-methylbutanenitrile
-
95% enantiomeric excess
-
?
cyanide + 2-thiophene carboxaldehyde
?
-
-
-
?
cyanide + 2-thiophene carboxaldehyde
?
-
-
-
?
cyanide + 3-phenylpropanal
(2S)-2-hydroxy-4-phenylbutanenitrile
-
-
-
-
?
cyanide + 3-phenylpropanal
(2S)-2-hydroxy-4-phenylbutanenitrile
-
93% enantiomeric excess
-
?
cyanide + 4-biphenyl carboxaldehyde
?
-
-
-
?
cyanide + 4-biphenyl carboxaldehyde
?
-
-
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
-
-
-
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
-
-
-
r
cyanide + benzaldehyde
(S)-mandelonitrile
-
68% yield, 54% enantiomeric excess
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
-
-
-
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
-
-
-
-
r
cyanide + benzaldehyde
(S)-mandelonitrile
-
94% enantiomeric excess
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
-
-
-
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
-
-
-
r
cyanide + benzaldehyde
(S)-mandelonitrile
-
-
-
-
r
cyanide + benzaldehyde
(S)-mandelonitrile
-
-
-
r
cyanide + benzaldehyde
(S)-mandelonitrile
-
98% enantiomeric excess
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
-
wild-type enzyme: 99% enantiomeric excess, 97% conversion rate
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
-
-
low enantioselectivity with 20% ee (S)
-
r
cyanide + benzaldehyde
(S)-mandelonitrile
concentrations of benzaldehyde higher than 1 M result in decreased enantioselectivity due to nonenzymatic formation of racemic mandelonitrile due to an excess of benzaldehyde and cyanide
-
-
?
cyanide + benzaldehyde
(S)-mandelonitrile
the (S)-cyanohydrin is formed with more than 99.5% enantiomeric excess
-
-
r
cyanide + prop-2-enal
(2S)-2-hydroxybut-3-enenitrile
-
94% enantiomeric excess with crude enzyme preparation
-
?
cyanide + prop-2-enal
(2S)-2-hydroxybut-3-enenitrile
-
47% enantiomeric excess
-
?
cyanide + propanal
(2S)-2-hydroxybutanenitrile
-
-
-
-
?
cyanide + propanal
(2S)-2-hydroxybutanenitrile
-
91% enantiomeric excess
-
?
HCN + 3-phenylpropionaldehyde
(2S)-2-hydroxy-4-phenylbutanenitrile
-
-
89% enantiomeric excess
?
HCN + 3-phenylpropionaldehyde
(2S)-2-hydroxy-4-phenylbutanenitrile
-
-
67% enantiomeric excess
?
HCN + acrolein
(2S)-2-hydroxybut-3-enenitrile
-
-
92% enantiomeric ecxess
?
HCN + acrolein
(2S)-2-hydroxybut-3-enenitrile
-
-
59% enantiomeric excess
?
HCN + benzaldehyde
(R)-mandelonitrile
-
-
-
?
HCN + benzaldehyde
(R)-mandelonitrile
-
-
-
?
HCN + benzaldehyde
(S)-mandelonitrile
-
-
99% enantiomeric excess
?
HCN + benzaldehyde
(S)-mandelonitrile
-
enzyme encapsulated in sol-gel matrix
-
-
?
HCN + benzaldehyde
(S)-mandelonitrile
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. Compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
-
-
?
HCN + benzaldehyde
(S)-mandelonitrile
-
-
99% enantiomeric excess
?
hexanal cyanohydrin
hexanal + HCN
-
aqua gel, 2 h, conversion ratio: 92%, enantiomeric excess: 94%
-
-
r
hexanal cyanohydrin
hexanal + HCN
-
free enzyme, 4 h, conversion ratio: 91%,enantiomeric excess: 94%
-
-
r
m-phenoxybenzaldehyde cyanohydrin
m-phenoxybenzaldehyde + HCN
-
aqua gel, 72 h, conversion ratio: 92%, enantiomeric excess: 98%
-
-
r
m-phenoxybenzaldehyde cyanohydrin
m-phenoxybenzaldehyde + HCN
-
free enzyme, 72 h, conversion ratio: 45%,enantiomeric excess: 82%
-
-
r
mandelonitrile
benzaldehyde + HCN
-
aqua gel, 0.5 h, conversion ratio: 97%, enantiomeric excess: 99%
-
-
r
mandelonitrile
benzaldehyde + HCN
-
CLEA, 72 h, conversion ratio: 55%, enantiomeric excess: 67%
-
-
r
mandelonitrile
benzaldehyde + HCN
-
free enzyme, 4 h, conversion ratio: 97%,enantiomeric excess: 97%
-
-
r
mandelonitrile
HCN + benzaldehyde
-
racemic
-
?
mandelonitrile
HCN + benzaldehyde
racemic
-
?
mandelonitrile
HCN + benzaldehyde
-
-
-
?
additional information
?
-
-
acetylferrocene and 1,1'-diacetylferrocene are not transformed with this enzyme
-
-
?
additional information
?
-
-
acetylferrocene and 1,1'-diacetylferrocene are not transformed with this enzyme
-
?
additional information
?
-
-
the enantiomeric excess of the product is optimal at pH 5.4 and at HCN concentration between 200 mM and 400 mM and clearly decreases at concentrations greater than 1.5 M. When the temperature decreases from 25°C to -5°C, the enantiomeric excess increases from 88% to 95%
-
-
?
additional information
?
-
-
the enantiomeric excess of the product is optimal at pH 5.4 and at HCN concentration between 200 mM and 400 mM and clearly decreases at concentrations greater than 1.5 M. When the temperature decreases from 25°C to -5°C, the enantiomeric excess increases from 88% to 95%
-
?
additional information
?
-
(3E)-2-hydroxy-4-phenylbut-3-enenitrile is not sufficently accepted by the enzyme in crude enzyme preparation
-
-
?
additional information
?
-
modeling of the complexes of the enzyme with its natural substrate acetone cyanohydrin as well as with the chiral compounds mandelonitrile and 2,3-dimethyl-2-hydroxybutyronitril. Enzymatic mechanism involves catalytic triad Ser80, His235, and Asp207 as a genertal acid/base
-
-
?
additional information
?
-
-
modeling of the complexes of the enzyme with its natural substrate acetone cyanohydrin as well as with the chiral compounds mandelonitrile and 2,3-dimethyl-2-hydroxybutyronitril. Enzymatic mechanism involves catalytic triad Ser80, His235, and Asp207 as a genertal acid/base
-
-
?
additional information
?
-
-
theoretical investigation of the catalytic mechanism
-
-
?
additional information
?
-
theoretical investigation of the catalytic mechanism
-
-
?
additional information
?
