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Information on EC 3.5.5.1 - nitrilase
for references in articles please use BRENDA:EC3.5.5.1
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EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.5 In nitriles
3.5.5.1 nitrilase
IUBMB Comments
Acts on a wide range of aromatic nitriles including (indol-3-yl)acetonitrile, and also on some aliphatic nitriles, and on the corresponding acid amides. cf. EC 4.2.1.84 nitrile hydratase.
The enzyme appears in viruses and cellular organisms
- 3.5.5.1
-
enantioselectivity
- amidase
-
hydratase
- rhodococcus
-
biocatalyst
- synthesis
- rhodochrous
- benzonitrile
- mandelonitrile
-
indole-3-acetic
- alcaligenes
- indole-3-acetonitrile
- 3-cyanopyridine
-
dinitriles
- phenylacetonitrile
- acrylonitrile
- bromoxynil
-
r-mandelic
- nhase
-
acidovorax
- ozaenae
- facilis
- industry
-
iminodiacetic
- gibberella
- analysis
showSynonyms
nitrilase, nitrilase 1, nitrilase bll6402, cyc705, nitrile aminohydrolase, benzonitrilase a, nlase, nitmc-fb, nitrilase i, nitras-atii, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetonitrilase
-
-
-
-
Arylacetonitrilase
-
-
-
-
BaNIT
benzonitrilase
-
-
-
-
benzonitrilase A
benzonitrilase B
bll6402
blr3397
cyc705
NIT
NIT1
NIT2
NIT3
NitA
NitAk1
NitraS-ATII
nitrilase 1
nitrilase AtNIT1
nitrilase bll6402
nitrile hydratase/amidase
Nlase
PaCNit
SsAH
SSO2122
additional information
BaNIT
-
chimera harboring 12 amino acid substitutions is obtained using nitrilase from Arabis alpine (AaNIT) and Brassica rapa (BrNIT)
BaNIT
-
chimera using nitrilase from Arabis alpine (AaNIT) and Brassica rapa (BrNIT)
BaNIT
-
chimera harboring 12 amino acid substitutions is obtained using nitrilase from Arabis alpine (AaNIT) and Brassica rapa (BrNIT)
BaNIT
-
chimera using nitrilase from Arabis alpine (AaNIT) and Brassica rapa ()
nitrile hydratase/amidase
Rhodococcus sp. (in: high G+C Gram-positive bacteria) Novo SP361
-
-
-
additional information
the enzyme belong to the nitrilase superfamily, branch 1.1 auxin-producing nitrilase, overview
additional information
enzyme belong to branch 10 of the nitrilase superfamily, overview
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a nitrile + 2 H2O = a carboxylate + NH3
-
-
-
-
a nitrile + 2 H2O = a carboxylate + NH3
acts on a wide range of aromatic nitriles including (indole-3-yl)-acetonitrile, and also on some aliphatic nitriles, and on the corresponding acid amines
-
a nitrile + 2 H2O = a carboxylate + NH3
Cys186 is essential for catalytic activity
a nitrile + 2 H2O = a carboxylate + NH3
Cys179 is essential for catalytic activity
a nitrile + 2 H2O = a carboxylate + NH3
enzyme structure and reaction mechanism
a nitrile + 2 H2O = a carboxylate + NH3
enzyme structure and reaction mechanism
a nitrile + 2 H2O = a carboxylate + NH3
acts on a wide range of aromatic nitriles including (indole-3-yl)-acetonitrile, and also on some aliphatic nitriles, and on the corresponding acid amines
Rhodococcus sp. (in: high G+C Gram-positive bacteria) Novo SP361
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of amide bond
hydrolysis of C-N bond
nitrile hydrolysis
-
-
N-bond hydrolysis
-
hydrolysis of C-N bond
Rhodococcus sp. (in: high G+C Gram-positive bacteria) Novo SP361
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
indole glucosinolate activation (herbivore attack), indole-3-acetate biosynthesis II, indole-3-acetate biosynthesis V (bacteria and fungi)
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SYSTEMATIC NAME
IUBMB Comments
nitrile aminohydrolase
Acts on a wide range of aromatic nitriles including (indol-3-yl)acetonitrile, and also on some aliphatic nitriles, and on the corresponding acid amides. cf. EC 4.2.1.84 nitrile hydratase.
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CAS REGISTRY NUMBER
COMMENTARY
157297-79-5
Arabidopsis thaliana columbiana and Lansberg gene NIT2
157575-01-4
Arabidopsis thaliana columbiana gene NIT3
157575-02-5
Arabidopsis thaliana columbiana gene NIT4
205331-43-7
Arabidopsis thaliana nit2 isoenzyme2
205394-78-1
Arabidopsis thaliana nit3 isoenzyme3
205394-80-5
Arabidopsis thaliana nit1 isoenzyme1
9024-90-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+/-)-isobutylsuccinonitrile + 2 H2O
(S)-3-cyano-5-methyl hexanoic acid
-
Substrates: -
Products: -
Products: -
?
(+/-)-isobutylsuccinonitrile + H2O
(S)-3-cyano-5-methyl hexanoic acid
-
Substrates: -
Products: -
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?
(2-chlorophenyl)(hydroxy)acetonitrile + H2O
2-(2-chlorophenyl)-2-hydroxyacetamide
Substrates: -
Products: -
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?
(3S)-3-(2,4-difluorophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(2,4-difluorophenyl)-3-hydroxypropanoic acid + NH3
(3S)-3-(3-methoxyphenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(3-methoxyphenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 88% yield, 95% enantiomeric excess
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?
(3S)-3-(3-nitrophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(3-nitrophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 88% yield, 99% enantiomeric excess
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?
(3S)-3-(4-bromophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-bromophenyl)-3-hydroxypropanoic acid + NH3
(3S)-3-(4-chlorophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-chlorophenyl)-3-hydroxypropanoic acid + NH3
(3S)-3-(4-cyanophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-cyanophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 92% yield, 95% enantiomeric excess
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?
(3S)-3-(4-fluorophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-fluorophenyl)-3-hydroxypropanoic acid + NH3
(3S)-3-(4-methoxyphenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-methoxyphenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 91% yield, 99% enantiomeric excess
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?
(3S)-3-(4-methylphenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-methylphenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 91% yield, 99% enantiomeric excess
Products: -
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?
(3S)-3-(4-nitrophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-nitrophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 87% yield, 97% enantiomeric excess
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?
(3S)-isobutylsuccinonitrile + H2O
(3S)-3-cyano-5-methyl hexanoic acid
-
Substrates: specific for the (3S)-isomer
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?
(methylthio)acetonitrile + H2O
2-(methylthio)acetic acid + NH3
Substrates: -
Products: -
Products: -
?
(phenylthio)acetonitrile + H2O
2-(phenylthio)acetic acid + NH3
Substrates: -
Products: -
Products: -
?
(R)-2-chloromandelonitrile + H2O
(R)-2-chloromandelic acid + (S)-2-chloromandelic acid + NH3
(R,S)-2-hydroxy-2-phenylacetonitrile + 2 H2O
(R)-2-hydroxy-2-phenylacetic acid + NH3
Substrates: i.e. (R,S)-mandelonitrile, preferred substrate, highly enantioselective reaction
Products: -
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?
(R,S)-2-phenylpropionitrile + H2O
?
-
Substrates: 1% activity compared to benzonitrile
Products: -
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?
(S)-2-acetoxy-2-phenylacetonitrile + H2O
(S)-2-acetoxy-2-phenylacetic acid + (S)-2-acetoxy-2-phenylacetamide
1,2-phenylenediacetonitrile + H2O
1,2-phenylenediacetic acid + NH3
Substrates: -
Products: -
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?
1,2-phenylenediacetonitrile + H2O
? + NH3
Substrates: 0.063% activity compared to iminodiacetonitrile
Products: -
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?
1,3-phenylenediacetonitrile + H2O
1,3-phenylenediacetic acid + NH3
Substrates: -
Products: -
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?
1,4-benzodinitrile + H2O
benzoic acid + NH3
-
Substrates: best substrate
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?
1,4-dicyanobutane + H2O
? + NH3
Substrates: 27.1% activity compared to iminodiacetonitrile
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?
1,4-dicyanobutane + H2O
hexanedioic acid + NH3
-
Substrates: 97% yield
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?
1,4-phenylenediacetonitrile + H2O
1,4-phenylenediacetic acid + NH3
Substrates: -
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?
1,5-dicyanopentane + H2O
heptanedioic acid + NH3
-
Substrates: 90% yield
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?
1,6-dicyanohexane + H2O
octanedioic acid + NH3
-
Substrates: 88% yield
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?
1-(cyanoacetyl)pyrrolidine + H2O
? + NH3
Substrates: low activity
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?
1-cyanocyclohexaneacetonitrile + H2O
1-cyanocyclohexaneacetic acid + NH3
Substrates: -
Products: -
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?
2 (R,S)-mandelonitrile + 2 H2O
(R)-(-)-mandelic acid + (S)-mandelonitrile
-
Substrates: -
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?
2 phenylacetonitrile + H2O
2-phenylacetate + NH3
-
Substrates: -
Products: -
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?
2,2-dimethylcyclopropyl cyanide + 2 H2O
2,2-dimethylcyclopropyl carboxylate + NH3
Substrates: -
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?
2,4-dichlorophenyl acetonitrile + 2 H2O
2,4-dichlorophenyl acetic acid + NH3
-
Substrates: -
Products: -
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?
2,4-pyridinedicarbonitrile + H2O
2-cyanopyridine-4-carboxylic acid + NH3
-
Substrates: 7% activity compared to benzonitrile
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?
2,6-pyridinedicarbonitrile + H2O
6-cyanopyridine-2-carboxylic acid + NH3
-
Substrates: 5% activity compared to benzonitrile
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?
