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(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbamide
(1R,3R)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-3-phenylcyclopropanecarbamide
(1R,3S)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3S)-3-phenylcyclopropanecarbamide
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbonitrile + H2O
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbamide
(25R)-3beta-hydroxycholest-5-en-27-oate
?
-
-
-
-
?
(2R)-2-hydroxy-3-methylbutanenitrile + H2O
(2R)-2-hydroxy-3-methylbutanamide
-
-
-
-
?
(2R)-2-hydroxybut-3-enenitrile + H2O
(2R)-2-hydroxybut-3-enamide
-
-
-
-
?
(2R)-2-hydroxybutanenitrile + H2O
(2R)-2-hydroxybutanamide
-
-
-
-
?
(2R)-2-hydroxyhexanenitrile + H2O
(2R)-2-hydroxyhexanamide
-
-
-
-
?
(2R)-2-hydroxypentanenitrile + H2O
(2R)-2-hydroxypentanamide
-
-
-
-
?
(R)-2-chloromandelonitrile + H2O
(R)-2-chloromandelamide
at 100% the rate of 2-hydroxy-4-phenylbutyronitrile
-
-
?
(R)-mandelonitrile + H2O
(R)-mandelamide
(R,S)-2-(4-nitrophenyl)-propionitrile + H2O
?
-
39% conversion
-
-
?
(R,S)-2-bromopropionitrile + H2O
?
-
47% conversion
-
-
?
(R,S)-2-chloropropionitrile + H2O
?
-
48% conversion
-
-
?
(R,S)-2-phenylbutyronitrile + H2O
?
-
51% conversion
-
-
?
(R,S)-2-phenylpropionitrile + H2O
?
-
43% conversion
-
-
?
(R,S)-3-oxo-2-phenylbutyronitrile + H2O
?
-
43% conversion
-
-
?
(S)-3-benzoyloxypentanedinitrile + H2O
3-amino-1-(2-amino-2-oxoethyl)-3-oxopropyl benzoate
-
substrate conversion: 38.5%, enantiomeric excess: 68.2
-
-
r
(S)-mandelonitrile + H2O
(S)-mandelamide
1,1,3,3,-tetramethylbutylisonitrile + H2O
1,1,3,3,-tetramethylisobutylamide
1-(4-bromo-phenyl)-aziridine-2-carbonitrile + H2O
1-(4-bromophenyl)aziridine-2-carboxamide
-
-
-
-
r
1-(4-methoxy-phenyl)-aziridine-2-carbonitrile + H2O
1-(4-methoxyphenyl)aziridine-2-carboxamide
-
-
-
-
r
1-cyanocyclohexaneacetonitrile + H2O
1-cyanocyclohexaneacetamide
1-naphthylnitrile + H2O
1-naphthylamide
17alpha-cyanomethyl-17beta-hydroxy-estra-4,9-dien-3-one + H2O
17alpha-acetamido-estra-1,3,5(10),9(11)-tetraene-3,17beta-diol
-
the steroidal group is metabolized very slowly
-
?
2(R)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(R)-(4-chloro-phenyl)-3-methyl-butyramide
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
2,2-dimethylcyclopropanecarbonitrile + H2O
?
2,3,4,5,6-pentafluorobenzonitrile + H2O
2,3,4,5,6-pentafluorobenzamide
-
-
-
-
?
2,3-dihydro-benzo(1,4)dioxine-2-carbonitrile + H2O
2,3-dihydro-1,4-benzodioxine-2-carboxamide
-
substrate conversion: 45.1%, enantiomeric excess: 0
-
-
r
2,6-dichlorobenzamide + H2O
2,6-dichlorobenzoic acid
2,6-difluorobenzonitrile + H2O
2,6-difluorobenzamide
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
2-aminopropionitrile + H2O
2-aminopropionic acid amide
-
90% of the activity with propionitrile
-
-
?
2-bromobenzonitrile + H2O
2-bromobenzamide
-
-
-
-
ir
2-chlorobenzaldehyde + HCN + H2O
(R)-2-chloromandelonitrile
-
-
90% conversion to alpha-hydroxy nitrile
-
?
2-chlorobenzonitrile + H2O
2-chlorobenzamide
-
-
-
-
ir
2-cyanobenzamide + H2O
benzene-1,2-dicarboxamide
2-cyanopyridine + H2O
pyridine-2-carbamide
2-fluorobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
2-fluorobenzonitrile + H2O
2-fluorobenzamide
-
-
-
-
ir
2-furonitrile + H2O
2-furoamide
2-hydroxy-4-phenylbutanenitrile + H2O
?
-
-
-
?
2-hydroxy-4-phenylbutyronitrile + H2O
2-hydroxy-4-phenylbutyramide
-
-
-
?
2-hydroxymethyl-3-phenyl-propionitrile + H2O
2-benzyl-3-hydroxypropanamide
-
-
-
-
r
2-hydroxypropionitrile + H2O
2-hydroxypropionic acid amide
2-methoxybenzonitrile + H2O
2-methoxybenzamide
-
-
-
-
ir
2-methoxymethyl-3-phenyl-propionitrile + H2O
2-benzyl-3-methoxypropanamide
-
-
-
-
r
2-methyl-3-butenenitrile + H2O
?
2-methylbenzonitrile + H2O
2-methylbenzamide
-
-
-
-
ir
2-naphthylacetonitrile + H2O
2-naphthylacetamide
2-nitro-5-thiocyanato-benzoic acid + H2O
?
-
-
-
-
?
2-nitrobenzaldehyde + HCN + H2O
? + H2O
-
-
20% conversion to alpha-hydroxy nitrile
-
?
2-phenylacetonitrile + H2O
2-phenylpropionamide
-
-
-
-
?
2-phenylbutyronitrile + H2O
2-phenylbutyramide
-
used as well as phenylacetonitrile
-
-
?
2-phenylglycinonitrile + H2O
aminoacetamide
-
used as well as phenylacetonitrile
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
3,4,5-trimethoxybenzonitrile + H2O
3,4,5-trimethoxybenzamide
3,4-dimethoxybenzonitrile + H2O
3,4-dimethoxybenzaldehyde + NH3
3-(1-cyanoethyl)benzoic acid + H2O
?
3-(trifluoromethyl)benzonitrile + H2O
3-(trifluoromethyl)benzamide
3-(trifluoromethyl)pyridine-4-carbonitrile + H2O
3-(trifluoromethyl)pyridine-4-carboxamide
-
-
-
-
ir
3-allyloxy-4-phenyl-butyronitrile + H2O
4-phenyl-3-(prop-2-en-1-yloxy)butanamide
-
-
-
-
r
3-aminopropionitrile + H2O
3-aminopropionic acid amide
-
2.7% of the activity with propionitrile
-
-
?
3-benzoyloxyglutaronitrile + H2O
(S)-3-benzoyloxy-4-cyanobutyramide
3-benzyloxy-3-vinyl-propionitrile + H2O
3-(benzyloxy)pent-4-enamide
-
-
-
-
r
3-benzyloxy-pentanonitrile + H2O
3-(benzyloxy)pentanamide
-
-
-
-
r
3-benzyloxyglutaronitrile + H2O
3-benzyloxy-4-cyanobutyramide
3-bromobenzonitrile + H2O
3-bromobenzamide
-
5% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-chlorobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
3-chlorobenzonitrile + H2O
3-chlorobenzamide
3-cyanopyridine + H2O
nicotinamide
3-cyanopyridine + H2O
pyridine-3-carbamide
3-cyanopyridine + H2O
pyridine-3-carboxamide
3-fluorobenzonitrile + H2O
3-fluorobenzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-hydroxy-3-phenylpropionitrile + H2O
3-hydroxy-3-phenylpropionamide
3-hydroxybenzonitrile + H2O
3-hydroxybenzamide
3-hydroxybutryronitrile + H2O
3-hydroxybutyramide
3-hydroxypropionitrile + H2O
3-hydroxypropanamide
-
35% of the activity with propionitrile
-
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropionamide
3-hydroxyvaleronitrile + H2O
3-hydroxyvaleramide
3-methoxybenzonitrile + H2O
3-methoxybenzamide
-
3% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-methylbenzonitrile + H2O
3-methylbenzamide
3-phenoxymandelonitrile + H2O
3-phenoxymandelamine
at 10% the rate of 2-hydroxy-4-phenylbutyronitrile
-
-
?
3-phenylpropanenitrile + H2O
3-phenylpropanamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
3-phenylpropionitrile + H2O
3-phenylpropionamide
-
used as well as phenylacetonitrile
-
-
?
4-(trifluoromethyl)benzonitrile + H2O
4-(trifluoromethyl)benzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
4-acetylbenzonitrile + H2O
4-acetylbenzamide
-
above 99% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
4-aminobenzonitrile + H2O
4-aminobenzamide
4-bromobenzonitrile + H2O
4-bromobenzamide
4-chloro-3-hydroxybutanenitrile + H2O
?
-
-
-
?
4-chloro-3-hydroxybutyronitrile + H2O
4-chloro-3-hydroxybutyramide
-
the following reaction by an amidase leads to the correspondend carboxylic acid
-
-
?
4-chlorobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
4-chlorobenzonitrile + H2O
4-chlorbenzamide
-
-
-
-
ir
4-chlorobenzonitrile + H2O
4-chlorobenzamide
4-chlorobutyronitrile + H2O
4-chlorobutyramide
-
-
-
?
4-cyanobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
4-cyanobenzamide + H2O
benzene-1,4-dicarboxamide
4-cyanobenzoic acid + H2O
4-(aminocarbonyl)benzoic acid
-
-
-
-
?
4-cyanopyridine + H2O
isonicotinamide
4-fluorobenzonitrile + H2O
4-fluorbenzamide
-
-
-
-
ir
4-fluorobenzonitrile + H2O
4-fluorobenzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-hydroxybenzaldehyde + HCN + H2O
? + H2O
-
-
55% conversion to alpha-hydroxy nitrile
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzamide
-
-
-
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid amide
4-hydroxyphenylacetonitrile + H2O
4-hydroxyphenylacetamide
4-methoxybenzonitrile + H2O
4-methoxybenzamide
-
above 99% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
4-methylbenzaldehyde + HCN + H2O
? + H2O
-
-
51% conversion to alpha-hydroxy nitrile
-
?
4-methylbenzonitrile + H2O
4-methylbenzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
4-methylmandelonitrile + H2O
4-methylmandelamine
at 60% the rate of 2-hydroxy-4-phenylbutyronitrile
-
-
?
4-nitrobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
5-cyanovaleramide
adiponitrile + H2O
5-cyanovaleric acid + H2O
6-amino-6-oxohexanoic acid
-
NilFe and NilCo
-
-
r
5-hydroxymethyl-2-furonitrile + H2O
5-hydroxymethyl-2-furamide
acetamiprid + H2O
(1E)-N'-carbamoyl-N-[(6-chloropyridin-3-yl)methyl]-N-methylethanimidamide
hydration at 22.41% compared to the activity with thiacloprid
-
-
?
acetonitrile + H2O
acetamide
acrylamide + H2O
acrylonitrile
acrylonitrile + H2O
2-propenoic acid amide
acrylonitrile + H2O
acrylamide
adiponitrile + 2 H2O
adipamide
adiponitrile + 2 H2O
adipic acid amide
adiponitrile + H2O
5-cyanovaleramide
aeroplysinin-1 + H2O
verongiaquinol
-
high substrate specificity towards the physiological substrate aeroplysinin-1
-
-
?
alpha-methylbenzyl cyanide + H2O
2-phenylpropanamide
an aliphatic amide
a nitrile + H2O
benzaldehyde + HCN
? + H2O
-
-
95% conversion to alpha-hydroxy nitrile
-
?
benzeneacetonitrile + H2O
?
very low activity
-
-
?
benzonitrile + H2O
benzamide
benzonitrile + H2O
benzoic acid amide
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
benzyl cyanide + H2O
2-phenylacetamide
85% of the activity compared to 3-cyanopyridine
-
-
?
benzylcyanide + H2O
2-phenylacetamide
-
-
-
-
r
butyronitrile + H2O
?