-
-
the enzyme catalyzes asymmetric cyanohydrin and Henry reactions. (R)-2-nitro-1-phenylethanol is not a substrate or HNL
-
-
?
additional information
?
-
-
the enzyme has low activity in performing Henry reactions
-
-
?
additional information
?
-
on the basis of extensive QM/MM MD and RAMD MD simulations, the catalytic mechanism of the enzyme and its substrate delivery and product (HCN) release are explored. The catalytic reaction approximately follows a two-stage mechanism. The first stage involves two fast processes including the proton abstraction of the substrate through a double-proton transfer and the C-CN bond cleavage, while the second stage concerns HCN formation and is rate-determining
-
-
?
additional information
?
-
-
When the temperature decreases from 25°C to -5°C, the enantiomeric excess increases from 67% to 74%
-
-
?
additional information
?
-
-
When the temperature decreases from 25°C to -5°C, the enantiomeric excess increases from 67% to 74%
-
?
additional information
?
-
the enzyme catalyzes enantioselective addition of HCN to aromatic, heteroaromatic and aliphatic aldehydes and ketones forming (S)-aldehyde cyanohydrins or (S)-ketone cyanohydrins
-
-
?
additional information
?
-
wild-type enzyme shows very low activity with 4-hydroxymandelonitrile, activity of mutant enzyme W128A is increased 450fold compared to wild-type value (Km-value for mutant enzyme W128A is 0.625 mM)
-
-
?
additional information
?
-
-
wild-type enzyme shows very low activity with 4-hydroxymandelonitrile, activity of mutant enzyme W128A is increased 450fold compared to wild-type value (Km-value for mutant enzyme W128A is 0.625 mM)
-
-
?
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0.28 - 1.49
(R)-mandelonitrile
2.6
(S)-2-nitro-1-phenylethanol
0.34 - 30
(S)-mandelonitrile
0.2 - 1.4
1-naphthalene carboxaldehyde
5.2
2,4-dimethylbenzaldehyde
pH 6.0, 25°C
67 - 150
2-hydroxy-2-methylpropanenitrile
0.8
2-Methyl-2-hydroxybutyronitrile
-
-
21.7
2-Methylbenzaldehyde
pH 6.0, 25°C
0.4 - 7.1
2-nitro-1-phenylethanol
34.1 - 47.5
2-thiophene carboxaldehyde
161.5
3,3-dimethyl-2-butanone
-
pH 5.4, 40°C
9.8
3-Methoxybenzaldehyde
pH 6.0, 25°C
14.4
3-methylbenzaldehyde
pH 6.0, 25°C
25.4
4-biphenyl carboxaldehyde
pH 4.2, 22°C
0.7 - 174
acetone cyanohydrin
61.5
acetyltrimethylsilane
-
pH 5.4, 40°C
15.7
piperonal
pH 6.0, 25°C
0.4 - 7.1
rac-2-nitro-1-phenylethanol
0.6 - 9.4
rac-mandelonitrile
additional information
additional information
-
0.28
(R)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C
0.61
(R)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C/N156D
1.49
(R)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C/N156G
2.6
(S)-2-nitro-1-phenylethanol
-
in 50 mM phosphate buffer pH 6.0, at 25°C
2.6
(S)-2-nitro-1-phenylethanol
-
in 50 mM phosphate buffer pH 6.0, at 22°C
0.34
(S)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C
0.47
(S)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C/N156D
0.49
(S)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C/N156G
1.2
(S)-mandelonitrile
-
in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication
1.4
(S)-mandelonitrile
-
in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication
1.86
(S)-mandelonitrile
mutant enzyme H103M, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
2.5 - 5
(S)-mandelonitrile
mutant enzyme H103L, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
4.1
(S)-mandelonitrile
pH 7.5
4.1
(S)-mandelonitrile
citrate buffer (50 mM, pH 4.0), at 25°C
4.5
(S)-mandelonitrile
pH 5.2, 23°C, mutant enzyme W128A
5.17
(S)-mandelonitrile
wild type enzyme, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
5.54
(S)-mandelonitrile
mutant enzyme K176P/K199P/K224P, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
6.98
(S)-mandelonitrile
mutant enzyme K176P, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
30
(S)-mandelonitrile
pH 5.2, 23°C, wild-type enzyme
0.2
1-naphthalene carboxaldehyde
pH 4.2, 22°C
1.4
1-naphthalene carboxaldehyde
pH 4.2, 22°C
67
2-hydroxy-2-methylpropanenitrile
pH 5.2, 23°C, wild-type enzyme
95
2-hydroxy-2-methylpropanenitrile
mutant enzyme H112A
101
2-hydroxy-2-methylpropanenitrile
recombinant enzyme
120
2-hydroxy-2-methylpropanenitrile
wild-type enzyme
120
2-hydroxy-2-methylpropanenitrile
mutant enzyme D130A
120
2-hydroxy-2-methylpropanenitrile
mutant enzyme D95A
125
2-hydroxy-2-methylpropanenitrile
mutant enzyme H5A
130
2-hydroxy-2-methylpropanenitrile
mutant enzyme H10A
150
2-hydroxy-2-methylpropanenitrile
pH 5.2, 23°C, mutant enzyme W128A
0.4
2-nitro-1-phenylethanol
mutant enzyme F125T/L146M, pH and temperature not specified in the publication
0.7
2-nitro-1-phenylethanol
mutant enzyme F125T/Y133F, pH and temperature not specified in the publication
1.4
2-nitro-1-phenylethanol
mutant enzyme V106F, pH and temperature not specified in the publication
1.6
2-nitro-1-phenylethanol
mutant enzyme V106F/L121Y, pH and temperature not specified in the publication
1.8
2-nitro-1-phenylethanol
mutant enzyme V106F/F125T, pH and temperature not specified in the publication
5
2-nitro-1-phenylethanol
mutant enzyme C81L, pH and temperature not specified in the publication
5
2-nitro-1-phenylethanol
mutant enzyme F125T, pH and temperature not specified in the publication
5
2-nitro-1-phenylethanol
mutant enzyme L121Y, pH and temperature not specified in the publication
5
2-nitro-1-phenylethanol
mutant enzyme L121Y/F125T/L146M, pH and temperature not specified in the publication
5
2-nitro-1-phenylethanol
mutant enzyme L121Y/F125T/Y133F, pH and temperature not specified in the publication
5
2-nitro-1-phenylethanol
mutant enzyme L121Y/L146M, pH and temperature not specified in the publication
5
2-nitro-1-phenylethanol
mutant enzyme L146M, pH and temperature not specified in the publication
5
2-nitro-1-phenylethanol
mutant enzyme V106F/L121Y/F125T, pH and temperature not specified in the publication
5
2-nitro-1-phenylethanol
mutant enzyme V106F/L146M, pH and temperature not specified in the publication
6.1
2-nitro-1-phenylethanol
wild type enzyme, pH and temperature not specified in the publication
7.1
2-nitro-1-phenylethanol
mutant enzyme Y133F, pH and temperature not specified in the publication
34.1
2-thiophene carboxaldehyde
pH 4.2, 22°C
47.5
2-thiophene carboxaldehyde
pH 4.2, 22°C
0.7
acetone cyanohydrin
-
-
4
acetone cyanohydrin
-
-
115
acetone cyanohydrin
pH 5.4
169
acetone cyanohydrin
-
mutant enzyme C81A
174
acetone cyanohydrin
-
wild-type enzyme
2 - 3
benzaldehyde
wild type enzyme, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
5.5
benzaldehyde
pH 6.0, 25°C
5.9
benzaldehyde
citrate buffer (50 mM, pH 4.0), at 25°C
12.3
benzaldehyde
mutant enzyme H103Y, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
13.4
benzaldehyde
mutant enzyme H103L, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
21.6
benzaldehyde
mutant enzyme K176P, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
27
benzaldehyde
mutant enzyme K176P/K199P/K224P, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
27.9
benzaldehyde
mutant enzyme H103M, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
179
cyanide
pH 7.5
179
cyanide
citrate buffer (50 mM, pH 4.0), at 25°C
0.6
mandelonitrile
mutant enzyme L152F, pH and temperature not specified in the publication
0.7
mandelonitrile
mutant enzyme I209G, pH and temperature not specified in the publication
0.8
mandelonitrile
mutant enzyme I209A, pH and temperature not specified in the publication
1.1
mandelonitrile
-
pH 5.4, 25°C, mutant enzyme G113S
1.4
mandelonitrile
-
pH 5.4, 25°C, wild-type enzyme
1.4
mandelonitrile
mutant enzyme V106F/L121Y, pH and temperature not specified in the publication
1.5
mandelonitrile
mutant enzyme F125T/L146M, pH and temperature not specified in the publication
2
mandelonitrile
mutant enzyme F125T, pH and temperature not specified in the publication
2
mandelonitrile