2-amino-2,3-dimethylbutanenitrile + 2 H2O
? + NH3
Substrates: -
Products: -
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?
2-amino-4-methylbenzonitrile + 2 H2O
2-amino-4-methylbenzoic acid + NH3
-
Substrates: -
Products: -
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?
2-amino-5-chloro-benzonitrile + 2 H2O
2-amino-5-chloro-benzoic acid + NH3
-
Substrates: -
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?
2-aminobenzonitrile + 2 H2O
2-aminobenzoic acid + NH3
-
Substrates: -
Products: -
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?
2-aminobutyronitrile + 2 H2O
2-aminobutyric acid + NH3
Substrates: high activity
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?
2-aminobutyronitrile + H2O
2-aminobutyric acid + NH3
-
Substrates: -
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?
2-aminopropionitrile + H2O
2-aminopropionic acid + NH3
-
Substrates: low activity
Products: -
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?
2-bromobenzonitrile + H2O
2-bromobenzoic acid + NH3
-
Substrates: best substrate of strain NCIB11216 and strain NCIB11215
Products: -
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?
2-chloro-2-phenylacetonitrile + H2O
2-chloro-2-phenylacetic acid + 2-chloro-2-phenylacetamide
2-chloro-3-cyanopyridine + H2O
?
-
Substrates: 0.21% activity compared to 3-cyanopyridine
Products: -
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?
2-chlorobenzonitrile + H2O
2-chlorobenzoic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: 1% of the activity compared to 2-cyanopyridine
Products: -
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?
2-chloromandelonitrile + 2 H2O
2-chloromandelic acid + NH3
Substrates: -
Products: -
Products: -
?
2-chloromandelonitrile + H2O
2-chloromandelic acid + NH3
Substrates: -
Products: -
Products: -
?
2-chloromandelonitrile + H2O
?
-
Substrates: 7% of the activity as compared to benzoylacetonitrile
Products: -
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?
2-chlorophenylacetonitrile + H2O
?
-
Substrates: 38% of the activity as compared to benzoylacetonitrile
Products: -
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?
2-cyanopyrazine + H2O
pyrazine-2-carboxylic acid + NH3
-
Substrates: -
Products: -
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?
2-cyanopyridine + 2 H2O
picolinic acid + NH3
-
Substrates: -
Products: -
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?
2-furanocarbonitrile + H2O
furan-2-carboxylic acid + NH3
-
Substrates: best substrate
Products: -
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?
2-furonitrile + 2 H2O
furoic acid + NH3
Substrates: no activity with wild-type enzyme, high activity with mutant enzyme R95T/L169A/S224Q
Products: -
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?
2-methylbutyronitrile + H2O
2-methylbutyric acid + NH3
-
Substrates: -
Products: -
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?
2-methylglutaronitrile + 4 H2O
2-methylglutaric acid + 2 NH3
Pyrococcus sp. MC-FB
-
Substrates: 9% of the activity compared to 2-cyanopyridine
Products: -
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?
2-nitrobenzonitrile + H2O
2-nitrobenzoic acid + NH3
-
Substrates: strain NCIB11215
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?
2-phenylacetonitrile + 2 H2O
2-phenylacetic acid + NH3
-
Substrates: 10.8% activity compared to benzonitrile
Products: -
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?
2-phenylacetonitrile + 2 H2O
phenylacetate + NH3
-
Substrates: substrate for isozyme complex NIT4A/B2
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?
2-phenylglycinonitrile + 2 H2O
amino(phenyl)acetic acid + NH3
Substrates: -
Products: -
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?
3,4,5-trimethoxybenzonitrile + 2 H2O
3,4,5-trimethoxybenzoic acid + NH3
-
Substrates: -
Products: -
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?
3-(2,4-dichlorophenyl)-3-hydroxypropanenitrile + H2O
(S)-3-(2,4-dichlorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
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?
3-(2-chlorophenyl)-3-hydroxypropanenitrile + H2O
3-(2-chlorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
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?
3-(2-chlorophenyl)pentanedinitrile + H2O
(3S)-3-(2-chlorophenyl)-4-cyanobutanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 5.1fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 74% enantiomeric excess by wild-type enzyme and with 97% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
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?
3-(3-chlorophenyl)pentanedinitrile + H2O
(3S)-3-(3-chlorophenyl)-4-cyanobutanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 3.1fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 93% enantiomeric excess by wild-type enzyme and with 98% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
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?
3-(4-bromophenyl)pentanedinitrile + H2O
(3S)-3-(4-bromophenyl)-4-cyanobutanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 18.6fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 97% enantiomeric excess by wild-type enzyme and with more than 99% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
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?
3-(4-chlorophenyl)-3-hydroxypropanenitrile + H2O
(S)-3-(4-chlorophenyl)-3-hydroxypropanoic acid + NH3
3-(4-chlorophenyl)pentanedinitrile + H2O
(3S)-3-(4-chlorophenyl)-4-cyanobutanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 11.0fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 97% enantiomeric excess by wild-type enzyme and with 99% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
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3-(4-fluorophenyl)-3-hydroxypropanenitrile + H2O
(S)-3-(4-fluorophenyl)-3-hydroxypropanoic acid + NH3
3-(4-fluorophenyl)pentanedinitrile + H2O
(3S)-4-cyano-3-(4-fluorophenyl)butanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 8.8fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 99% enantiomeric excess by wild-type enzyme and with more than 99% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
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3-(4-hydroxyphenyl)pentanedinitrile + H2O
(3S)-4-cyano-3-(4-hydroxyphenyl)butanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 78fold higher than activity of wild-type enzyme
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?
3-(4-hydroxyphenyl)propanenitrile + H2O
3-(4-hydroxyphenyl)propanoic acid + NH3
-
Substrates: -
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?
3-(4-methoxyphenyl)pentanedinitrile + H2O
(3S)-4-cyano-3-(4-methoxyphenyl)butanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 12.8fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 98% enantiomeric excess by wild-type enzyme and with more than 99% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
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3-(4-methylphenyl)pentanedinitrile + H2O
(3S)-4-cyano-3-(4-methylphenyl)butanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 6.7fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 98% enantiomeric excess by wild-type enzyme and with 99% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
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3-(4-tert-butylphenyl)pentanedinitrile + H2O
(3S)-3-(4-tert-butylphenyl)-4-cyanobutanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is2.3fold higher than activity of wild-type enzyme
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3-aminobutyronitrile + H2O
3-aminobutyric acid + NH3
Substrates: 201% of the activity compared to benzonitrile
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?
3-anilinoproprionitrile + 2 H2O
3-anilinopropionate + NH3
Substrates: -
Products: -
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?
3-bromo-4-hydroxybenzonitrile + H2O
3-bromo-4-hydroxybenzoate + NH3
-
Substrates: low activity
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3-butenenitrile + H2O
3-butenoic acid + NH3
Substrates: the enzyme displays a relatively high degree of specificity for 3-butenenitrile. Helical twist and substrate size correlate and when binding pocket residues are exchanged between two nitrilases that show the same twist but different specificities, their specificities change. It is proposed that helical twist influences the overall size of the binding pocket
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3-chloro-4-fluorobenzonitrile + H2O
3-chloro-4-fluorobenzoic acid + NH3
-
Substrates: -
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?
3-chloromandelonitrile + H2O
3-chloromandelic acid + NH3
Substrates: -
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?
3-cyanobenzonitrile + H2O
3-cyanobenzoic acid + NH3
-
Substrates: -
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?
3-furonitrile + 2 H2O
furan 3-carboxylic acid + NH3
-
Substrates: -
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3-hydroxy-3-(2-methoxyphenyl)propanenitrile + H2O
(S)-3-hydroxy-3-(2-methoxyphenyl)propanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
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3-hydroxy-3-(3-methoxyphenyl)propanenitrile + H2O
(S)-3-hydroxy-3-(3-methoxyphenyl)propanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
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3-hydroxy-3-(4-methoxyphenyl)propanenitrile + H2O
(S)-3-hydroxy-3-(4-methoxyphenyl)propanoic acid + NH3
3-hydroxy-3-(4-methylphenyl)propanenitrile + H2O
(S)-3-hydroxy-3-(4-methylphenyl)propanoic acid + NH3
3-hydroxy-glutaronitrile + 2 H2O
3-hydroxy-glutaric acid + NH3
Substrates: -
Products: -
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?
3-hydroxybenzonitrile + H2O
3-hydroxybenzoate + NH3
-
Substrates: 8.4% activity compared to benzonitrile
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?
3-hydroxyglutaronitrile + 4 H2O
3-hydroxyglutaric acid + 2 NH3
Substrates: activity is 1.15% compared to activity with iminodiacetonitrile
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3-hydroxyglutaronitrile + H2O
? + NH3
Substrates: 1.15% activity compared to iminodiacetonitrile
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?
3-hydroxypropionitrile + H2O
3-hydroxypropionic acid + NH3
Substrates: 2.57% activity compared to iminodiacetonitrile
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?
3-methoxybenzonitrile + H2O
3-methoxybenzoic acid + NH3
-
Substrates: -
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3-phenylpentanedinitrile + H2O
(3S)-4-cyano-3-phenylbutanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 5.8fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 96% enantiomeric excess by wild-type enzyme and with 96% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
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3-phenylpropionitrile + H2O
3-phenylpropanoate + NH3
Substrates: activity is 7.24% compared to activity with iminodiacetonitrile
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3-phenylpropionitrile + H2O
3-phenylpropionate + NH3
Substrates: 151% of the activity compared to benzonitrile
Products: -
Products: -
?
3-tolunitrile + H2O
3-methylbenzoic acid + NH3
-
Substrates: 5.5% activity compared to benzonitrile
Products: -
Products: -
?