-
-
-
?
butyronitrile + H2O
butyramide
butyronitrile + H2O
butyric acid amide
-
best substrate
-
-
?
chloroacetonitrile + H2O
chloroacetamide
chloroxynil amide + H2O
?
crotononitrile + H2O
(E)-2-butenoic acid amide
cyanamide + H2O
urea
-
-
-
?
cyanoacetamide
malononitrile + H2O
-
-
-
r
cyanopyrazine + H2O
pyrazincarbamide
-
-
-
-
?
cyanovaleramide
valerodinitrile + H2O
cyanovaleric acid + H2O
?
cyclopropylcyanide + H2O
?
-
-
-
-
?
dichlobenil acid + H2O
?
-
-
-
-
?
dichlobenil amide + H2O
?
ethyl 2-cyanobenzoate + H2O
ethyl 2-carbamoylbenzoate
-
-
-
-
ir
ethyl 3-cyanobenzoate + H2O
ethyl 3-carbamoylbenzoate
-
no conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
ethyl 4-cyanobenzoate + H2O
ethyl 4-carbamoylbenzoate
-
95% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
ethylene cyanhydrine + H2O
?
furan-2-carbonitrile + H2O
furan-2-carboxamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
glutaronitrile + H2O
?
-
38% of the activity with propionitrile
-
-
?
glycolonitrile + H2O
glycolamide
-
yield 63%
-
?
hexanedinitrile + H2O
?
hydration at 0.43% compared to the activity with thiacloprid
-
-
?
hydroxyacetonitrile + H2O
hydroxyacetamide
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
indole-3-acetonitrile + H2O
indole-3-acetamide
indole-3-nitrile + H2O
indole-3-acetamide
isobutyronitrile + H2O
?
-
-
-
?
isobutyronitrile + H2O
isobutyramide
isobutyronitrile + H2O
isobutyric acid amide
isovaleronitrile + H2O
isovaleric acid amide
malonitrile + H2O
?
-
44% of the activity with propionitrile
-
-
?
malononitrile + 2 H2O
malonamide
the use of the wild-type enzyme leads to malonamide formation with 97.3% malononitrile conversion. Variants Y68T and W72Y show a drastic change in regiospecificity by producing mainly the omega-cyanocarboxamide, cyanoacetamide, at a relatively low malononitrile conversion. Mutant enzyme Y68T/W72Y produces 97.1% omega-cyanocarboxamide
-
-
?
malononitrile + H2O
cyanoacetamide
the use of the wild-type enzyme leads to malonamide formation with 97.3% malononitrile conversion. Variants Y68T and W72Y show a drastic change in regiospecificity by producing mainly the omega-cyanocarboxamide, cyanoacetamide, at a relatively low malononitrile conversion. Mutant enzyme Y68T/W72Y produces 97.1% omega-cyanocarboxamide
-
-
r
methacrylonitrile + H2O
?
-
-
-
?
methacrylonitrile + H2O
methacrylamide
methacrylonitrile + H2O
methacrylic acid amide
-
-
-
-
?
methacrylonitrile + H2O
methylacrylamide
methacrylonitrile + H2O
methylacrylic acid amide
methoxyacetonitrile + H2O
?
-
-
-
-
?
methyl 4-cyanobenzoate + H2O
methyl 4-carbamoylbenzoate
-
98% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
n-butyronitrile + H2O
n-butyramide
-
-
-
-
r
n-butyronitrile + H2O
n-butyric acid amide
n-capronitrile + H2O
n-hexanoic acid amide
N-phenylglycinenitrile + H2O
?
-
-
-
-
?
n-valeronitrile + H2O
n-valeramide
nicotinonitrile + H2O
nicotinamide
o-chlorobenzonitrile + H2O
o-chlorobenzamide
p-aminobenzonitrile + H2O
p-aminobenzamide
-
conversion rate: 8.98%
-
-
?
p-chlorobenzonitrile + H2O
p-chlorobenzamide
-
conversion rate: 93.1%
-
-
?
p-hydroxybenzylcyanide + H2O
2-(4-hydroxyphenyl)acetamide
-
-
-
-
?
phenylacetonitrile + 2 H2O
phenylacetic acid + NH3
-
-
-
?
phenylacetonitrile + H2O
2-phenylacetamide
-
28% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
phenylacetonitrile + H2O
phenylacetamide
phthalodinitrile + 2 H2O
phthalamide
the wild-type enzyme forms 100% phthalamide from phthalodinitrile. The mutant enzymes Y68T and W72Y result in a higher 2-cyanobenzamide formation than their parent enzyme. Mutant enzyme Y68T/W72Y produces 100% 2-cyanobenzamide from phthalodinitrile
-
-
?
phthalodinitrile + H2O
2-cyanobenzamide
the wild-type enzyme forms 100% phthalamide from phthalodinitrile. The mutant enzymes Y68T and W72Y result in a higher 2-cyanobenzamide formation than their parent enzyme. Mutant enzyme Y68T/W72Y produces 100% 2-cyanobenzamide from phthalodinitrile
-
-
?
phthalonitrile + H2O
2-cyanobenzamide
-
lowest activity
-
-
?
phthalonitrile + H2O
?
-
-
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
propionitrile + H2O
propionamide
propionitrile + H2O
propionic acid amide
pyridine-2-carbonitrile + H2O
pyridine-2-carboxamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
pyridine-4-carbonitrile + H2O
pyridine-4-carboxamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
terephthalonitrile + 2 H2O
terephthalamide
the wild-type enzyme prefers terephthalonitrile to catalyze mainly into terephthalamide (84.3%) with a conversion up to 99.2 %. Variants Y68T and W72Y show a change in regiospecificity by producing mainly the 4-cyanobenzamide. Mutant enzyme Y68T/W72Y produces 98.2% 4-cyanobenzamide from terephthalonitrile
-
-
?
terephthalonitrile + H2O
4-cyanobenzamide
the wild-type enzyme prefers terephthalonitrile to catalyze mainly into terephthalamide (84.3%) with a conversion up to 99.2 %. Variants Y68T and W72Y show a change in regiospecificity by producing mainly the 4-cyanobenzamide. Mutant enzyme Y68T/W72Y produces 98.2% 4-cyanobenzamide from terephthalonitrile
-
-
?
tert-butylisonitrile + H2O
?
-
-
-
?
tert-butylisonitrile + H2O
tert-butyl amide
thiacloprid + H2O
1-[(2Z)-3-[(6-chloropyridin-3-yl)methyl]-1,3-thiazolidin-2-ylidene]urea
-
-
-
?
thiophen-2-ylacetonitrile + H2O
2-(thiophen-2-yl)acetamide
-
89% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
thiophene-2-carbonitrile + H2O
thiophen-2-carboxamide
-
-
-
-
ir
thiophene-2-carbonitrile + H2O
thiophene-2-carboxamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
toyocamycin + H2O
toyocamycin acid amide
-
-
-
?
trans-4-cyanocyclohexane-1-carboxylic acid + H2O
4-(aminocarbonyl)cyclohexanecarboxylic acid
trans-cinnamonitrile + H2O
trans-cinnamide
-
-
-
-
?
valeronitrile + H2O
?
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
valeronitrile + H2O
valeramide
additional information
?
-
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbamide
-
substrate conversion: 11.6%, enantiomeric excess: 83.8, 88.9 (methanol), 81.0 (n-hexane)
-
-
r
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbamide
-
substrate conversion: 11.6%, enantiomeric excess: 83.8, 88.9 (methanol), 81.0 (n-hexane)
-
-
r
(1R,3R)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-3-phenylcyclopropanecarbamide
-
substrate conversion: 49.1%, enantiomeric excess: 22.7, 31.1 (methanol), 21.6 (n-hexane)
-
-
r
(1R,3R)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-3-phenylcyclopropanecarbamide
-
substrate conversion: 49.1%, enantiomeric excess: 22.7, 31.1 (methanol), 21.6 (n-hexane)
-
-
r
(1R,3S)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3S)-3-phenylcyclopropanecarbamide
-
substrate conversion: 25.8%, enantiomeric excess: 95.4, 95.4 (methanol), 95.5 (n-hexane)
-
-
r
(1R,3S)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3S)-3-phenylcyclopropanecarbamide
-
substrate conversion: 25.8%, enantiomeric excess: 95.4, 95.4 (methanol), 95.5 (n-hexane)
-
-
r
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbonitrile + H2O
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbamide
-
substrate conversion: 40.3%, enantiomeric excess: 84.7
-
-
r
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbonitrile + H2O
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbamide
-
substrate conversion: 7.9%, enantiomeric excess: 3.2, 5.9 (methanol), 0.7 (n-hexane)
-
-
r
(R)-mandelonitrile + H2O
(R)-mandelamide
wild-type enzyme catalyzes the conversion of rac-mandelonitrile to (S)-mandelamide with an enantiomeric excess of 52.6%
-
-
?
(R)-mandelonitrile + H2O
(R)-mandelamide
wild-type enzyme catalyzes the conversion of rac-mandelonitrile to (S)-mandelamide with an enantiomeric excess of 52.6%
-
-
?
(S)-mandelonitrile + H2O
(S)-mandelamide
wild-type enzyme catalyzes the conversion of rac-mandelonitrile to (S)-mandelamide with an enantiomeric excess of 52.6%
-
-
?
(S)-mandelonitrile + H2O
(S)-mandelamide
wild-type enzyme catalyzes the conversion of rac-mandelonitrile to (S)-mandelamide with an enantiomeric excess of 52.6%
-
-
?
1,1,3,3,-tetramethylbutylisonitrile + H2O
1,1,3,3,-tetramethylisobutylamide
-
-
-
-
?
1,1,3,3,-tetramethylbutylisonitrile + H2O
1,1,3,3,-tetramethylisobutylamide
-
-
-
-
?
1-cyanocyclohexaneacetonitrile + H2O
1-cyanocyclohexaneacetamide
-
-
-
?
1-cyanocyclohexaneacetonitrile + H2O
1-cyanocyclohexaneacetamide
-
-
-
?
1-naphthylnitrile + H2O
1-naphthylamide
-
-
-
-
?
1-naphthylnitrile + H2O
1-naphthylamide
-
-
-
-
?
2(R)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(R)-(4-chloro-phenyl)-3-methyl-butyramide
-
enantioselective hydration
-
?
2(R)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(R)-(4-chloro-phenyl)-3-methyl-butyramide
-
enantioselective hydration
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
-
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
-
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
enantioselective hydration
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
-
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
enantioselective hydration
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
Comamonas oleophilus
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
?
29% of the activity compared to 3-cyanopyridine
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
?
-
-
-
?
2,6-dichlorobenzamide + H2O
2,6-dichlorobenzoic acid
-
-
-
-
?
2,6-dichlorobenzamide + H2O
2,6-dichlorobenzoic acid
-
-
-
-
?
2,6-difluorobenzonitrile + H2O
2,6-difluorobenzamide
-
-
-
-
?
2,6-difluorobenzonitrile + H2O
2,6-difluorobenzamide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-cyanobenzamide + H2O
benzene-1,2-dicarboxamide
-
-
-
?