mutant enzyme V106F/L121Y/F125T, pH and temperature not specified in the publication
2.1
mandelonitrile
mutant enzyme F125T/Y133F, pH and temperature not specified in the publication
2.7
mandelonitrile
mutant enzyme L121Y, pH and temperature not specified in the publication
3.1
mandelonitrile
mutant enzyme L121Y/F125T, pH and temperature not specified in the publication
3.1
mandelonitrile
mutant enzyme Y133F, pH and temperature not specified in the publication
3.3
mandelonitrile
wild type enzyme, pH and temperature not specified in the publication
3.6
mandelonitrile
mutant enzyme L121Y/F125T/L146M, pH and temperature not specified in the publication
3.7
mandelonitrile
mutant enzyme L146M, pH and temperature not specified in the publication
5.3
mandelonitrile
mutant enzyme V106F, pH and temperature not specified in the publication
6.7
mandelonitrile
mutant enzyme L121Y/L146M, pH and temperature not specified in the publication
8.6
mandelonitrile
mutant enzyme F210I, pH and temperature not specified in the publication
8.6
mandelonitrile
mutant enzyme L148F, pH and temperature not specified in the publication
9.4
mandelonitrile
mutant enzyme C81L, pH and temperature not specified in the publication
0.4
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme F125T/L146M
0.7
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme F125T/Y133F
1.4
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme V106F
1.6
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme V106F/L121Y
1.8
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme V106F/F125T
6.1
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, wild-type enzyme
7.1
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme Y133F
0.6
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L152F
0.7
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme I209G
0.8
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme I209A
1.4
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme V106F/L121Y
1.5
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme F125T/L146M
1.5
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121F
2
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme F125T
2
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme V106F/L121Y/F125T
2.1
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme F125T/Y133F
2.7
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121T
2.7
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121Y
2.8
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121A
3.1
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/F125T
3.1
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme Y133F
3.3
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, wild-type enzyme
3.6
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/F125T/L146M
3.7
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121V
3.7
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L146M
4
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121M
4.9
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121I
5.3
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme V106F
5.6
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121W
5.7
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121Q
6.6
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121S
6.7
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/L146M
8
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121H
8.1
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121C
8.6
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme F210I
8.6
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L148F
9.4
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme C81L
additional information
additional information
-
-
-
additional information
additional information
a kinetic investigation based on the rate curve method
-
additional information
additional information
-
a kinetic investigation based on the rate curve method
-
additional information
additional information
wild-type enzyme shows very low activity with 4-hydroxymandelonitrile, activity of mutant enzyme W128A is increased 450fold compared to wild-type value (Km-value for mutant enzyme W128A is 0.625 mM)
-
additional information
additional information
-
wild-type enzyme shows very low activity with 4-hydroxymandelonitrile, activity of mutant enzyme W128A is increased 450fold compared to wild-type value (Km-value for mutant enzyme W128A is 0.625 mM)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.98 - 12.7
(R)-mandelonitrile
1.83 - 122
(S)-mandelonitrile
6 - 23.5
1-naphthalene carboxaldehyde
18.5
2,4-dimethylbenzaldehyde
pH 6.0, 25°C
53.6
2-Methylbenzaldehyde
pH 6.0, 25°C
0.1 - 0.6
2-nitro-1-phenylethanol
31.5 - 100
2-thiophene carboxaldehyde
28.1
3-Methoxybenzaldehyde
pH 6.0, 25°C
49.2
3-methylbenzaldehyde
pH 6.0, 25°C
9.2
4-biphenyl carboxaldehyde
pH 4.2, 22°C
91.4
piperonal
pH 6.0, 25°C
0.1 - 0.6
rac-2-nitro-1-phenylethanol
3 - 106
rac-mandelonitrile
7.98
(R)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C
9.27
(R)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C/N156D
12.7
(R)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C/N156G
1.83
(S)-mandelonitrile
-
in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication
21.5
(S)-mandelonitrile
mutant enzyme H103L, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
21.67
(S)-mandelonitrile
-
in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication
23.9
(S)-mandelonitrile
mutant enzyme H103M, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
34.5
(S)-mandelonitrile
wild type enzyme, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
39.7
(S)-mandelonitrile
mutant enzyme K176P/K199P/K224P, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
41.8
(S)-mandelonitrile
mutant enzyme K176P, in 100 mM citrate buffer pH above 6.0, temperature not specified in the publication
52.9
(S)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C
88.1
(S)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C/N156D
122
(S)-mandelonitrile
pH 4.23, 25°C, mutant enzyme H103C/N156G
6
1-naphthalene carboxaldehyde
pH 4.2, 22°C
23.5
1-naphthalene carboxaldehyde
pH 4.2, 22°C
0.1
2-nitro-1-phenylethanol
mutant enzyme F125T/L146M, pH and temperature not specified in the publication
0.1
2-nitro-1-phenylethanol
mutant enzyme L121Y/L146M, pH and temperature not specified in the publication
0.1
2-nitro-1-phenylethanol
mutant enzyme V106F, pH and temperature not specified in the publication
0.1
2-nitro-1-phenylethanol
mutant enzyme V106F/L121Y, pH and temperature not specified in the publication
0.12
2-nitro-1-phenylethanol
mutant enzyme F125T/Y133F, pH and temperature not specified in the publication
0.15
2-nitro-1-phenylethanol
wild type enzyme, pH and temperature not specified in the publication
0.2
2-nitro-1-phenylethanol
mutant enzyme C81L, pH and temperature not specified in the publication
0.2
2-nitro-1-phenylethanol
mutant enzyme V106F/F125T, pH and temperature not specified in the publication
0.2
2-nitro-1-phenylethanol
mutant enzyme V106F/L146M, pH and temperature not specified in the publication
0.3
2-nitro-1-phenylethanol
mutant enzyme Y133F, pH and temperature not specified in the publication
0.5
2-nitro-1-phenylethanol
mutant enzyme L121Y, pH and temperature not specified in the publication
0.5
2-nitro-1-phenylethanol
mutant enzyme L121Y/F125T/L146M, pH and temperature not specified in the publication
0.5
2-nitro-1-phenylethanol
mutant enzyme L121Y/F125T/Y133F, pH and temperature not specified in the publication
0.5
2-nitro-1-phenylethanol
mutant enzyme L146M, pH and temperature not specified in the publication
0.5
2-nitro-1-phenylethanol
mutant enzyme V106F/L121Y/F125T, pH and temperature not specified in the publication
0.6
2-nitro-1-phenylethanol
mutant enzyme F125T, pH and temperature not specified in the publication
31.5
2-thiophene carboxaldehyde
pH 4.2, 22°C
100
2-thiophene carboxaldehyde