3-trans-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]prop-2-enenitrile + H2O
(2E)-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dien-1-yl]prop-2-enoic acid + NH3
3-[4-(dimethylamino)phenyl]pentanedinitrile + H2O
(3S)-4-cyano-3-[4-(dimethylamino)phenyl]butanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 28.0fold higher than activity of wild-type enzyme
Products: -
Products: -
?
3-[4-(methylsulfanyl)phenyl]pentanedinitrile + H2O
(3S)-4-cyano-3-[4-(methylsulfanyl)phenyl]butanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 18.0fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 97% enantiomeric excess by wild-type enzyme and with more than 99% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
Products: -
Products: -
?
3-[4-(propan-2-yl)phenyl]pentanedinitrile + H2O
(3S)-4-cyano-3-[4-(propan-2-yl)phenyl]butanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 18.0fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 95% enantiomeric excess by wild-type enzyme and with 98% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
Products: -
Products: -
?
3-[4-(trifluoromethyl)phenyl]pentanedinitrile + H2O
(3S)-4-cyano-3-[4-(trifluoromethyl)phenyl]butanoic acid
Substrates: the specific activity of mutant enzyme P194A/I201A/F202V is 4.8fold higher than activity of wild-type enzyme The S-enantiomer ist formed with 97% enantiomeric excess by wild-type enzyme and with 96% enantiomeric excess by the mutant enzyme P194A/I201A/F202V
Products: -
Products: -
?
4,5-dimethoxybenzonitrile + 2 H2O
4,5-dimethoxybenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-aminobenzonitrile + 2 H2O
4-aminobenzoic acid + NH3
Substrates: -
Products: -
Products: -
?
4-aminobutyronitrile + H2O
4-aminobutyric acid + NH3
Substrates: 251% of the activity compared to benzonitrile
Products: -
Products: -
?
4-bromobenzonitrile + 2 H2O
4-bromobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
4-chlorobenzoate + NH3
-
Substrates: 29.8% activity compared to benzonitrile
Products: -
Products: -
?
4-chloromandelonitrile + H2O
3-chloromandelic acid + NH3
Substrates: -
Products: -
Products: -
?
4-fluorobenzonitrile + 2 H2O
4-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzylcyanide + H2O
4-hydroxybenzoic acid + NH3
Substrates: low activity
Products: -
Products: -
?
4-methoxy-2-nitrobenzonitrile + 2 H2O
4-methoxy-2-nitrobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzonitrile + 2 H2O
4-methoxybenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl cyanide + 2 H2O
4-methoxyphenylacetic acid + NH3
Substrates: very low activity
Products: -
Products: -
?
4-methoxyphenylacetonitrile + H2O
4-methoxyphenylacetic acid + NH3
-
Substrates: 0.6% activity compared to 3-cyanopyridine
Products: -
Products: -
?
acetamide + H2O
acetate + NH3
-
Substrates: 119% of the activity as compared to acetonitrile
Products: -
Products: -
?
acrylamide + H2O
acrylic acid + NH3
-
Substrates: 101% of the activity as compared to acetonitrile
Products: -
Products: -
?
acrylonitrile + H2O
acrylate + NH3
Substrates: 400% of the activity compared to benzonitrile
Products: -
Products: -
?
adiponitrile + 2 H2O
adipic acid + 2 NH3
Substrates: -
Products: -
Products: -
?
allylcyanide + H2O
NH3 + but-3-enoic acid
-
Substrates: -
Products: -
Products: -
?
aminoacetonitrile + 2 H2O
aminoacetic acid + NH3
Substrates: 25% of the activity with acrylonitrile
Products: -
Products: -
?
aminoacetonitrile + H2O
aminoacetic acid + NH3
-
Substrates: 9.0% activity compared to 3-cyanopyridine
Products: -
Products: -
?
benzyl cyanide + 2 H2O
phenylacetic acid + NH3
Substrates: -
Products: -
Products: -
?
beta-aminopropionitrile + H2O
beta-aminopropionic acid + NH3
-
Substrates: 8.6% activity compared to 3-cyanopyridine
Products: -
Products: -
?
beta-cyano-L-alanine + 2 H2O
L-aspartate + NH3
Substrates: wild-type enzyme
Products: -
Products: -
?
bis-acrylamide + H2O
?
-
Substrates: 67% of the activity as compared to acetonitrile
Products: -
Products: -
?
bromoxynil + 2 H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
bromoxynil + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
-
Substrates: highly specific
Products: -
Products: -
?
butanedinitrile + H2O
? + NH3
Substrates: 104.8% activity compared to iminodiacetonitrile
Products: -
Products: -
?
chloroacetonitrile + H2O
chloroacetic acid + NH3
Substrates: low activity
Products: -
Products: -
?
chloroxynil + H2O
?
-
Substrates: 3',5-dihalogenated 4-hydroxybenzonitrile compound
Products: -
Products: -
?
cinnamonitrile + 2 H2O
cinnamic acid + NH3
Substrates: cinnamonitrile is a substrate for mutant enzyme K96R, no activity with wild-type enzyme
Products: -
Products: -
?
cis-1,2-dihydroxy-3-cyanocyclohexa-3,5-diene + H2O
5,6-dihydroxycyclohexa-1,3-diene-1-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
cis-5,6-dihydroxy-cyclohexa-1,3-diene-1-carbonitrile + H2O
(5R,6S)-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylic acid + NH3
cyano-5-valeramide + H2O
valeramide + NH3
Substrates: -
Products: -
Products: -
?
cyano-5-valeric acid + H2O
valeric acid + NH3
Substrates: -
Products: -
Products: -
?
cyclopropanecarbonitrile + H2O
cyclopropanecarboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
decanedinitrile + H2O
9-cyanononanoic acid + NH3
-
Substrates: 88% yield
Products: -
Products: -
?
di-phenylacetonitrile + H2O
? + NH3
Substrates: 72% of the activity compared to benzonitrile
Products: -
Products: -
?
DL-alpha-amino-4-methylthio butyronitrile + H2O
L-methionine + NH3
-
Substrates: -
Products: -
Products: -
?
DL-alpha-amino-n-capronitrile + H2O
L-norleucine + NH3
-
Substrates: -
Products: -
Products: -
?
DL-alpha-amino-n-valeronitrile + H2O
L-norvaline + NH3
-
Substrates: -
Products: -
Products: -
?
DL-alpha-aminoisocapronitrile + H2O
L-leucine + NH3
-
Substrates: -
Products: -
Products: -
?
DL-alpha-aminoisovaleronitrile + H2O
L-valine + NH3
-
Substrates: -
Products: -
Products: -
?
DL-alpha-aminopropionitrile + H2O
D-alanine + NH3
-
Substrates: -
Products: -
Products: -
?
fluoroacetonitrile + 2 H2O
fluoroacetic acid + NH3
Substrates: no activity with wild-type enzyme, moderate activity with mutant enzyme R95T/L169A/S224Q
Products: -
Products: -
?
glutaronitrile + H2O
? + NH3
Substrates: 319% of the activity compared to benzonitrile
Products: -
Products: -
?
glycinonitrile + H2O
?
-
Substrates: 23.27% activity compared to 3-cyanopyridine
Products: -
Products: -
?
hydroxy(phenyl)acetonitrile + H2O
?
-
Substrates: hydrolysis of alpha-hydroxynitriles is not enantioselective
Products: -
Products: -
?
hydroxy(phenyl)acetonitrile + H2O
hydroxy(phenyl)acetic acid + 2-hydroxy-2-phenylacetamide
indole acetonitrile + 2 H2O
indole acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
isobutyronitrile + H2O
isobutyric acid + NH3
-
Substrates: 4% activity compared to benzonitrile
Products: -
Products: -
?
isovaleronitrile + H2O
isovaleric acid + NH3
-
Substrates: 47.17% activity compared to 3-cyanopyridine
Products: -
Products: -
?
lactonitrile + H2O
lactic acid + NH3
-
Substrates: 4% activity compared to benzonitrile
Products: -
Products: -
?
m-tolunitrile + H2O
m-methylbenzoate + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + H2O
? + NH3
Substrates: 69% of the activity compared to benzonitrile
Products: -
Products: -
?
N-methyl-propionamide + H2O
?
-
Substrates: 161% of the activity as compared to acetonitrile
Products: -
Products: -
?
n-valeronitrile + H2O
n-valeric acid + NH3
-
Substrates: -
Products: -
Products: -
?
pentanenitrile + H2O
?
-
Substrates: 1.6% activity compared to 3-cyanopyridine
Products: -
Products: -
?
phenylacetonitrile + H2O
?
-
Substrates: 160% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
phenylglycinenitrile + 2 H2O
phenylglycine + NH3
Substrates: -
Products: -
Products: -
?
phenylpropionitrile + 2 H2O
phenylpropionate + NH3
-
Substrates: -
Products: -
Products: -
?
potassium cyanide + 2 H2O
potassium carbonate + NH3
Substrates: no activity with wild-type enzyme, high activity with mutant enzyme R95T/L169A/S224Q
Products: -
Products: -
?
propionitrile + H2O
propionate + NH3
Substrates: 416% of the activity compared to benzonitrile
Products: -
Products: -
?
pyrazinecarbonitrile + H2O
?
-
Substrates: 32.7% activity compared to 3-cyanopyridine
Products: -
Products: -
?
pyridine + H2O
?
-
Substrates: 23% of the activity as compared to acetonitrile
Products: -
Products: -
?
R(+)-mandelonitrile + H2O
?
Substrates: 316% substrate conversion compared to benzonitrile
Products: -
Products: -
?
succinonitrile + 2 H2O
succinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
trans-3-pentenenitrile + H2O
trans-3-pentenoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile + H2O
trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylic acid + NH3
trichloroacetonitrile + 2 H2O
trichloroacetate + NH3
Substrates: -
Products: -
Products: -
?