2-cyanobenzamide + H2O
benzene-1,2-dicarboxamide
-
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
-
-
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
-
-
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
46% of the activity compared to 3-cyanopyridine
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
46% of the activity compared to 3-cyanopyridine
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
-
-
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
-
-
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
-
-
-
-
?
2-furonitrile + H2O
2-furoamide
-
-
-
-
?
2-furonitrile + H2O
2-furoamide
-
-
-
-
?
2-hydroxypropionitrile + H2O
2-hydroxypropionic acid amide
-
i.e. DL-lactonitrile
-
-
?
2-hydroxypropionitrile + H2O
2-hydroxypropionic acid amide
-
116% of the activity with propionitrile
-
-
?
2-methyl-3-butenenitrile + H2O
?
-
-
-
-
?
2-methyl-3-butenenitrile + H2O
?
-
-
-
-
?
2-naphthylacetonitrile + H2O
2-naphthylacetamide
-
-
-
-
?
2-naphthylacetonitrile + H2O
2-naphthylacetamide
-
-
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
used as well as phenylacetonitrile
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is not enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is not enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
-
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
Rhodococcus sp. Novo SP361
-
-
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is highly enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is highly enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is highly enantioselective with the compound
-
-
?
3,4,5-trimethoxybenzonitrile + H2O
3,4,5-trimethoxybenzamide
-
conversion rate: 21.71%
-
-
?
3,4,5-trimethoxybenzonitrile + H2O
3,4,5-trimethoxybenzamide
-
conversion rate: 21.71%
-
-
?
3,4-dimethoxybenzonitrile + H2O
3,4-dimethoxybenzaldehyde + NH3
-
second step with amidase (EC 3.5.1.4)
-
-
?
3,4-dimethoxybenzonitrile + H2O
3,4-dimethoxybenzaldehyde + NH3
Rhodococcus sp. Novo SP361
-
second step with amidase (EC 3.5.1.4)
-
-
?
3-(1-cyanoethyl)benzoic acid + H2O
?
-
the enzyme is enantioselective with the compound
-
-
?
3-(1-cyanoethyl)benzoic acid + H2O
?
-
the enzyme is enantioselective with the compound
-
-
?
3-(1-cyanoethyl)benzoic acid + H2O
?
-
the enzyme is enantioselective with the compound
-
-
?
3-(trifluoromethyl)benzonitrile + H2O
3-(trifluoromethyl)benzamide
-
5% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-(trifluoromethyl)benzonitrile + H2O
3-(trifluoromethyl)benzamide
-
5% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-benzoyloxyglutaronitrile + H2O
(S)-3-benzoyloxy-4-cyanobutyramide
-
enantiomeric excess: 95%, 5 h
-
-
?
3-benzoyloxyglutaronitrile + H2O
(S)-3-benzoyloxy-4-cyanobutyramide
-
enantiomeric excess: 95%, 5 h
-
-
?
3-benzyloxyglutaronitrile + H2O
3-benzyloxy-4-cyanobutyramide
-
enantiomeric excess: 69%, 30 min
-
-
?
3-benzyloxyglutaronitrile + H2O
3-benzyloxy-4-cyanobutyramide
-
enantiomeric excess: 69%, 30 min
-
-
?
3-chlorobenzonitrile + H2O
3-chlorobenzamide
-
-
-
-
?
3-chlorobenzonitrile + H2O
3-chlorobenzamide
-
95% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
3-cyanopyridine + H2O
nicotinamide
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
H-NHase activity
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
H-NHase activity
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
lower activity
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
hydration at 5528% compared to the activity with thiacloprid
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
hydration at 5528% compared to the activity with thiacloprid
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
a niacin precursor
-
-
?
3-cyanopyridine + H2O
pyridine-3-carboxamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carboxamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carboxamide
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carboxamide
-
-
-
?
3-hydroxy-3-phenylpropionitrile + H2O
3-hydroxy-3-phenylpropionamide
-
-
-
-
?
3-hydroxy-3-phenylpropionitrile + H2O
3-hydroxy-3-phenylpropionamide
Rhodococcus sp. Novo SP361
-
-
-
-
?
3-hydroxybenzonitrile + H2O
3-hydroxybenzamide
-
-
-
-
?
3-hydroxybenzonitrile + H2O
3-hydroxybenzamide
-
-
-
-
?
3-hydroxybutryronitrile + H2O
3-hydroxybutyramide
-
yield 99%
-
?
3-hydroxybutryronitrile + H2O
3-hydroxybutyramide
-
yield 99%
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropionamide
-
yield 100%
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropionamide
-
yield 100%
-
?
3-hydroxyvaleronitrile + H2O
3-hydroxyvaleramide
-
yield 99%
-
?
3-hydroxyvaleronitrile + H2O
3-hydroxyvaleramide
-
yield 99%
-
?
3-methylbenzonitrile + H2O
3-methylbenzamide
lower activity
-
-
?
3-methylbenzonitrile + H2O
3-methylbenzamide
-
17% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-tolunitrile + H2O
?
-
-
-
-
?
3-tolunitrile + H2O
?
-
-
-
-
?
4-aminobenzonitrile + H2O
4-aminobenzamide
-
-
-
-
?
4-aminobenzonitrile + H2O
4-aminobenzamide
-
-
-
-
?
4-bromobenzonitrile + H2O
4-bromobenzamide
-
-
-
-
ir
4-bromobenzonitrile + H2O
4-bromobenzamide
-
above 99% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-chlorobenzonitrile + H2O
4-chlorobenzamide
-
-
-
-
?
4-chlorobenzonitrile + H2O
4-chlorobenzamide
-
-
-
-
?
4-chlorobenzonitrile + H2O
4-chlorobenzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-cyanobenzamide + H2O
benzene-1,4-dicarboxamide
-
-
-
?
4-cyanobenzamide + H2O
benzene-1,4-dicarboxamide
-
-
-
?
4-cyanopyridine + H2O
isonicotinamide
-
-
-
-
?
4-cyanopyridine + H2O
isonicotinamide
-
-
-
-
?
4-cyanopyridine + H2O
isonicotinamide
74% of the activity compared to 3-cyanopyridine
-
-
?
4-cyanopyridine + H2O
isonicotinamide
74% of the activity compared to 3-cyanopyridine
-
-
?
4-cyanopyridine + H2O
isonicotinamide
lower activity
-
-
?
4-cyanopyridine + H2O
isonicotinamide
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
4-cyanopyridine + H2O
isonicotinamide
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
4-cyanopyridine + H2O
isonicotinamide
-
-
-
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid amide
-
-
-
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid amide
-
-
-
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid amide
-
-
-
-
?
4-hydroxyphenylacetonitrile + H2O
4-hydroxyphenylacetamide
-
-
-
-
?
4-hydroxyphenylacetonitrile + H2O
4-hydroxyphenylacetamide
-
-
-
-
?
4-hydroxyphenylacetonitrile + H2O
4-hydroxyphenylacetamide
-
-
-
-
?
5-cyanovaleramide
adiponitrile + H2O
-
-
-
r
5-cyanovaleramide
adiponitrile + H2O
-
-
-
r
5-hydroxymethyl-2-furonitrile + H2O
5-hydroxymethyl-2-furamide
-
-
-
-
?
5-hydroxymethyl-2-furonitrile + H2O
5-hydroxymethyl-2-furamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
-
-
ir
acetonitrile + H2O
acetamide
-
-
-
ir
acetonitrile + H2O
acetamide
-
-
-
-
r
acetonitrile + H2O
acetamide
-
10% of the activity with propionitrile
-
-
?
acetonitrile + H2O
acetamide
-
10% of the activity with propionitrile
-
-
?
acetonitrile + H2O
acetamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
-
-
?
acetonitrile + H2O
acetamide
-
-
-
?
acetonitrile + H2O
acetamide
-
-
-
?
acetonitrile + H2O
acetamide
-
very low activity
-
-
?
acetonitrile + H2O
acetamide
-
-
-
?
acetonitrile + H2O
acetamide
-
very low activity
-
-
?
acetonitrile + H2O
acetamide
-
-
-
-
r
acetonitrile + H2O
acetamide
-
-
-
-
r
acetonitrile + H2O
acetamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
best substrate
-
-
?
acetonitrile + H2O
acetamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
best substrate
-
-
?
acetonitrile + H2O
acetamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
79% of the activity with acrylonitrile
-
-
?
acetonitrile + H2O
acetamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acetonitrile + H2O
acetamide
-
79% of the activity with acrylonitrile
-
-
?
acetonitrile + H2O
acetamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acetonitrile + H2O
acetamide
hydration at 29.02% compared to the activity with thiacloprid
-
-
?
acetonitrile + H2O
acetamide
hydration at 29.02% compared to the activity with thiacloprid
-
-
?
acrylamide + H2O
acrylonitrile
-
-
-
-
?
acrylamide + H2O
acrylonitrile
-
-
-
-
?
acrylamide + H2O
acrylonitrile
-
-
-
-
?
acrylamide + H2O
acrylonitrile
-
-
-
?
acrylamide + H2O
acrylonitrile
-
-
-
?
acrylamide + H2O
acrylonitrile
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
r
acrylonitrile + H2O
2-propenoic acid amide
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
78% of the activity with propionitrile
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylamide
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylamide
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
?
-
-
-
?
acrylonitrile + H2O
?
-
-
-
?
acrylonitrile + H2O
?
-
-
-
?
acrylonitrile + H2O
?
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
yield 100%
-
?
acrylonitrile + H2O
acrylamide
-
yield 100%
-
?
acrylonitrile + H2O
acrylamide
79% of the activity compared to 3-cyanopyridine
-
-
?
acrylonitrile + H2O
acrylamide
79% of the activity compared to 3-cyanopyridine
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
best substrate
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
best substrate
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
stereoselective reaction
-
-
?
acrylonitrile + H2O
acrylamide
analysis of the structure model of the enzyme-substrate complex and catalytic mechanism, overview
-
-
?
acrylonitrile + H2O
acrylamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
stereoselective reaction
-
-
?
acrylonitrile + H2O
acrylamide
analysis of the structure model of the enzyme-substrate complex and catalytic mechanism, overview
-
-
?
acrylonitrile + H2O
acrylamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
highest activity
-
-
?
acrylonitrile + H2O
acrylamide
-
highest activity
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
r
acrylonitrile + H2O
acrylamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acrylonitrile + H2O
acrylamide
-
-
-
-
r
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acrylonitrile + H2O
acrylamide
-
-
-
-
?
adiponitrile + 2 H2O
adipamide
-
yield 100%
-
?
adiponitrile + 2 H2O
adipamide
-
yield 100%
-
?
adiponitrile + 2 H2O
adipic acid amide
-
-
-
-
?
adiponitrile + 2 H2O
adipic acid amide
-
108% of the activity with propionitrile
-
-
?
adiponitrile + 2 H2O
adipic acid amide
-
-
-
-
?
adiponitrile + 2 H2O
adipic acid amide
wild-type enzyme forms only adipamide after a 4 h reaction. Y68T and W72Y mutations cause a significant shift in product formation and form primarily 5-cyanovaleramide. Mutant enzyme Y68T/W72Y produces 100% 5-cyanovaleramide
-
-
?
adiponitrile + 2 H2O
adipic acid amide
wild-type enzyme forms only adipamide after a 4 h reaction. Y68T and W72Y mutations cause a significant shift in product formation and form primarily 5-cyanovaleramide. Mutant enzyme Y68T/W72Y produces 100% 5-cyanovaleramide
-
-
?