pH 4.2, 22°C
26.6
benzaldehyde
pH 6.0, 25°C
47.4
benzaldehyde
mutant enzyme H103Y, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
83.2
benzaldehyde
mutant enzyme K176P, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
90.4
benzaldehyde
mutant enzyme H103L, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
93.5
benzaldehyde
mutant enzyme K176P/K199P/K224P, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
96.1
benzaldehyde
mutant enzyme H103M, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
96.6
benzaldehyde
wild type enzyme, in 100 mM citrate buffer pH 5.0, temperature not specified in the publication
3
mandelonitrile
mutant enzyme I209G, pH and temperature not specified in the publication
7
mandelonitrile
mutant enzyme L152F, pH and temperature not specified in the publication
7
mandelonitrile
mutant enzyme V106F, pH and temperature not specified in the publication
17
mandelonitrile
mutant enzyme L148F, pH and temperature not specified in the publication
20
mandelonitrile
mutant enzyme L146M, pH and temperature not specified in the publication
21
mandelonitrile
mutant enzyme F210I, pH and temperature not specified in the publication
22
mandelonitrile
mutant enzyme Y133F, pH and temperature not specified in the publication
23
mandelonitrile
mutant enzyme I209A, pH and temperature not specified in the publication
25
mandelonitrile
wild type enzyme, pH and temperature not specified in the publication
32
mandelonitrile
mutant enzyme F125T/L146M, pH and temperature not specified in the publication
32
mandelonitrile
mutant enzyme F125T/Y133F, pH and temperature not specified in the publication
33
mandelonitrile
mutant enzyme C81L, pH and temperature not specified in the publication
43
mandelonitrile
mutant enzyme L121Y/F125T, pH and temperature not specified in the publication
45
mandelonitrile
mutant enzyme L121Y/F125T/L146M, pH and temperature not specified in the publication
55
mandelonitrile
mutant enzyme V106F/L121Y, pH and temperature not specified in the publication
66
mandelonitrile
mutant enzyme F125T, pH and temperature not specified in the publication
82
mandelonitrile
mutant enzyme V106F/L121Y/F125T, pH and temperature not specified in the publication
106
mandelonitrile
mutant enzyme L121Y, pH and temperature not specified in the publication
0.1
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme F125T/L146M
0.1
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme V106F
0.12
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme F125T/Y133F
0.15
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, wild-type enzyme
0.2
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme V106F/F125T
0.3
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme Y133F
0.6
rac-2-nitro-1-phenylethanol
pH 5.0, temperature not specified in the publication, mutant enzyme F125T
3
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme I209G
3
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121T
5
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121H
6
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121Q
7
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L152F
7
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme V106F
9
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121S
15
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121V
15
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121W
17
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L148F
20
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121C
20
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L146M
21
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme F210I
22
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme Y133F
23
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme I209A
23
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121A
25
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, wild-type enzyme
32
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme F125T/L146M
32
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme F125T/Y133F
33
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme C81L
33
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121I
43
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121M
43
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/F125T
45
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/F125T/L146M
55
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme V106F/L121Y
66
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme F125T
77
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121F
82
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme V106F/L121Y/F125T
106
rac-mandelonitrile
pH 5.0, temperature not specified in the publication, mutant enzyme L121Y
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0.1
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121P
0.15
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme C81L
0.17
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme V106F
0.27
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme F125T
0.32
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme L146M
0.39
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme V106F/F125T
0.56
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/F125T/Y133F
0.62
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme L121Y
0.71
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/F125T/L146M
0.9
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme I12A
1.02
-
C-terminal His-tagged recombinant mutant enzyme H103L expressed in a RTS 100 wheat germ cell-free translation system, using benzaldehyde as substrate, pH and temperature not specified in the publication
1.1
-
recombinant mutant enzyme H103L expressed in Pichia pastoris, using benzaldehyde as substrate, pH and temperature not specified in the publication
1.4
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121G
1.55
-
C-terminal His-tagged recombinant wild type enzyme expressed in a RTS 100 wheat germ cell-free translation system, using benzaldehyde as substrate, pH and temperature not specified in the publication
1.73
-
recombinant wild type enzyme expressed in Escherichia coli JM109 cells, using benzaldehyde as substrate, pH and temperature not specified in the publication
1.97
-
untagged recombinant wild type enzyme expressed in a RTS 100 wheat germ cell-free translation system, using benzaldehyde as substrate, pH and temperature not specified in the publication
1.98
-
untagged recombinant mutant enzyme H103L expressed in a RTS 100 wheat germ cell-free translation system, using benzaldehyde as substrate, pH and temperature not specified in the publication
115
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/L146M
119
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121F
12
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L152F
140
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme V106F/L121Y/F125T
149
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121Y
2
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121T
2.03
-
recombinant wild type enzyme expressed in Leishmania tarentolae, using benzaldehyde as substrate, pH and temperature not specified in the publication
2.1
-
recombinant wild type enzyme expressed in Pichia pastoris, using benzaldehyde as substrate, pH and temperature not specified in the publication
2.18
-
recombinant mutant enzyme H103L expressed in Leishmania tarentolae, using benzaldehyde as substrate, pH and temperature not specified in the publication
22
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme C81L
24
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L146M
28
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme Y133F
29.2
-
recombinant mutant enzyme H103L expressed in Escherichia coli JM109 cells, using benzaldehyde as substrate, pH and temperature not specified in the publication