(2-ethylphenyl)(hydroxy)acetonitrile + H2O
2-(2-ethylphenyl)-2-hydroxyacetamide
Substrates: -
Products: -
Products: -
?
(2-ethylphenyl)(hydroxy)acetonitrile + H2O
2-(2-ethylphenyl)-2-hydroxyacetamide
Substrates: -
Products: -
Products: -
?
(2S)-1-[(4-methylphenyl)sulfonyl]piperidine-2-carbonitrile + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
(2S)-1-[(4-methylphenyl)sulfonyl]piperidine-2-carbonitrile + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
(3E)-2-hydroxypent-3-enenitrile + H2O
(3E)-2-hydroxypent-3-enamide
Substrates: -
Products: -
Products: -
?
(3E)-2-hydroxypent-3-enenitrile + H2O
(3E)-2-hydroxypent-3-enamide
Substrates: -
Products: -
Products: -
?
(3R)-1-[(4-methylphenyl)sulfonyl]piperidine-3-carbonitrile + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
(3R)-1-[(4-methylphenyl)sulfonyl]piperidine-3-carbonitrile + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
(3R)-3-methyl-1-[(4-methylphenyl)sulfonyl]pyrrolidine + H2O
?
-
Substrates: preferred substrate, amides are by-products of the nitrilase-catalyzed reaction
Products: -
Products: -
?
(3R)-3-methyl-1-[(4-methylphenyl)sulfonyl]pyrrolidine + H2O
?
-
Substrates: preferred substrate, amides are by-products of the nitrilase-catalyzed reaction
Products: -
Products: -
?
(3S)-3-(2,4-difluorophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(2,4-difluorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 91% yield, 99% enantiomeric excess
Products: -
Products: -
?
(3S)-3-(2,4-difluorophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(2,4-difluorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 91% yield, 99% enantiomeric excess
Products: -
Products: -
?
(3S)-3-(4-bromophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-bromophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 89% yield, 99% enantiomeric excess
Products: -
Products: -
?
(3S)-3-(4-bromophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-bromophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 89% yield, 99% enantiomeric excess
Products: -
Products: -
?
(3S)-3-(4-chlorophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-chlorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 92% yield, 99% enantiomeric excess
Products: -
Products: -
?
(3S)-3-(4-chlorophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-chlorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 92% yield, 99% enantiomeric excess
Products: -
Products: -
?
(3S)-3-(4-fluorophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-fluorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 93% yield, 99% enantiomeric excess
Products: -
Products: -
?
(3S)-3-(4-fluorophenyl)-3-hydroxypropanenitrile + H2O
(3S)-3-(4-fluorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: 93% yield, 99% enantiomeric excess
Products: -
Products: -
?
(3S)-3-hydroxy-3-phenylpropanenitrile + H2O
(3S)-3-hydroxy-3-phenylpropanoic acid + NH3
-
Substrates: 90% yield, 99% enantiomeric excess
Products: -
Products: -
?
(3S)-3-hydroxy-3-phenylpropanenitrile + H2O
(3S)-3-hydroxy-3-phenylpropanoic acid + NH3
-
Substrates: 90% yield, 99% enantiomeric excess
Products: -
Products: -
?
(E/Z)-2-methylbut-2-enenitrile + H2O
(E)-2-methylbut-2-enoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
(E/Z)-2-methylbut-2-enenitrile + H2O
(E)-2-methylbut-2-enoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
(E/Z)-2-methylbut-2-enenitrile + H2O
(E)-2-methylbut-2-enoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
(E/Z)-2-methylbut-2-enenitrile + H2O
(E)-2-methylbut-2-enoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
(methylthio)acetonitrile + H2O
(methylthio)acetic acid + NH3
Substrates: -
Products: -
Products: -
?
(methylthio)acetonitrile + H2O
(methylthio)acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
(R)-2-chloromandelonitrile + H2O
(R)-2-chloromandelic acid + (S)-2-chloromandelic acid + NH3
Substrates: -
Products: the wild type enzyme yields 76% (R)-2-chloromandelic acid and 9% (S)-2-chloromandelic acid at pH 7.5, as well as 12% (R)-2-chloromandelic acid and no (S)-2-chloromandelic acid at pH 4.5
Products: the wild type enzyme yields 76% (R)-2-chloromandelic acid and 9% (S)-2-chloromandelic acid at pH 7.5, as well as 12% (R)-2-chloromandelic acid and no (S)-2-chloromandelic acid at pH 4.5
?
(R)-2-chloromandelonitrile + H2O
(R)-2-chloromandelic acid + (S)-2-chloromandelic acid + NH3
Substrates: -
Products: the wild type enzyme yields 76% (R)-2-chloromandelic acid and 9% (S)-2-chloromandelic acid at pH 7.5, as well as 12% (R)-2-chloromandelic acid and no (S)-2-chloromandelic acid at pH 4.5
Products: the wild type enzyme yields 76% (R)-2-chloromandelic acid and 9% (S)-2-chloromandelic acid at pH 7.5, as well as 12% (R)-2-chloromandelic acid and no (S)-2-chloromandelic acid at pH 4.5
?
(S)-2-acetoxy-2-phenylacetonitrile + H2O
(S)-2-acetoxy-2-phenylacetic acid + (S)-2-acetoxy-2-phenylacetamide
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
(S)-2-acetoxy-2-phenylacetonitrile + H2O
(S)-2-acetoxy-2-phenylacetic acid + (S)-2-acetoxy-2-phenylacetamide
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
1,3-dicyanobenzene + H2O
?
-
Substrates: 8.4% activity compared to benzonitrile
Products: -
Products: -
?
1,3-dicyanobenzene + H2O
?
-
Substrates: 8.4% activity compared to benzonitrile
Products: -
Products: -
?
1,4-dicyanobenzene + H2O
?
-
Substrates: 79.5% activity compared to benzonitrile
Products: -
Products: -
?
1,4-dicyanobenzene + H2O
?
-
Substrates: 79.5% activity compared to benzonitrile
Products: -
Products: -
?
1-[(4-methylphenyl)sulfonyl]piperidine-4-carbonitrile + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
1-[(4-methylphenyl)sulfonyl]piperidine-4-carbonitrile + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
2 (R,S)-mandelonitrile + 4 H2O
(R)-mandelic acid + NH3 + (S)-mandelonitrile
-
Substrates: -
Products: -
Products: -
?
2 (R,S)-mandelonitrile + 4 H2O
(R)-mandelic acid + NH3 + (S)-mandelonitrile
-
Substrates: -
Products: -
Products: -
?
2 (R,S)-mandelonitrile + 4 H2O
(R)-mandelic acid + NH3 + (S)-mandelonitrile
-
Substrates: -
Products: -
Products: -
?
2 2-phenylacetonitrile + 3 H2O
phenylacetic acid + 2-phenylacetamide + NH3
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
2 2-phenylacetonitrile + 3 H2O
phenylacetic acid + 2-phenylacetamide + NH3
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
2 2-phenylpropionitrile + 3 H2O
2-phenylpropanoic acid + 2-phenylpropanamide + NH3
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
2 2-phenylpropionitrile + 3 H2O
2-phenylpropanoic acid + 2-phenylpropanamide + NH3
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
2 benzonitrile + 3 H2O
benzoic acid + benzamide + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
2 benzonitrile + 3 H2O
benzoic acid + benzamide + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
2 phenylacetonitrile + 3 H2O
phenylacetamide + phenylacetate + NH3
-
Substrates: in the presence of organic solvents, 25-95%, v/v
Products: -
Products: -
?
2 phenylacetonitrile + 3 H2O
phenylacetamide + phenylacetate + NH3
-
Substrates: -
Products: not completely converted to acid, 2% of the product is phenylacetamide
Products: not completely converted to acid, 2% of the product is phenylacetamide
?
2-amino-6-chloro-benzonitrile + 2 H2O
2-amino-6-chloro-benzoic acid + NH3
-
Substrates: good substrate, when the cells are induced by benzonitrile
Products: -
Products: -
?
2-amino-6-chloro-benzonitrile + 2 H2O
2-amino-6-chloro-benzoic acid + NH3
-
Substrates: good substrate, when the cells are induced by benzonitrile
Products: -
Products: -
?
2-amino-benzonitrile + H2O
2-aminobenzoic acid + NH3
-
Substrates: 88% of the activity as compared to acetonitrile
Products: -
Products: -
?
2-amino-benzonitrile + H2O
2-aminobenzoic acid + NH3
-
Substrates: 88% of the activity as compared to acetonitrile
Products: -
Products: -
?
2-chloro-2-phenylacetonitrile + H2O
2-chloro-2-phenylacetic acid + 2-chloro-2-phenylacetamide
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
2-chloro-2-phenylacetonitrile + H2O
2-chloro-2-phenylacetic acid + 2-chloro-2-phenylacetamide
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
2-chloro-4-cyanopyridine + H2O
?
-
Substrates: 7.48% activity compared to 3-cyanopyridine
Products: -
Products: -
?
2-chloro-4-cyanopyridine + H2O
?
-
Substrates: 75.9% activity compared to 3-cyanopyridine
Products: -
Products: -
?
2-chloro-4-cyanopyridine + H2O
?
-
Substrates: 75.9% activity compared to 3-cyanopyridine
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
2-pyridine carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
2-pyridine carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
2-pyridine carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
2-pyridinecarboxylic acid + NH3
-
Substrates: 7% activity compared to benzonitrile
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
2-pyridinecarboxylic acid + NH3
-
Substrates: 7% activity compared to benzonitrile
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
2-pyridinecarboxylic acid + NH3
-
Substrates: 7% activity compared to benzonitrile
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: low activity
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: no activity with wild-type enzyme, high activity with mutant enzyme R95T/L169A/S224Q
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: 110% of the activity compared to benzonitrile
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: 3.27% activity compared to iminodiacetonitrile
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: activity is 3.27% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
-
Substrates: 1.5% activity compared to 3-cyanopyridine
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine-2-carboxylic acid + NH3
-
Substrates: 14.2% activity compared to benzonitrile
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine-2-carboxylic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: -
Products: -
Products: -
?