adiponitrile + 2 H2O
adipic acid amide
-
-
-
-
?
adiponitrile + 2 H2O
adipic acid amide
-
-
-
-
?
adiponitrile + H2O
5-cyanovaleramide
-
-
-
-
?
adiponitrile + H2O
5-cyanovaleramide
-
-
-
-
?
adiponitrile + H2O
5-cyanovaleramide
wild-type enzyme forms only adipamide after a 4 h reaction. Y68T and W72Y mutations cause a significant shift in product formation and form primarily 5-cyanovaleramide. Mutant enzyme Y68T/W72Y produces 100% 5-cyanovaleramide
-
-
r
adiponitrile + H2O
5-cyanovaleramide
wild-type enzyme forms only adipamide after a 4 h reaction. Y68T and W72Y mutations cause a significant shift in product formation and form primarily 5-cyanovaleramide. Mutant enzyme Y68T/W72Y produces 100% 5-cyanovaleramide
-
-
r
alpha-methylbenzyl cyanide + H2O
2-phenylpropanamide
65% of the activity compared to 3-cyanopyridine
-
-
?
alpha-methylbenzyl cyanide + H2O
2-phenylpropanamide
-
-
-
-
r
an aliphatic amide
a nitrile + H2O
-
-
-
-
?
an aliphatic amide
a nitrile + H2O
-
ligand exchange reactions, overview
-
-
?
an aliphatic amide
a nitrile + H2O
-
-
-
-
?
an aliphatic amide
a nitrile + H2O
-
ligand exchange reactions, overview
-
-
?
an aliphatic amide
a nitrile + H2O
-
-
-
-
?
an aliphatic amide
a nitrile + H2O
-
ligand exchange reactions, overview
-
-
?
an aliphatic amide
a nitrile + H2O
-
-
-
-
?
an aliphatic amide
a nitrile + H2O
-
ligand exchange reactions, overview
-
-
?
benzonitrile + H2O
?
-
-
-
?
benzonitrile + H2O
?
-
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
82% of the activity compared to 3-cyanopyridine
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
-
-
-
?
benzonitrile + H2O
benzamide
lower activity
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
-
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
-
-
-
-
?
benzonitrile + H2O
benzamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
benzonitrile + H2O
benzamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
ir
benzonitrile + H2O
benzamide
hydration at 2532% compared to the activity with thiacloprid
-
-
?
benzonitrile + H2O
benzamide
hydration at 2532% compared to the activity with thiacloprid
-
-
?
benzonitrile + H2O
benzoic acid amide
-
1.3% of the activity with propionitrile
-
-
?
benzonitrile + H2O
benzoic acid amide
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
-
15% of the activity with acrylonitrile
-
-
?
benzonitrile + H2O
benzoic acid amide
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
-
low activity
-
-
?
benzonitrile + H2O
benzoic acid amide
-
low activity
-
-
?
benzonitrile + H2O
benzoic acid amide
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
-
19.4% of the activity with acrylonitrile
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
-
-
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
-
-
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
bromoxynil + H2O
?
-
-
-
-
?
bromoxynil + H2O
?
-
-
-
-
?
bromoxynil + H2O
?
-
-
-
-
?
bromoxynil + H2O
?
-
-
-
-
?
butyronitrile + H2O
butyramide
-
yield 100%
-
?
butyronitrile + H2O
butyramide
-
-
-
-
?
butyronitrile + H2O
butyramide
248% of the activity compared to 3-cyanopyridine
-
-
?
butyronitrile + H2O
butyramide
-
-
-
-
?
butyronitrile + H2O
butyramide
-
-
-
-
?
butyronitrile + H2O
butyramide
-
-
-
-
?
butyronitrile + H2O
butyramide
-
-
-
-
?
butyronitrile + H2O
butyramide
-
-
-
-
?
butyronitrile + H2O
butyramide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
butyronitrile + H2O
butyramide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
chloroacetonitrile + H2O
chloroacetamide
-
-
-
ir
chloroacetonitrile + H2O
chloroacetamide
-
-
-
ir
chloroacetonitrile + H2O
chloroacetamide
-
42% of the activity with propionitrile
-
-
?
chloroacetonitrile + H2O
chloroacetamide
-
42% of the activity with propionitrile
-
-
?
chloroacetonitrile + H2O
chloroacetamide
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
-
-
-
-
?
chloroxynil acid + H2O
?
-
-
-
-
?
chloroxynil acid + H2O
?
-
-
-
-
?
chloroxynil acid + H2O
?
-
-
-
-
?
chloroxynil acid + H2O
?
-
-
-
-
?
chloroxynil amide + H2O
?
-
-
-
-
?
chloroxynil amide + H2O
?
-
-
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
-
19% of the activity with propionitrile
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
-
19% of the activity with propionitrile
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
-
-
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
-
19% of the activity with propionitrile
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
-
-
-
-
?
cyanide + H2O
formamide
-
2% of the activity with propionitrile
-
-
?
cyanide + H2O
formamide
-
-
-
-
?
cyanovaleramide
valerodinitrile + H2O
-
-
-
-
?
cyanovaleramide
valerodinitrile + H2O
-
-
-
-
?
cyanovaleric acid + H2O
?
-
-
-
-
?
cyanovaleric acid + H2O
?
-
-
-
-
?
cyanovaleric acid + H2O
?
-
-
-
-
?
dichlobenil amide + H2O
?
-
-
-
-
?
dichlobenil amide + H2O
?
-
-
-
-
?
ethylene cyanhydrine + H2O
?
-
-
-
-
?
ethylene cyanhydrine + H2O
?
-
-
-
-
?
hydroxyacetonitrile + H2O
hydroxyacetamide
-
-
-
?
hydroxyacetonitrile + H2O
hydroxyacetamide
-
-
-
r
hydroxyacetonitrile + H2O
hydroxyacetamide
-
50% of the activity with propionitrile
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
-
-
-
?
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
hydration at 479.79% compared to the activity with thiacloprid
-
-
?
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
hydration at 479.79% compared to the activity with thiacloprid
-
-
?
indole-3-acetonitrile + H2O
indole-3-acetamide
-
conversion rate: 34.44%
-
-
?
indole-3-acetonitrile + H2O
indole-3-acetamide
-
conversion rate: 34.44%
-
-
?
indole-3-nitrile + H2O
indole-3-acetamide
-
-
-
?
indole-3-nitrile + H2O
indole-3-acetamide
-
the nitrile hydratase produces only indole-3-acetamide, no indole-3-acetic acid
-
?
ioxynil acid + H2O
?
-
-
-
-
?
ioxynil acid + H2O
?
-
-
-
-
?
isobutyronitrile + H2O
isobutyramide
215% of the activity compared to 3-cyanopyridine
-
-
?
isobutyronitrile + H2O
isobutyramide
-
-
-
?
isobutyronitrile + H2O
isobutyramide
-
-
-
-
?
isobutyronitrile + H2O
isobutyramide
-
-
-
-
?
isobutyronitrile + H2O
isobutyramide
hydration at 3.78% compared to the activity with thiacloprid
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
113% of the activity with propionitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
113% of the activity with propionitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
71% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
71% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
62.5% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
62.5% of the activity with acrylonitrile
-
-
?
isovaleronitrile + H2O
isovaleric acid amide
-
more active than trans-4-cyanocyclohexane-1-carboxylic acid as substrate
-
-
?
isovaleronitrile + H2O
isovaleric acid amide
-
-
product identification by liquid chromatography tandem mass spectrometry
-
?
isovaleronitrile + H2O
isovaleric acid amide
-
-
product identification by liquid chromatography tandem mass spectrometry
-
?
mandelonitrile + H2O
?
31% of the activity compared to 3-cyanopyridine
-
-
?
mandelonitrile + H2O
?
-
used as well as phenylacetonitrile
-
-
?
mandelonitrile + H2O
?
-
-
-
-
?
methacrylamide + H2O
?
-
causes the greatest induction of activity
-
-
?
methacrylamide + H2O
?
-
causes the greatest induction of activity
-
-
?
methacrylonitrile + H2O
methacrylamide
-
yield 100%
-
?
methacrylonitrile + H2O
methacrylamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
methacrylonitrile + H2O
methacrylamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
methacrylonitrile + H2O
methacrylamide
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
-
-
-
?
methacrylonitrile + H2O
methacrylamide
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
-
low activity
-
-
?
methacrylonitrile + H2O
methacrylamide
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
-
low activity
-
-
?
methacrylonitrile + H2O
methylacrylamide
96% of the activity compared to 3-cyanopyridine
-
-
?
methacrylonitrile + H2O
methylacrylamide
-
-
-
-
?
methacrylonitrile + H2O
methylacrylamide
-
-
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
-
-
-
r
methacrylonitrile + H2O
methylacrylic acid amide
-
53% of the activity with propionitrile
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
-
more active than trans-4-cyanocyclohexane-1-carboxylic acid as substrate
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
-
-
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
-
-
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
-
-
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
r
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
r
n-butyronitrile + H2O
n-butyric acid amide
-
33% of the activity with propionitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
140% of the activity with propionitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
33% of the activity with propionitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
140% of the activity with propionitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
-
-
-
-
?
n-capronitrile + H2O
n-hexanoic acid amide
-
46% of the activity with propionitrile
-
-
?
n-capronitrile + H2O
n-hexanoic acid amide
-
46% of the activity with propionitrile
-
-
?
n-capronitrile + H2O
n-hexanoic acid amide
-
-
-
-
?
n-capronitrile + H2O
n-hexanoic acid amide
-
-
-
-
?
n-valeronitrile + H2O
n-valeramide
-
-
-
-
?
n-valeronitrile + H2O
n-valeramide
-
-
-
-
?
naproxennitrile + H2O
?
-
the enzyme is enantioselective with the compound
-
-
?
naproxennitrile + H2O
?
-
the enzyme is enantioselective with the compound
-
-
?
naproxennitrile + H2O
?
-
the enzyme is enantioselective with the compound
-
-
?
nicotinonitrile + H2O
nicotinamide
-
-
-
-
?
nicotinonitrile + H2O
nicotinamide
-
-
-
-
?
o-chlorobenzonitrile + H2O
o-chlorobenzamide
-
-
-
-
?
o-chlorobenzonitrile + H2O
o-chlorobenzamide
-
-
-
-
?
phenylacetonitrile + H2O
phenylacetamide
-
337% activity compared to indole-3-acetonitrile
-
-
?
phenylacetonitrile + H2O
phenylacetamide
-
337% activity compared to indole-3-acetonitrile
-
-
?
phenylacetonitrile + H2O
phenylacetamide
-
-
-
-
?
phenylacetonitrile + H2O
phenylacetamide
-
-
-
-
?
phenylacetonitrile + H2O
phenylacetamide
-
337% activity compared to indole-3-acetonitrile
-
-
?
phenylacetonitrile + H2O
phenylacetamide
-
337% activity compared to indole-3-acetonitrile
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
-
5.3% of the activity with propionitrile
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
-
5% of the activity with propionitrile
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
-
-
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
-
62% of the activity with acrylonitrile
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
-
62% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
113% of the activity compared to 3-cyanopyridine
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
?
propionitrile + H2O
propionamide
-
-
-
-
r
propionitrile + H2O
propionamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
propionitrile + H2O
propionamide
-
-
-
-
r
propionitrile + H2O
propionamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
i.e. propionamide
r
propionitrile + H2O
propionic acid amide
-
-
i.e. propionamide
r
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
i.e. propionamide
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
i.e. propionamide
?
propionitrile + H2O
propionic acid amide
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
17% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
17% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
10% of conversion in 24 h
i.e. propionamide
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
10% of conversion in 24 h
i.e. propionamide
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
propionitrile + H2O
propionic acid amide
-
64% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionic acid amide
-
64% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionic acid amide
-
-
-
-
?
succinonitrile + H2O
?