3.8
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121S
30
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121A
33
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, wild-type enzyme
35
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121I
4
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121H
42
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme I209A
5.1
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme I209G
5.9
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121Q
53
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme F125T/L146M
55
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/F125T
57.2
-
mutant enzyme G113S
6.7
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme V106F
64
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/F125T/L146M
7
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L148F
88
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme V106F/L121Y
0.13
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme L121Y/L146M
0.13
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, wild-type enzyme
0.2
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme F125T/L146M
0.2
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121E
0.21
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme F125T/Y133F
0.21
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme V106F/L146M
0.29
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme V106F/L121Y/F125T
0.29
substrate: rac-2-nitro-1-phenylethanol, pH 5.0, temperature not specified in the publication, mutant enzyme Y133F
0.7
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121N
0.7
-
recombinant mutant enzyme H103L expressed in an Escherichia coli lysate (WakoPURE system), using benzaldehyde as substrate, pH and temperature not specified in the publication
14
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme F210I
14
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121W
16
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121C
16
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121V
52
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme F125T/Y133F
52
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme L121M
86
-
-
92
substrate: rac-mandelonitrile, pH 5.0, temperature not specified in the publication, mutant enzyme F125T
92
wild-type enzyme from leaves
additional information
-
expressed in Saccharomyces cerevisiae or Pichia pastoris
additional information
screening assay for hydroxynitrile lyases and its application in high-throughput screening of Escherichia coli mutant libraries, semi-quantitative test where the rate of colour formation corresponds to the particular enzyme activity of the sample
additional information
cyanide-based high-throughput screening assay is developed. The assay is useful to detect activity and enantioselectivity of hydroxynitrile lyases theoretically towards any cyanohydrin substrate
additional information
-
no specific activity is detected with recombinant wild type and mutant enzyme H103L when expressed in an Escherichia coli lysate (WakoPURE system) or as N-terminal His6-tagged enzyme in a RTS 100 wheat germ cell-free translation system
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D207A
mutant protein is insoluble
H103C
the mutated enzyme shows low enantioselectivity and specific activity for (S)-mandelonitrile synthesis. (S)-Mandelonitrile enantiomeric excess is 60%
H103C/N156D
hydroxynitrile lyase of mutant enzyme H103C/N156D is approximately four times higher than that for mutant enzyme H103C. (S)-Mandelonitrile enantiomeric excess is 32%
H235A
mutant protein is insoluble
S80A
mutant protein is insoluble
C81A
about 20% of wild-type activity
F125T/L146M
the mutant shows higher specific activity towards racemic mandelonitrile compared to the wild type enzyme
F125T/Y133F
the mutant shows higher specific activity towards racemic mandelonitrile compared to the wild type enzyme
H103L/W128A
increased activity with the substrate (2S)-hydroxy[4-(methoxy)cyclohex-3-en-1-yl]ethanenitrile compared to the starting clone W128A
H10A
mutation results in a 30000 Da protein with increased electrophoretic mobility on native high percentage (16%) polyacrylamide gels. the mutant enzyme displays almost wild-type specific activity in crude extracts, suggesting that His10 is not crucial for activity. However, activity is almost completely lost during purification, supporting the possibility that the H10A exchange has a destabilizing effect and may prevent formation of an active dimer of the enzyme after purification
I12A
mutant yields mostly insoluble protein, which suggests that the substitution hinders protein folding
K236L
inactive mutant protein, three-dimensional structure is similar to wild-type enzyme
K236R
0.15% of wild-type activity
L121F
6.9fold increase in specificity constants (kcat/Km) for racemic mandelonitrile
L121Y/L146M
the mutant shows higher specific activity towards racemic mandelonitrile compared to the wild type enzyme
L146M
the mutant shows lower specific activity towards racemic mandelonitrile compared to the wild type enzyme
L148F
the mutant shows lower specific activity towards racemic mandelonitrile compared to the wild type enzyme
T11A
2% of wild-type activity
V106F
the mutant shows lower specific activity towards racemic mandelonitrile compared to the wild type enzyme
V106F/L121Y
the mutant shows higher specific activity towards racemic mandelonitrile compared to the wild type enzyme
W128A/I219V
very weak activity in cleavage reaction with (2S)-hydroxy[4-(methoxy)cyclohex-3-en-1-yl]ethanenitrile
W128A/K147R
very weak activity in cleavage reaction with (2S)-hydroxy[4-(methoxy)cyclohex-3-en-1-yl]ethanenitrile
W128A/P187L
no activity in cleavage reaction with (2S)-hydroxy[4-(methoxy)cyclohex-3-en-1-yl]ethanenitrile
W128A/Q215H
slightly increased activity with the substrate (2S)-hydroxy[4-(methoxy)cyclohex-3-en-1-yl]ethanenitrile compared to the starting clone W128A
Y133F
the mutant shows lower specific activity towards racemic mandelonitrile compared to the wild type enzyme
D208A
Km-value for 2-hydroxy-2-methylpropanenitrile increases from 101 mM for wild-type enzyme to over 200 mM for the mutant enzyme
G113S
-
enhanced thermal stability compared to wild-type enzyme, mutant enzyme retains slight higher activity than the wild-type enzyme in an acidic environment, so the mutant enzyme maybe more effective for synthesis of (S)-cyanohydrin than the wild-type enzyme
H103C
the mutant displays 9.3fold increase in total specific activity in the cell-free extract compared with the wild type
H103I
the mutant displays 8.1fold increase in total specific activity in the cell-free extract compared with the wild type
H103M
the mutant displays 9.07fold increase in total specific activity in the cell-free extract compared with the wild type
H103Q
the mutant displays 4.06fold increase in total specific activity in the cell-free extract compared with the wild type
H103S
the mutant displays 2.9fold increase in total specific activity in the cell-free extract compared with the wild type
H103T
the mutant displays 3.4fold increase in total specific activity in the cell-free extract compared with the wild type
H103Y
inactive with (S)-mandelonitrile as substrate
H10A
limited decrease in activity
H112A
limited decrease in activity
H236A
mutant enzyme is unable to catalyze the decomposition of 2-hydroxy-2-methylpropanenitrile
H5A
limited decrease in activity
K176P
the mutant displays 2.02fold increase in total specific activity in the cell-free extract compared with the wild type
K176P/K199P/K224P
the mutant displays 6.97fold increase in total specific activity in the cell-free extract compared with the wild type
K176P/K224P
the mutant displays 5.05fold increase in total specific activity in the cell-free extract compared with the wild type
K199P