2-fluorobenzonitrile + H2O
2-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-fluorobenzonitrile + H2O
2-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-fluorobenzonitrile + H2O
2-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-furanocarbonitrile + H2O
2-furanocarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-furanocarbonitrile + H2O
2-furanocarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-furanocarbonnitrile + H2O
2-furanocarboxylic acid + NH3
-
Substrates: 171% activity compared to benzonitrile
Products: -
Products: -
?
2-furanocarbonnitrile + H2O
2-furanocarboxylic acid + NH3
-
Substrates: 171% activity compared to benzonitrile
Products: -
Products: -
?
2-furanocarbonnitrile + H2O
2-furanocarboxylic acid + NH3
-
Substrates: 171% activity compared to benzonitrile
Products: -
Products: -
?
2-hydroxy-2-phenylpropionitrile + 2 H2O
2-hydroxy-2-phenylpropionic acid + NH3
-
Substrates: acetophenone cyanohydrin, the substrate is transformed in cells to the corresponding acid (atrolactate) and amide (atrolactamide) at a ratio of about 3.4:1. The (R)-acid and the (S)-amide are formed preferentially from acetophenone cyanohydrin
Products: i.e. atrolactic acid
Products: i.e. atrolactic acid
?
2-hydroxy-2-phenylpropionitrile + 2 H2O
2-hydroxy-2-phenylpropionic acid + NH3
-
Substrates: acetophenone cyanohydrin, the substrate is transformed in cells to the corresponding acid (atrolactate) and amide (atrolactamide) at a ratio of about 3.4:1. The (R)-acid and the (S)-amide are formed preferentially from acetophenone cyanohydrin
Products: i.e. atrolactic acid
Products: i.e. atrolactic acid
?
2-hydroxy-2-phenylpropionitrile + 2 H2O
2-hydroxy-2-phenylpropionic acid + NH3
Substrates: acetophenone cyanohydrin, the substrate is transformed in cells to the corresponding acid (atrolactate) and amide (atrolactamide) at a ratio of about 3.4:1. The (R)-acid and the (S)-amide are formed preferentially from acetophenone cyanohydrin
Products: i.e. atrolactic acid
Products: i.e. atrolactic acid
?
2-hydroxy-2-phenylpropionitrile + 2 H2O
2-hydroxy-2-phenylpropionic acid + NH3
Substrates: acetophenone cyanohydrin, the substrate is transformed in cells to the corresponding acid (atrolactate) and amide (atrolactamide) at a ratio of about 3.4:1. The (R)-acid and the (S)-amide are formed preferentially from acetophenone cyanohydrin
Products: i.e. atrolactic acid
Products: i.e. atrolactic acid
?
2-hydroxy-2-phenylpropionitrile + 2 H2O
2-hydroxy-2-phenylpropionic acid + NH3
-
Substrates: acetophenone cyanohydrin, the substrate is transformed in cells to the corresponding acid (atrolactate) and amide (atrolactamide) at a ratio of about 3.4:1. The (R)-acid and the (S)-amide are formed preferentially from acetophenone cyanohydrin
Products: i.e. atrolactic acid
Products: i.e. atrolactic acid
?
2-hydroxy-2-phenylpropionitrile + 2 H2O
2-hydroxy-2-phenylpropionic acid + NH3
-
Substrates: acetophenone cyanohydrin, the substrate is transformed in cells to the corresponding acid (atrolactate) and amide (atrolactamide) at a ratio of about 3.4:1. The (R)-acid and the (S)-amide are formed preferentially from acetophenone cyanohydrin
Products: i.e. atrolactic acid
Products: i.e. atrolactic acid
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: substrate contains a quaternary carbon atom in the alpha-position toward the nitrile group
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: substrate contains a quaternary carbon atom in the alpha-position toward the nitrile group
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
Substrates: substrate contains a quaternary carbon atom in the alpha-position toward the nitrile group
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
Substrates: substrate contains a quaternary carbon atom in the alpha-position toward the nitrile group
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: substrate contains a quaternary carbon atom in the alpha-position toward the nitrile group
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: substrate contains a quaternary carbon atom in the alpha-position toward the nitrile group
Products: -
Products: -
?
2-methylglutaronitrile + 2 H2O
4-cyanopentanoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-methylglutaronitrile + 2 H2O
4-cyanopentanoic acid + NH3
E1A0Z9
Substrates: regioselectivity of Nit1
Products: -
Products: -
?
2-phenylpropionitrile + 2 H2O
2-phenylpropionic acid + NH3
Substrates: -
Products: -
Products: -
?
2-phenylpropionitrile + 2 H2O
2-phenylpropionic acid + NH3
Substrates: -
Products: -
Products: -
?
2-phenylpropionitrile + 2 H2O
2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-phenylpropionitrile + 2 H2O
2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-thiophenacetonitrile + H2O
2-thiophenacetic acid + NH3
-
Substrates: strain JM3
Products: -
Products: -
?
2-thiophenacetonitrile + H2O
2-thiophenacetic acid + NH3
-
Substrates: strain JM3
Products: -
Products: -
?
2-toluonitrile + H2O
NH3 + 2-methylbenzoate
-
Substrates: -
Products: -
Products: -
?
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. bromoxynil, is a better substrate than ioxynil, but shows lower reaction rate than chloroxynil and benzonitrile
Products: -
Products: -
?
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. bromoxynil, is a better substrate than ioxynil, but shows lower reaction rate than chloroxynil and benzonitrile
Products: -
Products: -
?
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. bromoxynil, is a better substrate than ioxynil, but shows lower reaction rate than chloroxynil and benzonitrile
Products: -
Products: -
?
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. bromoxynil, is a better substrate than ioxynil, but shows lower reaction rate than chloroxynil and benzonitrile
Products: -
Products: -
?
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. bromoxynil, is a better substrate than ioxynil, but shows lower reaction rate than chloroxynil and benzonitrile
Products: -
Products: -
?
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. bromoxynil, is a better substrate than ioxynil, but shows lower reaction rate than chloroxynil and benzonitrile
Products: -
Products: -
?
3,5-dichloro-4-hydroxybenzonitrile + H2O
3,5-dichloro-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. chloroxynil, is a better substrate than bromoxynil and ioxynil, but shows lower reaction rate than benzonitrile
Products: -
Products: -
?
3,5-dichloro-4-hydroxybenzonitrile + H2O
3,5-dichloro-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. chloroxynil, is a better substrate than bromoxynil and ioxynil, but shows lower reaction rate than benzonitrile
Products: -
Products: -
?
3,5-dichloro-4-hydroxybenzonitrile + H2O
3,5-dichloro-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. chloroxynil, is a better substrate than bromoxynil and ioxynil, but shows lower reaction rate than benzonitrile
Products: -
Products: -
?
3,5-dichloro-4-hydroxybenzonitrile + H2O
3,5-dichloro-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. chloroxynil, is a better substrate than bromoxynil and ioxynil, but shows lower reaction rate than benzonitrile
Products: -
Products: -
?
3,5-dichloro-4-hydroxybenzonitrile + H2O
3,5-dichloro-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. chloroxynil, is a better substrate than bromoxynil and ioxynil, but shows lower reaction rate than benzonitrile
Products: -
Products: -
?
3,5-dichloro-4-hydroxybenzonitrile + H2O
3,5-dichloro-4-hydroxybenzoic acid + NH3
-
Substrates: i.e. chloroxynil, is a better substrate than bromoxynil and ioxynil, but shows lower reaction rate than benzonitrile
Products: -
Products: -
?
3,5-diiodo-4-hydroxybenzonitrile + H2O
3,5-diiodo-4-hydroxybenzoic acid + NH3
-
Substrates: worst substrate with lowest reaction rate
Products: -
Products: -
?
3,5-diiodo-4-hydroxybenzonitrile + H2O
3,5-diiodo-4-hydroxybenzoic acid + NH3
-
Substrates: worst substrate with lowest reaction rate
Products: -
Products: -
?
3,5-diiodo-4-hydroxybenzonitrile + H2O
3,5-diiodo-4-hydroxybenzoic acid + NH3
-
Substrates: worst substrate with lowest reaction rate
Products: -
Products: -
?
3,5-diiodo-4-hydroxybenzonitrile + H2O
3,5-diiodo-4-hydroxybenzoic acid + NH3
-
Substrates: worst substrate with lowest reaction rate
Products: -
Products: -
?
3,5-diiodo-4-hydroxybenzonitrile + H2O
3,5-diiodo-4-hydroxybenzoic acid + NH3
-
Substrates: worst substrate with lowest reaction rate
Products: -
Products: -
?
3,5-diiodo-4-hydroxybenzonitrile + H2O
3,5-diiodo-4-hydroxybenzoic acid + NH3
-
Substrates: worst substrate with lowest reaction rate
Products: -
Products: -
?
3-(4-chlorophenyl)-3-hydroxypropanenitrile + H2O
(S)-3-(4-chlorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-(4-chlorophenyl)-3-hydroxypropanenitrile + H2O
(S)-3-(4-chlorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-(4-fluorophenyl)-3-hydroxypropanenitrile + H2O
(S)-3-(4-fluorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-(4-fluorophenyl)-3-hydroxypropanenitrile + H2O
(S)-3-(4-fluorophenyl)-3-hydroxypropanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-aminobenzonitrile + H2O
3-aminobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-aminobenzonitrile + H2O
3-aminobenzoic acid + NH3
-
Substrates: 2% activity compared to benzonitrile
Products: -
Products: -
?