-
135% of the activity with propionitrile
-
-
?
succinonitrile + H2O
?
hydration at 13.17% compared to the activity with thiacloprid
-
-
?
succinonitrile + H2O
?
hydration at 13.17% compared to the activity with thiacloprid
-
-
?
tert-butylisonitrile + H2O
tert-butyl amide
-
-
-
-
?
tert-butylisonitrile + H2O
tert-butyl amide
-
-
-
-
?
tert-butylisonitrile + H2O
tert-butyl amide
-
-
-
-
?
tert-butylisonitrile + H2O
tert-butyl amide
-
-
-
-
?
trans-4-cyanocyclohexane-1-carboxylic acid + H2O
4-(aminocarbonyl)cyclohexanecarboxylic acid
-
-
-
?
trans-4-cyanocyclohexane-1-carboxylic acid + H2O
4-(aminocarbonyl)cyclohexanecarboxylic acid
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
2.7% of the activity with propionitrile
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
2.7% of the activity with propionitrile
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
more than 3 times more active than trans-4-cyanocyclohexane-1-carboxylic acid as substrate
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
almost 9000fold higher activity towards valeronitrile compared to (R,S)-2-phenylpropionitrile
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
almost 9000fold higher activity towards valeronitrile compared to (R,S)-2-phenylpropionitrile
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
-
-
-
-
?
valeronitrile + H2O
valeramide
-
-
-
-
r
valeronitrile + H2O
valeramide
-
-
-
-
?
valeronitrile + H2O
valeramide
-
-
-
-
?
additional information
?
-
-
(indol-3-yl)acetamide is no substrate, no formation of iodoacetic acid
-
-
?
additional information
?
-
-
(indol-3-yl)acetamide is no substrate, no formation of iodoacetic acid
-
-
?
additional information
?
-
-
no activity with aeroplysinin-1 derivatives (1S,2R)-3,5-dibromo-1-(cyanomethyl)-4-methoxycyclohexa-3,5-diene-1,2-diyl diacetate, (2-hydroxy-4-methoxyphenyl)acetonitrile, and (3,5-dibromo-2-hydroxy-4-methoxyphenyl)acetonitrile
-
-
?
additional information
?
-
-
the enzyme acts on low-molecular aliphatic nitriles with 2-5 carbons but not on aliphatic nitriles with more than 6 carbons
-
-
?
additional information
?
-
-
aliphatic nitriles with more than 5 carbons and aromatic nitriles cannot act as substrate
-
-
?
additional information
?
-
-
aliphatic nitriles with more than 5 carbons and aromatic nitriles cannot act as substrate
-
-
?
additional information
?
-
-
an unusual preference for branched and cyclic aliphatic nitriles is noted
-
-
?
additional information
?
-
-
wide substrate spectrum
-
-
?
additional information
?
-
-
wide substrate spectrum
-
-
?
additional information
?
-
Corynebacterium nitrilophilus
-
highest rate of reaction with short chain aliphatic nitriles
-
-
?
additional information
?
-
-
substrate binding preferences and pK(a) determinations of a nitrile hydratase model complex, catalytic mechanism, overview
-
-
?
additional information
?
-
-
substrate specificity of strain 38.1.2, no activity with 4-tolunitrile, overview
-
-
?
additional information
?
-
recombinant NHaseK can hydrolyze a wide range of aliphatic, aromatic, and heterocyclic nitriles, and converts racemic nitriles to the corresponding S-amides, with E values ranging from 9 to 17
-
-
?
additional information
?
-
-
substrate specificity of strain 38.1.2, no activity with 4-tolunitrile, overview
-
-
?
additional information
?
-
recombinant NHaseK can hydrolyze a wide range of aliphatic, aromatic, and heterocyclic nitriles, and converts racemic nitriles to the corresponding S-amides, with E values ranging from 9 to 17
-
-
?
additional information
?
-
-
the NHase active site of the strain F28 might consist of cysteine and serine
-
-
?
additional information
?
-
-
the NHase active site of the strain F28 might consist of cysteine and serine
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
aromatic nitriles are barely hydrated by the enzyme
-
-
?
additional information
?
-
-
formamide, acetamide, acrylamide, propionamide, n-butyramide, isobutyramide, n-valeramide, succinamide, benzamide, phenylacetamide and lactamide are no substrates
-
-
?
additional information
?
-
-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide, no or reduced activity in NhpR transcriptional regulator defective mutants
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
aromatic nitriles are barely hydrated by the enzyme
-
-
?
additional information
?
-
-
formamide, acetamide, acrylamide, propionamide, n-butyramide, isobutyramide, n-valeramide, succinamide, benzamide, phenylacetamide and lactamide are no substrates
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide, no or reduced activity in NhpR transcriptional regulator defective mutants
-
-
?
additional information
?
-
-
S enantiomer conversion is 14 times greater than the rate of R enantiomer conversion
-
-
?
additional information
?
-
-
roles of second- and third-shell residues of the active site structure in catalysis, overview. Three of the predicted second-shell residues, alpha-Asp164, beta-Glu56, and beta-His147, and one predicted third-shell residue, beta-His71, have significant effects on the catalytic efficiency of the enzyme, while one of the predicted residues, alpha-Glu168, and the three residues not predicted, alpha-Arg170, alpha-Tyr171, and beta-Tyr215, do not have any significant effects on the catalytic efficiency of the enzyme
-
-
?
additional information
?
-
the Fe-type NHase exhibits broad substrate specificity
-
-
?
additional information
?
-
-
S enantiomer conversion is 14 times greater than the rate of R enantiomer conversion
-
-
?
additional information
?
-
-
roles of second- and third-shell residues of the active site structure in catalysis, overview. Three of the predicted second-shell residues, alpha-Asp164, beta-Glu56, and beta-His147, and one predicted third-shell residue, beta-His71, have significant effects on the catalytic efficiency of the enzyme, while one of the predicted residues, alpha-Glu168, and the three residues not predicted, alpha-Arg170, alpha-Tyr171, and beta-Tyr215, do not have any significant effects on the catalytic efficiency of the enzyme
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
computational molecular dynamics modelling of ligand docking and substrate transport and binding, overview
-
-
?
additional information
?
-
-
NHase hydrates a nitrile to provide the corresponding amide product via an addition reaction of one water molecule, active site structure involving amidate nitrogen donors from the peptide backbone, overview
-
-
?
additional information
?
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine
-
-
?
additional information
?
-
the enzyme shows a preference for aromatic nitriles as substrates rather than aliphatic ones. Tryptophan residue betaTrp72 may be involved in substrate binding
-
-
?
additional information
?
-
the enzyme shows a preference for aromatic nitriles as substrates rather than aliphatic ones. Tryptophan residue betaTrp72 may be involved in substrate binding
-
-
?
additional information
?
-
-
NHase hydrates a nitrile to provide the corresponding amide product via an addition reaction of one water molecule, active site structure involving amidate nitrogen donors from the peptide backbone, overview
-
-
?
additional information
?
-
-
computational molecular dynamics modelling of ligand docking and substrate transport and binding, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine
-
-
?
additional information
?
-
the enzyme shows a preference for aromatic nitriles as substrates rather than aliphatic ones. Tryptophan residue betaTrp72 may be involved in substrate binding
-
-
?
additional information
?
-
the enzyme shows a preference for aromatic nitriles as substrates rather than aliphatic ones. Tryptophan residue betaTrp72 may be involved in substrate binding
-
-
?
additional information
?
-
-
the thermoactive nitrilase from Pyrococcus abyssi hydrolyses small aliphatic nitriles like fumaro- and malononitril, docking calculations for fumaro- and malononitriles, modelling, overview
-
-
?
additional information
?
-
-
substrate specificity of strain 77.1, no activity with 4-tolunitrile and 3-chlorobenzonitrile, overview
-
-
?
additional information
?
-
-
substrate specificity of strain 77.1, no activity with 4-tolunitrile and 3-chlorobenzonitrile, overview
-
-
?
additional information
?
-
-
besides aromatic and heterocyclic nitriles, aliphatic ones are hydrated preferentially
-
-
?
additional information
?
-
-
no activity with (R,S)-2-(4-isobutylphenyl)propionitrile and (R,S)-3-(1-cyanoethyl)benzoic acid
-
-
?
additional information
?
-
-
structural and mechanistic insights from electron paramagnetic resonance and density functional theory studies
-
-
?
additional information
?
-
-
structural and mechanistic insights from electron paramagnetic resonance and density functional theory studies
-
-
?
additional information
?
-
-
besides aromatic and heterocyclic nitriles, aliphatic ones are hydrated preferentially
-
-
?
additional information
?
-
-
no activity with (R,S)-2-(4-isobutylphenyl)propionitrile and (R,S)-3-(1-cyanoethyl)benzoic acid
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
?
additional information
?
-
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. The enzyme is aselective with a range of different 2-phenylacetonitriles. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
?
additional information
?
-
-
no activity with chloroxynil amide
-
-
?
additional information
?
-
-
no activity with chloroxynil amide
-
-
?
additional information
?
-
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. The enzyme is aselective with a range of different 2-phenylacetonitriles. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
?
additional information
?
-
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
H-NHase acts preferentially on aliphatic nitriles, while L-NHase has a higher affinity for aromatic nitriles
-
-
?
additional information
?
-
-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE
-
-
?
additional information
?
-
-
no activity with 2,6-dichlorobenzamide and dichlobenil acid
-
-
?
additional information
?
-
-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE
-
-
?
additional information
?
-
-
H-NHase acts preferentially on aliphatic nitriles, while L-NHase has a higher affinity for aromatic nitriles
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
no activity with 2,6-dichlorobenzamide and dichlobenil acid
-
-
?
additional information
?
-
-
no detectably transformation with 2-methyl-2-butenenitrile, benzonitrile and phenylacetonitrile
-
-
?
additional information
?
-
-
NHase is a non-heme iron enzyme catalyzing the hydration of various nitriles to the corresponding amides
-
-
?
additional information
?
-
-
hydrogen bonds between betaArg56 and alphaCys114 sulfenic acid are important to maintain the enzymatic activity, molecular dynamics simulations determining the differences in the dynamics of lightactive and dark-inactive forms of NHase, overview
-
-
?
additional information
?
-
-
NHase is a non-heme iron enzyme catalyzing the hydration of various nitriles to the corresponding amides
-
-
?
additional information
?
-
-
no detectably transformation with 2-methyl-2-butenenitrile, benzonitrile and phenylacetonitrile
-
-
?
additional information
?
-
-
the nitrile hydratase can hydrate aliphatic, aromatic and heterocyclic nitriles under very mild conditions, in mixtures of pH 7 buffer and a range of organic solvents, often with excellent chemoselectivity. Major determinant of hydration occurring is the degree of steric hindrance around the nitrile moiety and/or size of the substrates
-
-
?
additional information
?
-
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
?
additional information
?
-
-
the nitrile hydratase can hydrate aliphatic, aromatic and heterocyclic nitriles under very mild conditions, in mixtures of pH 7 buffer and a range of organic solvents, often with excellent chemoselectivity. Major determinant of hydration occurring is the degree of steric hindrance around the nitrile moiety and/or size of the substrates
-
-
?
additional information
?
-
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
?
additional information
?
-
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
?
additional information
?