the mutant displays 1.38fold increase in total specific activity in the cell-free extract compared with the wild type
K199P/K224P
the mutant displays 4.25fold increase in total specific activity in the cell-free extract compared with the wild type
K224P
the mutant displays 2.53fold increase in total specific activity in the cell-free extract compared with the wild type
S80A
mutant enzyme is completely inactive in the 2-hydroxy-2-methylpropanenitrile cleaving assay. No differences to wild type MeHNL according to oligomeric structure, molecular weight, and behavior in the standard purification procedure
T11A
-
specific activity is 24fold lower than that of the wild-type enzyme
H103C/N156G
-
the double mutant is suitable for (S)-mandelonitrile synthesis, improving its enantioselectivity and specific activity. The specific activity of the H103C/N156G mutant enzyme is improved to 154 U/mg from 52 U/mg as compared with wild type enzyme for (S)-mandelonitrile production, and the enantiomeric excess of (S)-mandelonitrile produced by the double mutant is increased to 93% from 55% compared with wild type enzyme
H103C/N156G
the specific activity of the H103C/N156G mutant for (S)-mandelonitrile production is raised to 154 U/mg (wild-type hydroxynitrile lyase: 52 U/mg). The enantiomeric excess is increased to 93% (wild-type: 55%). Km-value for (R)-mandelonitrile and kcat for (S)-mandelonitrile increase by the mutation at Asn156, thus contributing to the increase in enantiomeric excess
C81L
1.3fold increase in kcat for racemic mandelonitrile
C81L
the mutant has high enantioselectivity towards (R)-mandelonitrile with a kcat value 1.3times higher compared to the wild type enzyme
C81S
3% of wild-type activity
C81S
no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing. Mutation does not change the charge or size of the amino acid side chain, but nevertheless greatly reduces activity
E79A
1% of wild-type activity
E79A
no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing. Mutation greatly reduces, but does not abolish activity. The negative charge provided by Glu-79 may be required in the active site, but a direct participation of this residue in enzyme catalysis is not suggested
F125T
2.6fold increase in kcat for racemic mandelonitrile, 4.5fold increase in specificity constants (kcat/Km) for racemic mandelonitrile
F125T
the mutant has high enantioselectivity towards (R)-mandelonitrile with a kcat value 2.6times and a kcat/Km value 4.5times higher compared to the wild type enzyme
F210I
mutant yields mostly insoluble protein, which suggests that the substitution hinders protein folding
F210I
the mutant shows lower specific activity towards racemic mandelonitrile compared to the wild type enzyme
H235A
no activity
H235A
inactive mutant enzyme, no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing
I209A
3.9fold increase in specificity constants (kcat/Km) for racemic mandelonitrile
I209A
the mutant has higher enantioselectivity towards (R)-mandelonitrile with a kcat/Km value 3.9times higher compared to the wild type enzyme
I209G
mutant yields mostly insoluble protein, which suggests that the substitution hinders protein folding, moderate substrate inhibition by rac-mandelonitrile
I209G
the mutant shows lower specific activity towards racemic mandelonitrile compared to the wild type enzyme
L121Y
5.3fold increase in specificity constants (kcat/Km) for racemic mandelonitrile, 4.2fold increase in kcat for racemic mandelonitrile, the mutant enzyme shows the same high (S)-enantioselectivity (98% ee) as wild-type enzyme. The mutant catalyzes the cleavage of 2-nitro-1-phenylethanol 4.8 times more efficiently than the wild type enzyme, this is similar to the 4.5-fold increase seen for mandelonitrile cleavage
L121Y
the mutant has high enantioselectivity towards (S)-mandelonitrile with a kcat value 4.2times higher and a kcat/Km value 5.3times higher compared to the wild type enzyme
L121Y/F125T
1.7fold increase in kcat for racemic mandelonitrile, 1.9fold increase in specificity constants (kcat/Km) for racemic mandelonitrile
L121Y/F125T
the mutant has high enantioselectivity towards (R)-mandelonitrile with a kcat value 4.2times higher and a kcat/Km value 1.7times higher compared to the wild type enzyme
L121Y/F125T
the mutant shows higher specific activity towards racemic mandelonitrile compared to the wild type enzyme
L121Y/F125T/L146M
5.5fold increase in activity over the wild type enzyme
L121Y/F125T/L146M
the mutant shows higher specific activity towards racemic mandelonitrile compared to the wild type enzyme
L152F
1.5fold increase in specificity constants (kcat/Km) for racemic mandelonitrile
L152F
the mutant has higher enantioselectivity towards (R)-mandelonitrile with a kcat/Km value 1.5times higher compared to the wild type enzyme
S80A
no activity
S80A
no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing
V106F/L121Y/F125T
3.3fold increase in kcat for racemic mandelonitrile, 5.5fold increase in specificity constants (kcat/Km) for racemic mandelonitrile
V106F/L121Y/F125T
the mutant has high enantioselectivity towards (R)-mandelonitrile with a kcat value 3.3times higher compared to the wild type enzyme
W128A
higher conversion and better selectivity than wild-type enzyme with the substrate 4-methoxycyclohex-3-ene-1-carbaldehyde
W128A
lower conversion and lower selectivity than wild-type enzyme with the substrate 4-methoxycyclohex-3-ene-1-carbaldehyde
C81A
-
specific activity is 93% of the wild-type value
C81A
the mutant is also inhibited by acetate
H103L
-
highly active and soluble mutant
H103L
the mutant displays 11.1fold increase in total specific activity in the cell-free extract compared with the wild type
W128A
-
mutant enzyme is (S)-selective as the wild-type enzyme
W128A
activity with the natural substrate 2-hydroxy-2-methylpropanenitrile (acetone cyanohydrin) is 70% of wild-type activity. The specific activities of MeHNL-W128A for the unnatural substrates mandelonitrile and 4-hydroxymandelonitrile are increased 9fold and 450fold, respectively, compared with the wild-type. The crystal structure of the mutant W128A substrate free form at 2.1 A resolution indicates that the W128A substitution has significantly enlarged the active-site channel entrance, and thereby explains the observed changes in substrate specificity for bulky substrates
W128A
although the variant W128A shows a higher activity with respect to (S)-3-phenoxy-benzaldehyde cyanohydrin, the enantioselectivity is reduced to 85%, compared to 97% of wild-type enzyme
W128A
substitution of tryptophan128 by an alanine residue enlarges the entrance channel to the active site of MeHNL and thus facilitates access of sterically demanding substrates to the active site, increased conversion rate towards 3-phenoxybenzaldehyde, octan-3-one and heptan-3-one
W128C
-
mutant enzyme is (S)-selective as the wild-type enzyme
W128C
mutation increases the specific activity towards 4-hydroxymandelonitrile of the various MeHNL mutant compared to the wild-type enzyme
W128L
-
mutant enzyme is (S)-selective as the wild-type enzyme
W128L
mutation increases the specific activity towards 4-hydroxymandelonitrile of the various MeHNL mutant compared to the wild-type enzyme
W128Y
-
mutant enzyme is (S)-selective as the wild-type enzyme
W128Y
mutation increases the specific activity towards 4-hydroxymandelonitrile of the various MeHNL mutant compared to the wild-type enzyme
additional information
C-terminally truncated enzymes exhibit activities of 75, 102, 65 and 48 U/l for enzyme after removing 2, 4, 6, and 8 amino acids, respectively
additional information
-
C-terminally truncated enzymes exhibit activities of 75, 102, 65 and 48 U/l for enzyme after removing 2, 4, 6, and 8 amino acids, respectively
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Selmar, D.; Lieberei, R.; Biehl, B.; Conn, E.E.