3-aminobenzonitrile + H2O
3-aminobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-aminobenzonitrile + H2O
3-aminobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-aminobenzonitrile + H2O
3-aminobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-bromobenzonitrile + H2O
3-bromobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-bromobenzonitrile + H2O
3-bromobenzoic acid + NH3
-
Substrates: best substrate
Products: -
Products: -
?
3-chlorobenzonitrile + 2 H2O
3-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + 2 H2O
3-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + 2 H2O
3-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + 2 H2O
3-chlorobenzoic acid + NH3
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + 2 H2O
3-chlorobenzoic acid + NH3
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + H2O
3-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + H2O
3-chlorobenzoic acid + NH3
-
Substrates: 41% activity compared to benzonitrile
Products: -
Products: -
?
3-chlorobenzonitrile + H2O
3-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + H2O
3-chlorobenzoic acid + NH3
-
Substrates: 87% activity compared to benzonitrile
Products: -
Products: -
?
3-chlorobenzonitrile + H2O
3-chlorobenzoic acid + NH3
-
Substrates: 11% activity compared to benzonitrile
Products: -
Products: -
?
3-chlorobenzonitrile + H2O
3-chlorobenzoic acid + NH3
-
Substrates: 87% activity compared to benzonitrile
Products: -
Products: -
?
3-chlorobenzonitrile + H2O
3-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + H2O
3-chlorobenzoic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: 14% of the activity compared to 2-cyanopyridine
Products: -
Products: -
?
3-chlorobenzonitrile + H2O
3-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzoylacetonitrile + H2O
?
-
Substrates: 43% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
3-chlorobenzoylacetonitrile + H2O
?
-
Substrates: 43% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
3-pyridinecarboxylic acid + NH3
-
Substrates: 28% activity compared to benzonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
3-pyridinecarboxylic acid + NH3
-
Substrates: 41% activity compared to benzonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
3-pyridinecarboxylic acid + NH3
-
Substrates: 41% activity compared to benzonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
3-pyridinecarboxylic acid + NH3
-
Substrates: 41% activity compared to benzonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
Cereibacter sphaeroides LHS-305
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: 100% activity, the enzyme is highly specific towards heterocyclic nitriles such as 3- and 4-cyanopyridine
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: 100% activity, the enzyme is highly specific towards heterocyclic nitriles such as 3- and 4-cyanopyridine
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: lower activity for the purified enzyme compared to the activity in resting cells
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
Substrates: about 50% activity compared to acrylonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
Substrates: about 50% activity compared to acrylonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
Substrates: low activity
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
-
Substrates: 102% of the activity as compared to acetonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
Substrates: 50% of the activity with acrylonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
E1A0Z9
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine-3-carboxylic acid + NH3
-
Substrates: 32.4% activity compared to benzonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine-3-carboxylic acid + NH3
Substrates: 151% of the activity compared to benzonitrile
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine-3-carboxylic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: 30% of the activity compared to 2-cyanopyridine
Products: -
Products: -
?
3-cyanopyridine + H2O
pyridine 3-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + H2O
pyridine 3-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + H2O
pyridine 3-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
3-fluorobenzonitrile + H2O
3-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-fluorobenzonitrile + H2O
3-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-fluorobenzonitrile + H2O
3-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-(4-methoxyphenyl)propanenitrile + H2O
(S)-3-hydroxy-3-(4-methoxyphenyl)propanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-hydroxy-3-(4-methoxyphenyl)propanenitrile + H2O
(S)-3-hydroxy-3-(4-methoxyphenyl)propanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-hydroxy-3-(4-methylphenyl)propanenitrile + H2O
(S)-3-hydroxy-3-(4-methylphenyl)propanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-hydroxy-3-(4-methylphenyl)propanenitrile + H2O
(S)-3-hydroxy-3-(4-methylphenyl)propanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-hydroxy-3-phenylpropanenitrile + H2O
(S)-3-hydroxy-3-phenylpropanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-hydroxy-3-phenylpropanenitrile + H2O
(S)-3-hydroxy-3-phenylpropanoic acid + NH3
-
Substrates: nitrilase bll6402 catalyzes the enantioselective hydrolysis of aromatic beta-hydroxy nitriles to give (S)-enriched beta-hydroxy carboxylic acids with recovery of (R)-enriched beta-hydroxy nitriles
Products: -
Products: -
?
3-hydroxy-3-phenylpropionitrile + H2O
3-hydroxy-3-phenylpropionic acid + NH3
-
Substrates: beta-substituted substrate
Products: -
Products: -
?
3-hydroxy-3-phenylpropionitrile + H2O
3-hydroxy-3-phenylpropionic acid + NH3
Rhodococcus sp. (in: high G+C Gram-positive bacteria) Novo SP361
-
Substrates: beta-substituted substrate
Products: -
Products: -
?
3-hydroxybenzonitrile + H2O
3-hydroxybenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzonitrile + H2O
3-hydroxybenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzonitrile + H2O
3-hydroxybenzoic acid + NH3
-
Substrates: 80% activity compared to benzonitrile
Products: -
Products: -
?
3-hydroxybenzonitrile + H2O
3-hydroxybenzoic acid + NH3
-
Substrates: 1% activity compared to benzonitrile
Products: -
Products: -
?
3-hydroxybenzonitrile + H2O
3-hydroxybenzoic acid + NH3
-
Substrates: 80% activity compared to benzonitrile
Products: -
Products: -
?
3-hydroxyglutaronitrile + 2 H2O
(R)-3-hydroxy-4-cyanobutanoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-hydroxyglutaronitrile + 2 H2O
(R)-3-hydroxy-4-cyanobutanoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-hydroxypropionitrile + H2O
3-hydroxypropanoate + NH3
Substrates: low activity
Products: -
Products: -
?
3-hydroxypropionitrile + H2O
3-hydroxypropanoate + NH3
Substrates: very low activity
Products: -
Products: -
?
3-hydroxypropionitrile + H2O
3-hydroxypropanoate + NH3
Substrates: activity is 2.57% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
3-hydroxyvaleronitrile + H2O
3-hydroxyvaleric acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-hydroxyvaleronitrile + H2O
3-hydroxyvaleric acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-methoxylbenzoylacetonitrile + H2O
?
-
Substrates: 38% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
3-methoxylbenzoylacetonitrile + H2O
?
-
Substrates: 38% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
3-methylbenzonitrile + H2O
3-methylbenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-methylbenzonitrile + H2O
3-methylbenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
Substrates: 110% of the activity compared to benzonitrile
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: 16% of the activity compared to 2-cyanopyridine
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
-
Substrates: 841.7% activity compared to benzonitrile
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
-
Substrates: 174.8% activity compared to benzonitrile
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
-
Substrates: 841.7% activity compared to benzonitrile
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
-
Substrates: 174.8% activity compared to benzonitrile
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
-
Substrates: 841.7% activity compared to benzonitrile
Products: -
Products: -
?
3-nitrobenzonitrile + H2O
3-nitrobenzoic acid + NH3
-
Substrates: 174.8% activity compared to benzonitrile
Products: -
Products: -
?
3-phenylpropanenitrile + H2O
phenylacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-phenylpropanenitrile + H2O
phenylacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-phenylpropanenitrile + H2O
phenylacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-phenylpropionitrile + H2O
3-phenylpropionic acid + NH3
Substrates: the enzyme has 270times more activity with 3-phenylpropionitrile than that observed with benzonitrile
Products: -
Products: -
?
3-phenylpropionitrile + H2O
3-phenylpropionic acid + NH3
Substrates: -
Products: -
Products: -
?
3-phenylpropionitrile + H2O
3-phenylpropionic acid + NH3
Substrates: 7.24% activity compared to iminodiacetonitrile
Products: -
Products: -
?
3-phenylpropionitrile + H2O
3-phenylpropionic acid + NH3
Substrates: 7.24% activity compared to iminodiacetonitrile
Products: -
Products: -
?
3-phenylpropionitrile + H2O
3-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-phenylpropionitrile + H2O
3-phenylpropionic acid + NH3
E1A0Z9
Substrates: -
Products: -
Products: -
?
3-phenylproprionitrile + H2O
3-phenylpropionic acid + NH3
Substrates: 1650% substrate conversion compared to benzonitrile
Products: -
Products: -
?
3-phenylproprionitrile + H2O
3-phenylpropionic acid + NH3
Substrates: 1650% substrate conversion compared to benzonitrile
Products: -
Products: -
?
3-tolunitrile + H2O
3-methylbenzoate + NH3
-
Substrates: 33% activity compared to benzonitrile
Products: -
Products: -
?
3-tolunitrile + H2O
3-methylbenzoate + NH3
-
Substrates: 9% activity compared to benzonitrile
Products: -
Products: -
?
3-toluonitrile + H2O
NH3 + 3-methylbenzoate
-
Substrates: -
Products: -
Products: -
?
3-toluonitrile + H2O
NH3 + 3-methylbenzoate
-
Substrates: -
Products: -
Products: -
?
3-trans-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]prop-2-enenitrile + H2O
(2E)-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dien-1-yl]prop-2-enoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-trans-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]prop-2-enenitrile + H2O
(2E)-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dien-1-yl]prop-2-enoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-trans-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]prop-2-enenitrile + H2O
(2E)-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dien-1-yl]prop-2-enoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-aminobenzonitrile + H2O
4-aminobenzoic acid + NH3
-
Substrates: 7% activity compared to benzonitrile
Products: -
Products: -
?