-
substrate specificity of trimeric enzyme compared to the isolated alpha-subunit, overview. Activity of the alpha-subunit of a nitrile hydratase distinguishes among possible mechanisms of nitrile hydration by adding significant weight to those that rely solely on residues derived from the alpha-subunit. No activity with thiocyanate
-
-
?
additional information
?
-
substrate specificity of trimeric enzyme compared to the isolated alpha-subunit, overview. Activity of the alpha-subunit of a nitrile hydratase distinguishes among possible mechanisms of nitrile hydration by adding significant weight to those that rely solely on residues derived from the alpha-subunit. No activity with thiocyanate
-
-
?
additional information
?
-
substrate specificity of trimeric enzyme compared to the isolated alpha-subunit, overview. Activity of the alpha-subunit of a nitrile hydratase distinguishes among possible mechanisms of nitrile hydration by adding significant weight to those that rely solely on residues derived from the alpha-subunit. No activity with thiocyanate
-
-
?
additional information
?
-
-
substrate specificity of trimeric enzyme compared to the isolated alpha-subunit, overview. Activity of the alpha-subunit of a nitrile hydratase distinguishes among possible mechanisms of nitrile hydration by adding significant weight to those that rely solely on residues derived from the alpha-subunit. No activity with thiocyanate
-
-
?
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H80A
mutant of alpha-subunit, activity (kcat = 220/s) accounts for about 20% of the wild-type activity (kcat = 1100/s) while the Km value is slightly reduced (187 mM)
H80A/H81A
mutant of alpha-subunit, activity (kcat = 132/s) accounts for 12% of the wild-type activity (kcat = 1100/s) while the Km value is nearly unchanged at 205 mM. Hydrogen-bonding interactions crucial for the catalytic function of the alphaCys104-SOH ligand are disrupted. Disruption of these hydrogen bonding interactions likely alters the nucleophilicity of the sulfenic acid oxygen and the Lewis acidity of the active site Fe(III) ion
H80W/H81W
mutant of alpha-subunit, disruption of these hydrogen bonding interactions likely alters the nucleophilicity of the sulfenic acid oxygen and the Lewis acidity of the active site Fe(III) ion
H81A
mutant of alpha-subunit, activity (kcat = 77/s) accounts for 4% of the wild-type activity (kcat = 1100/s) while the Km value is slightly reduced (179 mM)
H80A
-
mutant of alpha-subunit, activity (kcat = 220/s) accounts for about 20% of the wild-type activity (kcat = 1100/s) while the Km value is slightly reduced (187 mM)
-
H80A/H81A
-
mutant of alpha-subunit, activity (kcat = 132/s) accounts for 12% of the wild-type activity (kcat = 1100/s) while the Km value is nearly unchanged at 205 mM. Hydrogen-bonding interactions crucial for the catalytic function of the alphaCys104-SOH ligand are disrupted. Disruption of these hydrogen bonding interactions likely alters the nucleophilicity of the sulfenic acid oxygen and the Lewis acidity of the active site Fe(III) ion
-
H81A
-
mutant of alpha-subunit, activity (kcat = 77/s) accounts for 4% of the wild-type activity (kcat = 1100/s) while the Km value is slightly reduced (179 mM)
-
S122A
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
S122C
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
S122D
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
W47E
beta subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
S122A
-
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
-
S122C
-
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
-
S122D
-
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
-
W47E
-
beta subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
-
alphaD164N
-
site-directed mutagenesis
alphaE168Q
-
site-directed mutagenesis
alphaR170Q
-
site-directed mutagenesis
betaE56Q
-
site-directed mutagenesis
betaH71F
-
site-directed mutagenesis
betaH71L
-
site-directed mutagenesis
betaH71N
-
site-directed mutagenesis
betaY215F
-
site-directed mutagenesis
M150C
beta-subunit mutant enzyme, 32% increase in half-life at 50°C, the kcat/Km value is 1.1fold higher than the kcat/Km value of the wild-type enzyme
S189E
beta-subunit mutant enzyme, 107% increase in half-life at 50°C, the kcat/Km value is 2.2fold higher than the kcat/Km value of the wild-type enzyme
T173Y
beta-subunit mutant enzyme, 7% increase in half-life at 50°C, the kcat/Km value is 1.5fold higher than the kcat/Km value of the wild-type enzyme
alphaD164N
-
site-directed mutagenesis
-
alphaE168Q
-
site-directed mutagenesis
-
alphaR170Q
-
site-directed mutagenesis
-
betaE56Q
-
site-directed mutagenesis
-
betaH71L
-
site-directed mutagenesis
-
M150C
-
beta-subunit mutant enzyme, 32% increase in half-life at 50°C, the kcat/Km value is 1.1fold higher than the kcat/Km value of the wild-type enzyme
-
S189E
-
beta-subunit mutant enzyme, 107% increase in half-life at 50°C, the kcat/Km value is 2.2fold higher than the kcat/Km value of the wild-type enzyme
-
T173Y
-
beta-subunit mutant enzyme, 7% increase in half-life at 50°C, the kcat/Km value is 1.5fold higher than the kcat/Km value of the wild-type enzyme
-
alphaT109S
site-directed mutagenesis, the mutant shows similar characteristics compared to the wild-type enzyme
alphaY114T
site-directed mutagenesis, the mutant shows a very low cobalt content and catalytic activity compared to the wild-type enzyme, and oxidative modifications of aCys111 and aCys113 residues are not observed
betaY68F
site-directed mutagenesis, the mutant shows an elevated Km value and a significantly decreased kcat value compared to the wild-type enzyme
T109S
similar characteristics to the wild-type enzyme
Y114T
very low cobalt content and catalytic activity compared to the wild-type enzyme
alphaT109S
-
site-directed mutagenesis, the mutant shows similar characteristics compared to the wild-type enzyme
-
alphaY114T
-
site-directed mutagenesis, the mutant shows a very low cobalt content and catalytic activity compared to the wild-type enzyme, and oxidative modifications of aCys111 and aCys113 residues are not observed
-
betaY68F
-
site-directed mutagenesis, the mutant shows an elevated Km value and a significantly decreased kcat value compared to the wild-type enzyme
-
T109S
-
similar characteristics to the wild-type enzyme
-
Y114T
-
very low cobalt content and catalytic activity compared to the wild-type enzyme
-
S113A
-
the mutation partially affects catalytic activity and does not change the pH profiles of the kinetic parameters, the electronic state of the Fe center is altered
Y72F
-
the mutant exhibits no activity
S113A
-
the mutation partially affects catalytic activity and does not change the pH profiles of the kinetic parameters, the electronic state of the Fe center is altered
-
Y72F
-
the mutant exhibits no activity
-
A51L
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 74.3%
alphaV5L
-
site-directed mutagenesis, exchange in the H-NHase does not influence the catalytic activity or the Co2+ content
F37H
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 96.8%
F37H/F51L
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 94.6%
F37H/L48A
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 95.1%
F37Y
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 88.7%
F51Q
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 60.2%
L48Q
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 59.7%
W72Y
with adiponitrile as substrate the wild-type enzyme forms only adipamide after a 4 h reaction. Y68T and W72Y mutations cause a significant shift in product formation and form primarily 5-cyanovaleramide. The use of the wild-type enzyme leads to malonamide formation with 97.3% malononitrile conversion. Variants Y68T and W72Y show a drastic change in regiospecificity by producing mainly the omega-cyanocarboxamide, cyanoacetamide, at a relatively low malononitrile conversion. The wild-type enzyme prefers terephthalonitrile to catalyze mainly into terephthalamide (84.3%) with a conversion up to 99.2 %. Variants Y68T and W72Y show a change in regiospecificity by producing mainly the 4-cyanobenzamide. The wild-type enzyme forms 100% phthalamide from phthalodinitrile. The mutant enzymes Y68T and W72Y result in a higher 2-cyanobenzamide formation than their parent enzyme
Y68T
with adiponitrile as substrate the wild-type enzyme forms only adipamide after a 4 h reaction. Y68T and W72Y mutations cause a significant shift in product formation and form primarily 5-cyanovaleramide. The use of the wild-type enzyme leads to malonamide formation with 97.3% malononitrile conversion. Variants Y68T and W72Y show a drastic change in regiospecificity by producing mainly the omega-cyanocarboxamide, cyanoacetamide, at a relatively low malononitrile conversion. The wild-type enzyme prefers terephthalonitrile to catalyze mainly into terephthalamide (84.3%) with a conversion up to 99.2%. Variants Y68T and W72Y show a change in regiospecificity by producing mainly the 4-cyanobenzamide. The wild-type enzyme forms 100% phthalamide from phthalodinitrile. The mutant enzymes Y68T and W72Y result in a higher 2-cyanobenzamide formation than their parent enzyme
Y68T/W72Y
the mutant enzyme displays a totally different regioselectivity towards dinitriles than its parent enzyme. The use of the wild-type enzyme leads to malonamide formation with 97.3% malononitrile conversion. Mutant enzyme Y68T/W72Y produces 97.1% omega-cyanocarboxamide. The wild-type enzyme forms only adipamide after a 4 h reaction. Mutant enzyme Y68T/W72Y produces 100% 5-cyanovaleramide. The wild-type enzyme prefers terephthalonitrile to catalyze mainly into terephthalamide (84.3%) with a conversion up to 99.2 %. Mutant enzyme Y68T/W72Y produces 98.2% 4-cyanobenzamide from terephthalonitrile. The wild-type enzyme forms 100% phthalamide from phthalodinitrile. Mutant enzyme Y68T/W72Y produces 100% 2-cyanobenzamide from phthalodinitrile
A51L
-
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 74.3%
-
alphaV5L
-
site-directed mutagenesis, exchange in the H-NHase does not influence the catalytic activity or the Co2+ content
-
F37H
-
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 96.8%
-
F37Y
-
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 88.7%
-
F51Q
-
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 60.2%
-
L48Q
-
wild-type enzyme catalyzes the conversion of (S)-mandelamide with an enantiomeric excess of 52.6%, the beta-subunit mutant enzyme catalyzes the reaction with an enantiomeric excess of 59.7%
-
W72Y
-
with adiponitrile as substrate the wild-type enzyme forms only adipamide after a 4 h reaction. Y68T and W72Y mutations cause a significant shift in product formation and form primarily 5-cyanovaleramide. The use of the wild-type enzyme leads to malonamide formation with 97.3% malononitrile conversion. Variants Y68T and W72Y show a drastic change in regiospecificity by producing mainly the omega-cyanocarboxamide, cyanoacetamide, at a relatively low malononitrile conversion. The wild-type enzyme prefers terephthalonitrile to catalyze mainly into terephthalamide (84.3%) with a conversion up to 99.2 %. Variants Y68T and W72Y show a change in regiospecificity by producing mainly the 4-cyanobenzamide. The wild-type enzyme forms 100% phthalamide from phthalodinitrile. The mutant enzymes Y68T and W72Y result in a higher 2-cyanobenzamide formation than their parent enzyme
-
Y68T
-
with adiponitrile as substrate the wild-type enzyme forms only adipamide after a 4 h reaction. Y68T and W72Y mutations cause a significant shift in product formation and form primarily 5-cyanovaleramide. The use of the wild-type enzyme leads to malonamide formation with 97.3% malononitrile conversion. Variants Y68T and W72Y show a drastic change in regiospecificity by producing mainly the omega-cyanocarboxamide, cyanoacetamide, at a relatively low malononitrile conversion. The wild-type enzyme prefers terephthalonitrile to catalyze mainly into terephthalamide (84.3%) with a conversion up to 99.2%. Variants Y68T and W72Y show a change in regiospecificity by producing mainly the 4-cyanobenzamide. The wild-type enzyme forms 100% phthalamide from phthalodinitrile. The mutant enzymes Y68T and W72Y result in a higher 2-cyanobenzamide formation than their parent enzyme
-
Y68T/W72Y
-
the mutant enzyme displays a totally different regioselectivity towards dinitriles than its parent enzyme. The use of the wild-type enzyme leads to malonamide formation with 97.3% malononitrile conversion. Mutant enzyme Y68T/W72Y produces 97.1% omega-cyanocarboxamide. The wild-type enzyme forms only adipamide after a 4 h reaction. Mutant enzyme Y68T/W72Y produces 100% 5-cyanovaleramide. The wild-type enzyme prefers terephthalonitrile to catalyze mainly into terephthalamide (84.3%) with a conversion up to 99.2 %. Mutant enzyme Y68T/W72Y produces 98.2% 4-cyanobenzamide from terephthalonitrile. The wild-type enzyme forms 100% phthalamide from phthalodinitrile. Mutant enzyme Y68T/W72Y produces 100% 2-cyanobenzamide from phthalodinitrile
-
R157A
mutant of alpha-subunit, activity (kcat = 10/s) accounts for less than 1% of the wild-type activity (kcat = 1100/s) while the Km value is nearly unchanged at 205 mM
R157A
mutant of alpha-subunit, disruption of these hydrogen bonding interactions likely alters the nucleophilicity of the sulfenic acid oxygen and the Lewis acidity of the active site Fe(III) ion
R157A
-