alpha-Hydroxynitrile lyase in Hevea brasiliensis and its significance for rapid cyanogenesis
Physiol. Plant.
75
97-101
1989
Hevea brasiliensis
-
brenda
White, W.L.B.; Ariaz-Garzon, D.I.; McMahon, J.M.; Sayre, R.T.
Cyanogenesis in Cassava. The role of hydroxynitrile lyase in root cyanide production
Plant Physiol.
116
1219-1225
1998
Manihot esculenta (P52705)
brenda
Lauble, H.; Decanniere, K.; Wajant, H.; Frster, S.; Effenberger, F.
Crystallization and preliminary X-ray diffraction analysis of hydroxynitrile lyase from cassava (manihot esculenta)
Acta Crystallogr. Sect. D
55
904-906
1999
Manihot esculenta
-
brenda
Wagner, U.G.; Hasslacher, M.; Griengl, H.; Schwab, H.; Kratky, C.
Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis
Structure
4
811-822
1996
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2003
Hevea brasiliensis
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2001
Hevea brasiliensis
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Hevea brasiliensis
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Hydroxynitrile lyase catalyzed enantioselective HCN addition to O-protected alpha-hydroxyaldehydes
Tetrahedron Asymmetry
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1999
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2005
Manihot esculenta
brenda
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Hevea brasiliensis (P52704), Hevea brasiliensis
brenda
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Hevea brasiliensis (P52704), Hevea brasiliensis
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Over-expression of hydroxynitrile lyase in transgenic cassava roots accelerates cyanogenesis and food detoxification
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2004
Manihot esculenta
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2004
Hevea brasiliensis
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brenda
Veum, L.; Hanefeld, U.; Pierre, A.
The first encapsulation of hydroxynitrile lyase from Hevea brasiliensis in a sol-gel matrix
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60
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2004
Hevea brasiliensis
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brenda
Cabirol, F.L.; Hanefeld, U.; Sheldon, R.A.
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2006
Hevea brasiliensis
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Purkarthofer, T.; Skranc, W.; Schuster, C.; Griengl, H.
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2007
Hevea brasiliensis
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2007
Hevea brasiliensis (P52704)
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Rustler, S.; Motejadded, H.; Altenbuchner, J.; Stolz, A.
Simultaneous expression of an arylacetonitrilase from Pseudomonas fluorescens and a (S)-oxynitrilase from Manihot esculenta in Pichia pastoris for the synthesis of (S)-mandelic acid
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2008
Manihot esculenta
brenda
von Langermann, J.; Guterl, J.K.; Pohl, M.; Wajant, H.; Kragl, U.
Hydroxynitrile lyase catalyzed cyanohydrin synthesis at high pH-values
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31
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2008
Manihot esculenta (P52705), Manihot esculenta
brenda
Semba, H.; Dobashi, Y.; Matsui, T.
Expression of hydroxynitrile lyase from Manihot esculenta in yeast and its application in (S)-mandelonitrile production using an immobilized enzyme reactor
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2008
Manihot esculenta (P52705), Manihot esculenta
brenda
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Enzymatic synthesis of optically pure cyanohydrins in microchannels using a crude cell lysate
Chem. Eng. J.
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2008
Hevea brasiliensis
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brenda
Avi, M.; Wiedner, R.M.; Griengl, H.; Schwab, H.
Improvement of a stereoselective biocatalytic synthesis by substrate and enzyme engineering: 2-hydroxy-(4-oxocyclohexyl)acetonitrile as the model
Chemistry
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2008
Hevea brasiliensis (P52704)
brenda
Schmidt, A.; Gruber, K.; Kratky, C.; Lamzin, V.S.
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Hevea brasiliensis (P52704)
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Ueberbacher, B.J.; Griengl, H.; Weber, H.
Chemo-enzymatic synthesis of new ferrocenyl-oxazolidinones and their application as chiral auxiliaries
Tetrahedron Asymmetry
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2008
Hevea brasiliensis (P52704)
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brenda
Wagner, U.G.; Schall, M.; Hasslacher, M.; Hayn, M.; Griengl, H.; Schwab, H.; Kratky, C.
Crystallization and preliminary X-ray diffraction studies of a hydroxynitrile lyase from Hevea brasiliensis
Acta Crystallogr. Sect. D
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1996
Hevea brasiliensis (P52704)
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Van Pelt, S.; Van Rantwijk, F.; Sheldon, R.
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Manihot esculenta
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Bauer, M.; Griengl, H.; Steiner, W.
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Hevea brasiliensis (P52704), Hevea brasiliensis
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Manihot esculenta (P52705)
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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
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2007
Hevea brasiliensis (P52704)
brenda
Hickel, A.; Graupner, M.; Lehner, D.; Hemnetter, A.; Glatter, O.; Griengl, H.
Stability of the hydroxynitrile lyase from Hevea brasiliensis: a fluorescence and dynamic light scattering study
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1997
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Wajant, H.; Pfizenmaier, K.
Identification of potential active-site residues in the hydroxynitrile lyase from Manihot esculenta by site-directed mutagenesis
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Hasslacher, M.; Schall, M.; Hayn, M.; Griengl, H.; Kohlwein, S.D.; Schwab, H.
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Hevea brasiliensis (P52704), Hevea brasiliensis
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Hevea brasiliensis (P52704), Hevea brasiliensis
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Guterl, J.K.