4-aminobenzonitrile + H2O
4-aminobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-aminobenzonitrile + H2O
4-aminobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-aminobenzonitrile + H2O
4-aminobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-bromobenzonitrile + H2O
4-bromobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-bromobenzonitrile + H2O
4-bromobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + 2 H2O
4-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + 2 H2O
4-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + 2 H2O
4-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + 2 H2O
4-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + 2 H2O
4-chlorobenzoic acid + NH3
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + 2 H2O
4-chlorobenzoic acid + NH3
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
4-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
4-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
4-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
4-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
4-chlorobenzoic acid + NH3
-
Substrates: 40% activity compared to benzonitrile
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
4-chlorobenzoic acid + NH3
-
Substrates: 19% activity compared to benzonitrile
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
4-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
4-chlorobenzoic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: 11% of the activity compared to 2-cyanopyridine
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
?
Substrates: 329% substrate conversion compared to benzonitrile
Products: -
Products: -
?
4-chlorobenzonitrile + H2O
?
Substrates: 329% substrate conversion compared to benzonitrile
Products: -
Products: -
?
4-chlorobenzoylacetonitrile + H2O
?
-
Substrates: 16% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
4-chlorobenzoylacetonitrile + H2O
?
-
Substrates: 16% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
4-chlorobutyronitrile + H2O
4-chlorobutyrate + NH3
Substrates: activity is 11.1% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
4-chlorobutyronitrile + H2O
4-chlorobutyrate + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobutyronitrile + H2O
4-chlorobutyrate + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobutyronitrile + H2O
4-chlorobutyric acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobutyronitrile + H2O
4-chlorobutyric acid + NH3
Substrates: 11.1% activity compared to iminodiacetonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: best substrate
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
Substrates: 1138% substrate conversion compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
Substrates: 1138% substrate conversion compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: best substrate
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: best substrate
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: 130% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: best substrate showing 217% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: 130% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: best substrate showing 217% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: 130% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: best substrate showing 217% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
4-pyridinecarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
Substrates: no activity with wild-type enzyme, moderate activity with mutant enzyme R95T/L169A/S224Q
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
-
Substrates: 69.25% activity compared to 3-cyanopyridine, the enzyme is highly specific towards heterocyclic nitriles such as 3- and 4-cyanopyridine
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
-
Substrates: 0.07% activity compared to 3-cyanopyridine
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
-
Substrates: 69.25% activity compared to 3-cyanopyridine, the enzyme is highly specific towards heterocyclic nitriles such as 3- and 4-cyanopyridine
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
Substrates: 2.48% activity compared to iminodiacetonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
-
Substrates: 79.5% activity compared to 3-cyanopyridine
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
-
Substrates: 79.5% activity compared to 3-cyanopyridine
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine-4-carboxylic acid + NH3
-
Substrates: 410.7% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine-4-carboxylic acid + NH3
-
Substrates: 410.7% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine-4-carboxylic acid + NH3
Substrates: 225% of the activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + H2O
pyridine 4-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + H2O
pyridine 4-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + H2O
pyridine 4-carboxylic acid + NH3
Substrates: 410.7% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + H2O
pyridine 4-carboxylic acid + NH3
Substrates: 410.7% activity compared to benzonitrile
Products: -
Products: -
?
4-cyanopyridine + H2O
pyridine 4-carboxylic acid + NH3
Substrates: activity is 2.48% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
4-fluorobenzonitrile + H2O
4-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-fluorobenzonitrile + H2O
4-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-fluorobenzonitrile + H2O
4-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid + NH3
-
Substrates: 3% activity compared to benzonitrile
Products: -
Products: -
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid + NH3
-
Substrates: very low activity
Products: -
Products: -
?
4-hydroxyphenylacetonitrile + H2O
4-hydroxyphenylacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-hydroxyphenylacetonitrile + H2O
4-hydroxyphenylacetic acid + NH3
-
Substrates: substrate for isozyme complex NIT4A/B2
Products: -
Products: -
?
4-methylbenzonitrile + H2O
4-methylbenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-methylbenzonitrile + H2O
4-methylbenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzonitrile + H2O
4-nitrobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzonitrile + H2O
4-nitrobenzoic acid + NH3
Substrates: 151% of the activity compared to benzonitrile
Products: -
Products: -
?
4-nitrobenzonitrile + H2O
4-nitrobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzonitrile + H2O
4-nitrobenzoic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: 11% of the activity compared to 2-cyanopyridine
Products: -
Products: -
?
4-nitrobenzonitrile + H2O
4-nitrobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-phenylbutyronitrile + H2O
4-phenylbutyric acid + NH3
Substrates: -
Products: -
Products: -
?
4-phenylbutyronitrile + H2O
4-phenylbutyric acid + NH3
Substrates: -
Products: -
Products: -
?
4-phenylbutyronitrile + H2O
4-phenylbutyric acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-tolunitrile + H2O
4-methylbenzoate + NH3
-
Substrates: 16% activity compared to benzonitrile
Products: -
Products: -
?
4-tolunitrile + H2O
4-methylbenzoate + NH3
-
Substrates: 5% activity compared to benzonitrile
Products: -
Products: -
?
4-tolunitrile + H2O
4-methylbenzoic acid + NH3
-
Substrates: 125% activity compared to benzonitrile
Products: -
Products: -
?
4-tolunitrile + H2O
4-methylbenzoic acid + NH3
-
Substrates: 3.4% activity compared to benzonitrile
Products: -
Products: -
?
4-toluonitrile + H2O
NH3 + 4-methylbenzoate
-
Substrates: -
Products: -
Products: -
?
4-toluonitrile + H2O
NH3 + 4-methylbenzoate
-
Substrates: -
Products: -
Products: -
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6-heptenenitrile + H2O
6-heptenoic acid + NH3
Substrates: the enzyme shows a preference for several aliphatic alkenenitriles with peak activity against 6-heptenenitrile. Helical twist and substrate size correlate and when binding pocket residues are exchanged between two nitrilases that show the same twist but different specificities, their specificities change. It is proposed that helical twist influences the overall size of the binding pocket
Products: -
Products: -
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6-heptenenitrile + H2O
6-heptenoic acid + NH3
-
Substrates: substrate for isozyme NIT4A/B2
Products: -
Products: -
?
acetonitrile + 2 H2O
acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
acetonitrile + H2O
acetate + NH3
-
Substrates: 2.31% activity compared to 3-cyanopyridine
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Products: -
?
acetonitrile + H2O
acetate + NH3
Substrates: 135% of the activity compared to benzonitrile
Products: -
Products: -
?
acetonitrile + H2O
acetic acid + NH3
-
Substrates: 12% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
acetonitrile + H2O
acetic acid + NH3
-
Substrates: -
Products: -
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?
acetonitrile + H2O
acetic acid + NH3
-
Substrates: 1.0% activity compared to 3-cyanopyridine
Products: -
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?
acetonitrile + H2O
acetic acid + NH3
-
Substrates: no formation of amide
Products: -
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?
acetonitrile + H2O
acetic acid + NH3
-
Substrates: no formation of amide
Products: -
Products: -
?
acrylonitrile + 2 H2O
acrylic acid + NH3
Substrates: very low activity
Products: -
Products: -
?
acrylonitrile + 2 H2O
acrylic acid + NH3
-
Substrates: preferred substrate, acrylonitrile is also a good inducer of enzyme production
Products: -
Products: -
?
acrylonitrile + 2 H2O
acrylic acid + NH3
-
Substrates: preferred substrate, acrylonitrile is also a good inducer of enzyme production
Products: -
Products: -
?
acrylonitrile + 2 H2O
acrylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
acrylonitrile + 2 H2O
acrylic acid + NH3
Cereibacter sphaeroides LHS-305
-
Substrates: -
Products: -
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?
acrylonitrile + 2 H2O
acrylic acid + NH3
Substrates: best substrate
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: high activity
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: low activity
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: low activity
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
Substrates: -
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 35% activity compared to benzonitrile
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 43.96% activity compared to 3-cyanopyridine
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 43.96% activity compared to 3-cyanopyridine
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 6.6% activity compared to benzonitrile
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 6.6% activity compared to benzonitrile
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: -
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 6.6% activity compared to benzonitrile
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 107% of the activity as compared to acetonitrile
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 107% of the activity as compared to acetonitrile
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 17.2% activity compared to 3-cyanopyridine
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: best substrate, no formation of amide
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: best substrate of strain SI
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: best substrate, no formation of amide
Products: -
Products: -
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acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: only hydrolysed after recovered activity by preincubation with benzonitrile or dialysis against buffer containing 50%, v/v, glycerol and 10% saturated ammonium sulfate
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: best substrate
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 22.4% activity compared to benzonitrile
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
Substrates: 100% activity, the optimum substrate concentration is 225 mM acrylonitrile
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 22.4% activity compared to benzonitrile
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: best substrate
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: 22.4% activity compared to benzonitrile
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
Substrates: 100% activity, the optimum substrate concentration is 225 mM acrylonitrile
Products: -
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?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
adiponitrile + 2 H2O
adipic acid + NH3
Substrates: high activity
Products: -
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?
adiponitrile + H2O
adipic acid + NH3
Substrates: preferred substrate, specific for aliphatic nitriles
Products: -
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?
adiponitrile + H2O
adipic acid + NH3
Substrates: no formation of amide
Products: -
Products: -
?
adiponitrile + H2O
adipic acid + NH3
-
Substrates: 106.29% activity compared to 3-cyanopyridine
Products: -
Products: -
?
adiponitrile + H2O
adipic acid + NH3
Substrates: activity is 27.1% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
adiponitrile + H2O
adipic acid + NH3
-
Substrates: no formation of amide
Products: -
Products: -
?
adiponitrile + H2O
adipic acid + NH3
-
Substrates: no formation of amide
Products: -
Products: -
?
adiponitrile + H2O
adipic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: 3% of the activity compared to 2-cyanopyridine
Products: -
Products: -
?
allyl cyanide + H2O
prop-2-enoic acid + NH3
Substrates: high activity
Products: -
Products: -
?
allyl cyanide + H2O
prop-2-enoic acid + NH3
Substrates: -
Products: -
Products: -
?
alpha,alpha-dimethylmalononitrile + H2O
2-cyano-2-methylpropanoic acid + NH3
-
Substrates: 93% yield
Products: -
Products: -
?
alpha,alpha-dimethylmalononitrile + H2O
2-cyano-2-methylpropanoic acid + NH3
-
Substrates: 93% yield
Products: -
Products: -
?
aminoacetonitrile + H2O
?