mutant of alpha-subunit, activity (kcat = 10/s) accounts for less than 1% of the wild-type activity (kcat = 1100/s) while the Km value is nearly unchanged at 205 mM
-
R157A
-
mutant of alpha-subunit, disruption of these hydrogen bonding interactions likely alters the nucleophilicity of the sulfenic acid oxygen and the Lewis acidity of the active site Fe(III) ion
-
up
the putative activator (17K) gene next to the beta-subunit gene is proven to be important for the functional expression of recombinant NHaseK in Escherichia coli
up
-
the putative activator (17K) gene next to the beta-subunit gene is proven to be important for the functional expression of recombinant NHaseK in Escherichia coli
-
betaW47E
-
site-directed mutagenesis
betaW47E
-
site-directed mutagenesis
-
additional information
-
improvement of thermal stability of the industrialized mesophilic NHase by introducing stable salt-bridge interactions into its thermal sensitive regions
additional information
transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH
additional information
transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH
additional information
-
improvement of thermal stability of the industrialized mesophilic NHase by introducing stable salt-bridge interactions into its thermal sensitive regions
-
additional information
-
transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH
-
additional information
the chimeric NHase (SBpNHase) from the thermal sensitive nitrile hydratasese from Bordetella petrii and the relatively thermal-stable nitrile hydratases from Pseudonocardia thermophila is constructed by swapping the corresponding C-domains
additional information
-
the chimeric NHase (SBpNHase) from the thermal sensitive nitrile hydratasese from Bordetella petrii and the relatively thermal-stable nitrile hydratases from Pseudonocardia thermophila is constructed by swapping the corresponding C-domains
additional information
-
the chimeric NHase (SBpNHase) from the thermal sensitive nitrile hydratasese from Bordetella petrii and the relatively thermal-stable nitrile hydratases from Pseudonocardia thermophila is constructed by swapping the corresponding C-domains
-
additional information
-
Fe of an Fe-dependent recombinant nitrile hydratase (wild-type, NilFe) is replaced by Co generating an Co-substituted enzyme (NilCo)
additional information
homologous protein fragment swapping method is used for the improvement of the stability of NHase from Pseudomonas putida NRRL-18668, site targeted amino recombination software and molecular dynamics are used for determination of the crossover sites for fragment recombination, overview. One thermophilic NHase fragment M1 to G98 from Comamonas testosteroni 5-MGAM-4D and two fragments K165-V196 and K165-D209 from Pseudonocardia thermophila JCM3095 are selected to swap the corresponding fragments of Pseudomonas putida NHase. The chimeric NHases show 1.4 to 3.5fold enhancement in thermostability, some show reduced activity and product inhibition compared to wild-type Pseudomonas putida NHase. But mutants 3AB and 3ABC show increased activity due to altered secondary structure compared to the Pseudomonas putida wild-type
additional information
homologous protein fragment swapping method is used for the improvement of the stability of NHase from Pseudomonas putida NRRL-18668, site targeted amino recombination software and molecular dynamics are used for determination of the crossover sites for fragment recombination, overview. One thermophilic NHase fragment M1 to G98 from Comamonas testosteroni 5-MGAM-4D and two fragments K165-V196 and K165-D209 from Pseudonocardia thermophila JCM3095 are selected to swap the corresponding fragments of Pseudomonas putida NHase. The chimeric NHases show 1.4 to 3.5fold enhancement in thermostability, some show reduced activity and product inhibition compared to wild-type Pseudomonas putida NHase. But mutants 3AB and 3ABC show increased activity due to altered secondary structure compared to the Pseudomonas putida wild-type
additional information
-
homologous protein fragment swapping method is used for the improvement of the stability of NHase from Pseudomonas putida NRRL-18668, site targeted amino recombination software and molecular dynamics are used for determination of the crossover sites for fragment recombination, overview. One thermophilic NHase fragment M1 to G98 from Comamonas testosteroni 5-MGAM-4D and two fragments K165-V196 and K165-D209 from Pseudonocardia thermophila JCM3095 are selected to swap the corresponding fragments of Pseudomonas putida NHase. The chimeric NHases show 1.4 to 3.5fold enhancement in thermostability, some show reduced activity and product inhibition compared to wild-type Pseudomonas putida NHase. But mutants 3AB and 3ABC show increased activity due to altered secondary structure compared to the Pseudomonas putida wild-type
-
additional information
-
homologous protein fragment swapping method is used for the improvement of the stability of NHase from Pseudomonas putida NRRL-18668, site targeted amino recombination software and molecular dynamics are used for determination of the crossover sites for fragment recombination, overview. One thermophilic NHase fragment M1 to G98 from Comamonas testosteroni 5-MGAM-4D and two fragments K165-V196 and K165-D209 from Pseudonocardia thermophila JCM3095 are selected to swap the corresponding fragments of Pseudomonas putida NHase. The chimeric NHases show 1.4 to 3.5fold enhancement in thermostability, some show reduced activity and product inhibition compared to wild-type Pseudomonas putida NHase. But mutants 3AB and 3ABC show increased activity due to altered secondary structure compared to the wild-type
additional information
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the thermostability and product tolerance of nitrile hydratase are enhanced by fusing with two of the self-assembling amphipathic peptides, EAK16 (AEAEAKAKAEAEAKAK) at the N- and C-terminus and ELK16 (LELELKLKLELELKLK) at the N-terminus. When self-assembling amphipathic peptide ELK16 is fused to the N-terminus of the enzymes beta-subunit, the resultant enzyme (SAP-NHase-2) becomes an active inclusion body, while EAK16 does not affect the enzyme solubility when fused to the enzyme's C-terminus (SAP-NHase-10) or N-termninus (AP-NHase-1) of the beta-subunit
additional information
-
homologous protein fragment swapping method is used for the improvement of the stability of NHase from Pseudomonas putida NRRL-18668, site targeted amino recombination software and molecular dynamics are used for determination of the crossover sites for fragment recombination, overview. One thermophilic NHase fragment M1 to G98 from Comamonas testosteroni 5-MGAM-4D and two fragments K165-V196 and K165-D209 from Pseudonocardia thermophila JCM3095 are selected to swap the corresponding fragments of Pseudomonas putida NHase. The chimeric NHases show 1.4 to 3.5fold enhancement in thermostability, some show reduced activity and product inhibition compared to wild-type Pseudomonas putida NHase. But mutants 3AB and 3ABC show increased activity due to altered secondary structure compared to the wild-type
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additional information
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the thermostability and product tolerance of nitrile hydratase are enhanced by fusing with two of the self-assembling amphipathic peptides, EAK16 (AEAEAKAKAEAEAKAK) at the N- and C-terminus and ELK16 (LELELKLKLELELKLK) at the N-terminus. When self-assembling amphipathic peptide ELK16 is fused to the N-terminus of the enzymes beta-subunit, the resultant enzyme (SAP-NHase-2) becomes an active inclusion body, while EAK16 does not affect the enzyme solubility when fused to the enzyme's C-terminus (SAP-NHase-10) or N-termninus (AP-NHase-1) of the beta-subunit
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additional information
improvement of thermal stability of the industrialized mesophilic NHase by introducing stable salt-bridge interactions into its thermal sensitive regions
additional information
homologous protein fragment swapping method is used for the improvement of the stability of NHase from Pseudomonas putida NRRL-18668, site targeted amino recombination software and molecular dynamics are used for determination of the crossover sites for fragment recombination, overview. One thermophilic NHase fragment M1 to G98 from Comamonas testosteroni 5-MGAM-4D and two fragments K165-V196 and K165-D209 from Pseudonocardia thermophila JCM3095 are selected to swap the corresponding fragments of Pseudomonas putida NHase. The chimeric NHases show 1.4 to 3.5fold enhancement in thermostability, some show reduced activity and product inhibition compared to wild-type Pseudomonas putida NHase. But mutants 3AB and 3ABC show increased activity due to altered secondary structure compared to the Pseudomonas putida wild-type
additional information
homologous protein fragment swapping method is used for the improvement of the stability of NHase from Pseudomonas putida NRRL-18668, site targeted amino recombination software and molecular dynamics are used for determination of the crossover sites for fragment recombination, overview. One thermophilic NHase fragment M1 to G98 from Comamonas testosteroni 5-MGAM-4D and two fragments K165-V196 and K165-D209 from Pseudonocardia thermophila JCM3095 are selected to swap the corresponding fragments of Pseudomonas putida NHase. The chimeric NHases show 1.4 to 3.5fold enhancement in thermostability, some show reduced activity and product inhibition compared to wild-type Pseudomonas putida NHase. But mutants 3AB and 3ABC show increased activity due to altered secondary structure compared to the Pseudomonas putida wild-type
additional information
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transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH
additional information
the chimeric NHase (SBpNHase) from the thermal sensitive nitrile hydratasese from Bordetella petrii and the relatively thermal-stable nitrile hydratases from Pseudonocardia thermophila is constructed by swapping the corresponding C-domains
additional information
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transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH
-
additional information
-
homologous protein fragment swapping method is used for the improvement of the stability of NHase from Pseudomonas putida NRRL-18668, site targeted amino recombination software and molecular dynamics are used for determination of the crossover sites for fragment recombination, overview. One thermophilic NHase fragment M1 to G98 from Comamonas testosteroni 5-MGAM-4D and two fragments K165-V196 and K165-D209 from Pseudonocardia thermophila JCM3095 are selected to swap the corresponding fragments of Pseudomonas putida NHase. The chimeric NHases show 1.4 to 3.5fold enhancement in thermostability, some show reduced activity and product inhibition compared to wild-type Pseudomonas putida NHase. But mutants 3AB and 3ABC show increased activity due to altered secondary structure compared to the Pseudomonas putida wild-type
-
additional information
-
improvement of thermal stability of the industrialized mesophilic NHase by introducing stable salt-bridge interactions into its thermal sensitive regions
-
additional information
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construction of an amidase-negative, amiE-, recombinant strain TH3 with 25% increased nitrile hydratase activity and 60% reduced amidase activity compared to the wild-type strain TH. Usage of TH3 free cells as biocatalysts at 18°C for acrylamide production, increased by 23% and 87% reduced acrylic acid by-product formation conmpared to the wild-type
additional information
-
transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH. Three types of salt bridge - active center-adjacent (in A1), internal neighboring-residue-bridged (in A2) and C-terminal-residue-bridged (A3) - are constructed in NHase-TH. A C-terminal salt-bridge strategy is powerful for enzyme stability intensification through triggering global changes of the salt bridge networks, molecular dynamic simulation, overview
additional information
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construction of an amidase-negative, amiE-, recombinant strain TH3 with 25% increased nitrile hydratase activity and 60% reduced amidase activity compared to the wild-type strain TH. Usage of TH3 free cells as biocatalysts at 18°C for acrylamide production, increased by 23% and 87% reduced acrylic acid by-product formation conmpared to the wild-type
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additional information
-
transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH. Three types of salt bridge - active center-adjacent (in A1), internal neighboring-residue-bridged (in A2) and C-terminal-residue-bridged (A3) - are constructed in NHase-TH. A C-terminal salt-bridge strategy is powerful for enzyme stability intensification through triggering global changes of the salt bridge networks, molecular dynamic simulation, overview
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analysis