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Hevea brasiliensis (P52704)
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Cui, F.C.; Pan, X.L.; Liu, J.Y.
Catalytic mechanism of hydroxynitrile lyase from Hevea brasiliensis: a theoretical investigation
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Hevea brasiliensis, Hevea brasiliensis (P52704)
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Hasslacher, M.; Kratky, C.; Griengl, H.; Schwab, H.; Kohlwein, S.D.
Hydroxynitrile lyase from Hevea brasiliensis: molecular characterization and mechanism of enzyme catalysis
Proteins
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1997
Hevea brasiliensis (P52704), Hevea brasiliensis
brenda
Frhlich, R.F.G.; Zabelinskaja-Mackova, A.A.; Fechter, M.H.; Griengl, H.
Novel access to chiral 1,1'-disubstituted ferrocene derivatives via double stereoselective cyanohydrin synthesis exploiting the hydroxynitrile lyase from Hevea brasiliensis
Tetrahedron Asymmetry
14
355-362
2003
Hevea brasiliensis (P52704)
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brenda
Klempier, N.; Pichler, U.; Griengl, H.
Synthesis of alpha,beta-unsaturated (S)-cyanohydrins using the oxynitrilase from Hevea brasiliensis
Tetrahedron Asymmetry
6
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1995
Hevea brasiliensis (P52704)
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Schmidt, M.; Herve, S.; KLempier, N.; Griengl, H.
Preparation of optically active cyanohydrins using the (S)-hydroxynitrile lyase from Hevea brasiliensis
Tetrahedron
52
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1996
Hevea brasiliensis (P52704)
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brenda
Yuryev, R.; Purkarthofer, T.; Gruber, M.; Griengl, H.; Liese, A.
Kinetic studies of the asymmetric Henry reaction catalyzed by hydroxynitrile lyase from Hevea brasiliensis
Biocatal. Biotransform.
28
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2010
Hevea brasiliensis
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brenda
Yuryev, R.; Briechle, S.; Gruber-Khadjawi, M.; Griengl, H.; Liese, A.
Asymmetric retro-Henry reaction catalyzed by hydroxynitrile lyase from Hevea brasiliensis
ChemCatChem
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2010
Hevea brasiliensis
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Semba, H.; Ichige, E.; Imanaka, T.; Atomi, H.; Aoyagi, H.
Efficient production of active form recombinant cassava hydroxynitrile lyase using Escherichia coli in low-temperature culture
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2010
Manihot esculenta (P52705), Manihot esculenta
brenda
Dadashipour, M.; Fukuta, Y.; Asano, Y.
Comparative expression of wild-type and highly soluble mutant His103Leu of hydroxynitrile lyase from Manihot esculenta in prokaryotic and eukaryotic expression systems
Protein Expr. Purif.
77
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2010
Manihot esculenta
brenda
Padhi, S.K.; Fujii, R.; Legatt, G.A.; Fossum, S.L.; Berchtold, R.; Kazlauskas, R.J.
Switching from an esterase to a hydroxynitrile lyase mechanism requires only two amino acid substitutions
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2010
Hevea brasiliensis, Manihot esculenta
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Narayanan, N.N.; Ihemere, U.; Ellery, C.; Sayre, R.T.
Overexpression of hydroxynitrile lyase in cassava roots elevates protein and free amino acids while reducing residual cyanogen levels
PLoS ONE
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Manihot esculenta
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Asano, Y.; Dadashipour, M.; Yamazaki, M.; Doi, N.; Komeda, H.
Functional expression of a plant hydroxynitrile lyase in Escherichia coli by directed evolution: creation and characterization of highly in vivo soluble mutants
Protein Eng. Des. Sel.
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2011
Manihot esculenta (P52705)
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Dadashipour, M.; Yamazaki, M.; Momonoi, K.; Tamura, K.; Fuhshuku, K.; Kanase, Y.; Uchimura, E.; Kaiyun, G.; Asano, Y.
S-selective hydroxynitrile lyase from a plant Baliospermum montanum: molecular characterization of recombinant enzyme
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2011
Baliospermum montanum (D1MX73), Baliospermum montanum
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Von Langermann, J.; Wapenhensch, S.
Hydroxynitrile lyase-catalyzed synthesis of enantiopure cyanohydrins in Biocatalytic Active Static Emulsions (BASE) with suppression of the non-enzymatic side reaction
Adv. Synth. Catal.
356
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2014
Manihot esculenta (P52705)
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Nakano, S.; Dadashipour, M.; Asano, Y.
Structural and functional analysis of hydroxynitrile lyase from Baliospermum montanum with crystal structure, molecular dynamics and enzyme kinetics
Biochim. Biophys. Acta
1844
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2014
Baliospermum montanum (D1MX73), Baliospermum montanum, Manihot esculenta (P52705), Manihot esculenta
brenda
von Langermann, J.; Nedrud, D.M.; Kazlauskas, R.J.
Increasing the reaction rate of hydroxynitrile lyase from Hevea brasiliensis toward mandelonitrile by copying active site residues from an esterase that accepts aromatic esters
ChemBioChem
15
1931-1938
2014
Hevea brasiliensis (P52704), Hevea brasiliensis
brenda
Kawahara, N.; Asano, Y.
Mutagenesis of an Asn156 residue in a surface region of S-selective hydroxynitrile lyase from Baliospermum montanum enhances catalytic efficiency and enantioselectivity
ChemBioChem
16
1891-1895
2015
Baliospermum montanum (D1MX73), Baliospermum montanum
brenda
Asano, Y.; Kawahara, N.
A new S-hydroxynitrile lyase from Baliospermum montanum - its structure, molecular dynamics simulation, and improvement by protein engineering
Ind. Biotechnol.
12
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2016
Baliospermum montanum
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brenda
Van Rantwijk, F.; Stolz, A.
Enzymatic cascade synthesis of (S)-2-hydroxycarboxylic amides and acids Cascade reactions employing a hydroxynitrile lyase, nitrile-converting enzymes and an amidase
J. Mol. Catal. B
114
25-30
2015
Manihot esculenta (P52705)
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Rauwerdink, A.; Lunzer, M.; Devamani, T.; Jones, B.; Mooney, J.; Zhang, Z.J.; Xu, J.H.; Kazlauskas, R.J.; Dean, A.M.
Evolution of a catalytic mechanism
Mol. Biol. Evol.
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2016
Hevea brasiliensis
brenda
Zhao, Y.; Chen, N.; Mo, Y.; Cao, Z.
A full picture of enzymatic catalysis by hydroxynitrile lyases from Hevea brasiliensis Protonation dependent reaction steps and residue-gated movement of the substrate and the product
Phys. Chem. Chem. Phys.
16
26864-26875
2014
Hevea brasiliensis (P52704)
brenda