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the enzyme is used in production of acrylamide from acrylonitrile. For maximum production of Co2+ containing nitrile hydratase, is cultured in the medium containing lactose (18.0 g/l), peptone (1.0 g/l), yeast extract (2.0 g/l), MgSO4 (0.5 g/l), K2HPO4 (0.6 g/l), urea (9.0 g/l), and CoCl2 (0.01 g/l), pH 7.0, and incubated at 35°C for 24 h in an incubator shaker (160 rpm). Nitrile hydratase exhibits relatively high specificity for aliphatic nitriles. Free cells are immobilized using 2% (w/v) agar solution to enhance enzyme stability and reusability in repetitive cycles of acrylamide production. Under optimized conditions, nearly complete bioconversion of acrylonitrile is achieved with a fair recovery of 85% using free and immobilized cells equivalent to 500 mg/dry cell weight/l
degradation
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treatment of acetonitrile-containing wastes on-site, Brevundimonas diminuta containing enzyme degrades acetonitrile at concentrations up to 6 M
degradation
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treatment of acetonitrile-containing wastes on-site, Rhodococcus pyridinivorans S85-2 containing enzyme degrades acetonitrile at concentrations up to 6 M
degradation
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treatment of acetonitrile-containing wastes on-site, Brevundimonas diminuta containing enzyme degrades acetonitrile at concentrations up to 6 M
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degradation
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treatment of acetonitrile-containing wastes on-site, Rhodococcus pyridinivorans S85-2 containing enzyme degrades acetonitrile at concentrations up to 6 M
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environmental protection
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degradation of nitrile waste
environmental protection
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NHase is used in two-step degradation (including amidase, EC 3.5.1.4) of acetonitrile-containing waste
environmental protection
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NHase is used in two-step degradation (including amidase, EC 3.5.1.4) of acetonitrile-containing waste
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environmental protection
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degradation of nitrile waste
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industry
biotransformation of nitrile. Nitrile hydratase from Rhodococcus rhodochrous J1 is used for industrial production of acrylamide and nicotinamide. Production of enzyme by recombinant Escherichia coli is superior to that in R. rhodochrous J1. Genetically engineered Escherichia coli can be used for industrial applications instead of Rhodococcus rhodochrous J1. High-molecular weight nitrile hydratase may be more suitable for industrial application than low-molecular weight nitrile hydratase because of its higher product tolerance, which would lead to a high product concentration
industry
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biotransformation of nitrile. Nitrile hydratase from Rhodococcus rhodochrous J1 is used for industrial production of acrylamide and nicotinamide. Production of enzyme by recombinant Escherichia coli is superior to that in R. rhodochrous J1. Genetically engineered Escherichia coli can be used for industrial applications instead of Rhodococcus rhodochrous J1. High-molecular weight nitrile hydratase may be more suitable for industrial application than low-molecular weight nitrile hydratase because of its higher product tolerance, which would lead to a high product concentration
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pharmacology
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synthesis, biotransformation and biocatalysis of unsaturated/saturated aliphatic, aromatic and heterocyclic nitriles
pharmacology
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synthesis, biotransformation and biocatalysis of unsaturated/saturated aliphatic, aromatic and heterocyclic nitriles
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synthesis
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synthesis
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useful for acrylamide production
synthesis
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useful for acrylamide production
synthesis
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industrial production of nicotinamide
synthesis
-
useful for modification of polyacrylonitrile fibers and granulates
synthesis
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H-NHase is used in the industrial production of acrylamide and nicotinamide
synthesis
-
production of nicotinamide (=vitamin B3) for vitamin supplement for food and animal feed
synthesis
-
production of 2-naphthylacetamide by one-pot chemo-enzymatic conversion
synthesis
-
production of alpha-hydroxy nitriles by use of enzyme
synthesis
-
production of D-tert-leucine-nitrile from racemic tert-leucine-nitrile by use of enzyme plus D-selective amidase from Variovorax paradoxus
synthesis
-
production of propionamide by use of enzyme in ultrafiltration-membrane reactor with maximum volumetric production of 0.5 g propionamide per litre and h
synthesis
-
industrial production of (S)-2,2-dimethylcyclopropanecarboxylic acid
synthesis
-
enzyme can be used in conjunction with a stereoselective amidase to synthesize ethyl (S)-4-chloro-3-hydroxybutyrate, an intermediate for a hypercholesterolemia drug, Atorvastatin
synthesis
-
nitrile hydratase is an enzyme used in the industrial biotechnological production of acrylamide
synthesis
-
nitrile hydratase is used for large scale industrial production of important commodities such as acrylamide and nicotinamide
synthesis
-
the enzyme is useful in synthesis of compounds by hydrating biotransformations, optimization of strain cultivation and enzyme production and activity, overview
synthesis
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bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, carried out in continuously stirred tank UF-membrane bioreactors arranged in series, the reactor configuration enables both enzymes, involved in the cascade reaction, to work with optimized kinetics, without any purification, exploiting their differing temperature dependences, method optimization, overview
synthesis
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bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, operated in either batch or continuous mode, method optimization, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is a cellfree extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
synthesis
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transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
synthesis
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transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
synthesis
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NHases are important for large scale production of acrylamide and nicotinamide
synthesis
industrial production of highly purified acrylamide and nicotinamide. The thermostability and catalytic efficiency of the subunit-fused nitrile hydratase is improved by semi-rational engineering
synthesis
the enzyme from Rhodococcus aetherivorans JB1208 shows high regioselectivity and strong substrate tolerance for alicyclic dinitrile and affords a potentially industrial route to gabapentin (a precursor of gamma-aminobutyric acid, which has been approved for treatment of a variety of central nervous system disorders, partial seizures, and restless legs syndrome)
synthesis
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use of recombinant Corynebacterium cells for the production of acrylamide from acrylonitrile results in a conversion yield of 93% and a final acrylamide concentration of 42.5% within 6 h when the total amount of fed acrylonitrile is 456 g
synthesis
-
transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
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synthesis
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transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is a cellfree extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
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synthesis
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the enzyme is useful in synthesis of compounds by hydrating biotransformations, optimization of strain cultivation and enzyme production and activity, overview
-
synthesis
-
transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
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synthesis
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production of 2-naphthylacetamide by one-pot chemo-enzymatic conversion
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
production of D-tert-leucine-nitrile from racemic tert-leucine-nitrile by use of enzyme plus D-selective amidase from Variovorax paradoxus
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
enzyme can be used in conjunction with a stereoselective amidase to synthesize ethyl (S)-4-chloro-3-hydroxybutyrate, an intermediate for a hypercholesterolemia drug, Atorvastatin
-
synthesis
-
use of recombinant Corynebacterium cells for the production of acrylamide from acrylonitrile results in a conversion yield of 93% and a final acrylamide concentration of 42.5% within 6 h when the total amount of fed acrylonitrile is 456 g
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
useful for acrylamide production
-
synthesis
-
industrial production of highly purified acrylamide and nicotinamide. The thermostability and catalytic efficiency of the subunit-fused nitrile hydratase is improved by semi-rational engineering
-
synthesis
-
nitrile hydratase is used for large scale industrial production of important commodities such as acrylamide and nicotinamide
-
synthesis
-
useful for modification of polyacrylonitrile fibers and granulates
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, operated in either batch or continuous mode, method optimization, overview
-
synthesis
-
bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, carried out in continuously stirred tank UF-membrane bioreactors arranged in series, the reactor configuration enables both enzymes, involved in the cascade reaction, to work with optimized kinetics, without any purification, exploiting their differing temperature dependences, method optimization, overview
-
synthesis
-
production of propionamide by use of enzyme in ultrafiltration-membrane reactor with maximum volumetric production of 0.5 g propionamide per litre and h
-
synthesis
-
the enzyme from Rhodococcus aetherivorans JB1208 shows high regioselectivity and strong substrate tolerance for alicyclic dinitrile and affords a potentially industrial route to gabapentin (a precursor of gamma-aminobutyric acid, which has been approved for treatment of a variety of central nervous system disorders, partial seizures, and restless legs syndrome)
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
production of nicotinamide (=vitamin B3) for vitamin supplement for food and animal feed
-
synthesis
-
H-NHase is used in the industrial production of acrylamide and nicotinamide
-
additional information
-
Rhodococcus erythropolis A4 converts benzonitrile herbicides into amides, the strain is able to hydrolyze 2,6-dichlorobenzamide into 2,6-dichlorobenzoic acid, and produces also the carboxylic acids from the other herbicides. Transformation of nitriles into amides decreases acute toxicities for chloroxynil and dichlobenil, but increases them for bromoxynil and ioxynil. The amides inhibit root growth in Lactuca sativa less than the nitriles but more than the acids. The conversion of the nitrile group may be the first step in the mineralization of benzonitrile herbicides but cannot be itself considered to be a detoxification
additional information
-
Rhodococcus rhodochrous PA-34 converts benzonitrile herbicides into amides, but the strain does not hydrolyze 2,6-dichlorobenzamide into 2,6-dichlorobenzoic acid. Transformation of nitriles into amides decreases acute toxicities for chloroxynil and dichlobenil, but increases them for bromoxynil and ioxynil. The amides inhibit root growth in Lactuca sativa less than the nitriles but more than the acids. The conversion of the nitrile group may be the first step in the mineralization of benzonitrile herbicides but cannot be itself considered to be a detoxification
additional information
-
Rhodococcus erythropolis A4 converts benzonitrile herbicides into amides, the strain is able to hydrolyze 2,6-dichlorobenzamide into 2,6-dichlorobenzoic acid, and produces also the carboxylic acids from the other herbicides. Transformation of nitriles into amides decreases acute toxicities for chloroxynil and dichlobenil, but increases them for bromoxynil and ioxynil. The amides inhibit root growth in Lactuca sativa less than the nitriles but more than the acids. The conversion of the nitrile group may be the first step in the mineralization of benzonitrile herbicides but cannot be itself considered to be a detoxification
-
additional information
-
Rhodococcus rhodochrous PA-34 converts benzonitrile herbicides into amides, but the strain does not hydrolyze 2,6-dichlorobenzamide into 2,6-dichlorobenzoic acid. Transformation of nitriles into amides decreases acute toxicities for chloroxynil and dichlobenil, but increases them for bromoxynil and ioxynil. The amides inhibit root growth in Lactuca sativa less than the nitriles but more than the acids. The conversion of the nitrile group may be the first step in the mineralization of benzonitrile herbicides but cannot be itself considered to be a detoxification
-