Substrates: about 30% activity compared to acrylonitrile
Products: -
Products: -
?
aminoacetonitrile + H2O
?
Substrates: about 30% activity compared to acrylonitrile
Products: -
Products: -
?
benzamide + H2O
benzoate + NH3
Substrates: -
Products: -
Products: -
?
benzamide + H2O
benzoic acid + NH3
-
Substrates: 257% of the activity as compared to acetonitrile
Products: -
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?
benzamide + H2O
benzoic acid + NH3
-
Substrates: catalysed by a highly purified nitrilase, but very low activity
Products: -
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?
benzonitrile + 2 H2O
benzoate + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoate + NH3
Substrates: preferred substrate
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoate + NH3
-
Substrates: 94% of the activity as compared to acetonitrile
Products: -
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?
benzonitrile + 2 H2O
benzoate + NH3
-
Substrates: 94% of the activity as compared to acetonitrile
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoate + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoate + NH3
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoate + NH3
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: 100% substrate conversion
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: 100% substrate conversion
Products: -
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?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: strain ATCC 8750
Products: -
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benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: preferred substrate, when the cells are induced by benzonitrile
Products: -
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?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: strain ATCC 8750
Products: -
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?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: preferred substrate, when the cells are induced by benzonitrile
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Cereibacter sphaeroides LHS-305
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 42.14% activity compared to 3-cyanopyridine
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 42.14% activity compared to 3-cyanopyridine
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: very low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: only traces of activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: best substrate with highest reaction rate
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: best substrate with highest reaction rate
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: specific for nitrile groups directly attached to the benzene ring
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: high activity in strain NCIB11216 and strain NCIB11215
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 70.4% activity compared to 3-cyanopyridine
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 70.4% activity compared to 3-cyanopyridine
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: strain SI, low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: 7% of the activity compared to 2-cyanopyridine
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: the substrate concentration of 40 mM is optimum for hydrolyzing benzonitrile
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Rhodococcoides fascians MTCC-1531
-
Substrates: the substrate concentration of 40 mM is optimum for hydrolyzing benzonitrile
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: best substrate
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: best substrate with highest reaction rate
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: the substrate concentration of 40 mM is optimum for hydrolyzing benzonitrile
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: the substrate concentration of 40 mM is optimum for hydrolyzing benzonitrile
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: best substrate with highest reaction rate
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: best substrate with highest reaction rate
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: 100% activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: best substrate with highest reaction rate
Products: -
Products: -
?
benzoylacetonitrile + 2 H2O
benzoylacetate + NH3
-
Substrates: -
Products: -
Products: -
?
benzoylacetonitrile + 2 H2O
benzoylacetate + NH3
-
Substrates: -
Products: -
Products: -
?
benzyl (2S)-2-cyanopiperidine-1-carboxylate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
benzyl (2S)-2-cyanopiperidine-1-carboxylate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
benzyl (3R)-3-methylpyrrolidine-1-carboxylate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl (3R)-3-methylpyrrolidine-1-carboxylate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl 4-cyanopiperidine-1-carboxylate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl 4-cyanopiperidine-1-carboxylate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl [(1R,3R)-3-cyanocyclohexyl]carbamate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl [(1R,3R)-3-cyanocyclohexyl]carbamate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl [(1R,3R)-3-cyanocyclohexyl]carbamate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl [(1R,3R)-3-cyanocyclohexyl]carbamate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl [(1S,3R)-3-cyanocyclohexyl]carbamate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl [(1S,3R)-3-cyanocyclohexyl]carbamate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl [(1S,3R)-3-cyanocyclohexyl]carbamate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
benzyl [(1S,3R)-3-cyanocyclohexyl]carbamate + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
bromoxynil + H2O
?
-
Substrates: enzyme utilizes the herbicide substrate as nitrogen source
Products: -
Products: -
?
bromoxynil + H2O
?
-
Substrates: 3',5-dihalogenated 4-hydroxybenzonitrile compound, high activity, substrate is a herbicide
Products: -
Products: -
?
bromoxynil + H2O
?
-
Substrates: strain NCIB11215, very low activity, 3',5-dihalogenated 4-hydroxybenzonitrile compound
Products: -
Products: -
?
butyronitrile + H2O
butyrate + NH3
Substrates: 425% of the activity compared to benzonitrile
Products: -
Products: -
?
butyronitrile + H2O
butyrate + NH3
-
Substrates: preference of the enzyme for phenylglycinonitrile
Products: -
Products: -
?
butyronitrile + H2O
butyric acid + NH3
-
Substrates: 17.6% activity compared to benzonitrile
Products: -
Products: -
?
butyronitrile + H2O
butyric acid + NH3
-
Substrates: 20% activity compared to benzonitrile
Products: -
Products: -
?
cinnamonitrile + H2O
cinnamic acid + NH3
Substrates: 7.87% activity compared to iminodiacetonitrile
Products: -
Products: -
?
cinnamonitrile + H2O
cinnamic acid + NH3
Substrates: activity is 7.87% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
cinnamonitrile + H2O
cinnamic acid + NH3
Substrates: 7.87% activity compared to iminodiacetonitrile
Products: -
Products: -
?
cis-5,6-dihydroxy-cyclohexa-1,3-diene-1-carbonitrile + H2O
(5R,6S)-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
cis-5,6-dihydroxy-cyclohexa-1,3-diene-1-carbonitrile + H2O
(5R,6S)-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
crotonitrile + H2O
crotonic acid + NH3
Substrates: 80.3% activity compared to benzonitrile
Products: -
Products: -
?
crotonitrile + H2O
crotonic acid + NH3
Substrates: 80.3% activity compared to benzonitrile
Products: -
Products: -
?
crotononitrile + 2 H2O
crotonic acid + NH3
-
Substrates: -
Products: -
Products: -
?
crotononitrile + 2 H2O
crotonic acid + NH3
-
Substrates: -
Products: -
Products: -
?
crotononitrile + H2O
NH3 + (z)-but-2-en-1-ol
-
Substrates: -
Products: -
Products: -
?
crotononitrile + H2O
NH3 + (z)-but-2-en-1-ol
-
Substrates: -
Products: -
Products: -
?
crotononitrile + H2O
NH3 + (z)-but-2-en-1-ol
-
Substrates: low activity
Products: -
Products: -
?
cyclohexanecarbonitrile + 2 H2O
cyclohexanecarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
cyclohexanecarbonitrile + 2 H2O
cyclohexanecarboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
dodecanenitrile + H2O
dodecanoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
dodecanenitrile + H2O
dodecanoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
fumaronitrile + H2O
fumaric acid + NH3
Substrates: -
Products: -
Products: -
?
fumaronitrile + H2O
fumaric acid + NH3
-
Substrates: 84% yield
Products: -
Products: -
?
fumaronitrile + H2O
fumaric acid + NH3
-
Substrates: 84% yield
Products: -
Products: -
?
glutaronitrile + H2O
glutaric acid + NH3
-
Substrates: 93% yield
Products: -
Products: -
?
glutaronitrile + H2O
glutaric acid + NH3
E1A0Z9
Substrates: -
Products: -
Products: -
?
glutaronitrile + H2O
glutaric acid + NH3
Substrates: activity towards glutaronitrile is 8.5% of that towards succinonitrile
Products: -
Products: -
?
glycolonitrile + 2 H2O
glycolic acid + NH3
Substrates: high activity
Products: -
Products: -
?
glycolonitrile + 2 H2O
glycolic acid + NH3
Substrates: -
Products: -
Products: -
?
glycolonitrile + 2 H2O
glycolic acid + NH3
Substrates: 40% of the activity with acrylonitrile
Products: -
Products: -
?
glycolonitrile + H2O
?
-
Substrates: 18% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
glycolonitrile + H2O
?
Substrates: about 40% activity compared to acrylonitrile
Products: -
Products: -
?
glycolonitrile + H2O
?
Substrates: about 40% activity compared to acrylonitrile
Products: -
Products: -
?
glycolonitrile + H2O
ammonium glycolate + ?
-
Substrates: -
Products: -
Products: -
?
hydrocinnamonitrile + H2O
hydrocinnamic acid + NH3
-
Substrates: -
Products: -
Products: -
?
hydrocinnamonitrile + H2O
hydrocinnamic acid + NH3
-
Substrates: the enzyme has 431times more activity with hydrocinnamonitrile than that observed with benzonitrile
Products: -
Products: -
?
hydrocinnamonitrile + H2O
hydrocinnamic acid + NH3
-
Substrates: the enzyme has 431times more activity with hydrocinnamonitrile than that observed with benzonitrile
Products: -
Products: -
?
hydroxy(3-phenoxyphenyl)acetonitrile + H2O
2-hydroxy-2-(3-phenoxyphenyl)acetamide
Substrates: -
Products: -
Products: -
?
hydroxy(3-phenoxyphenyl)acetonitrile + H2O
2-hydroxy-2-(3-phenoxyphenyl)acetamide
Substrates: -
Products: -
Products: -
?
hydroxy(4-methylphenyl)acetonitrile + H2O
2-hydroxy-2-(4-methylphenyl)acetamide
Substrates: -
Products: -
Products: -
?
hydroxy(4-methylphenyl)acetonitrile + H2O
2-hydroxy-2-(4-methylphenyl)acetamide
Substrates: -
Products: -
Products: -
?
hydroxy(phenyl)acetonitrile + H2O
hydroxy(phenyl)acetic acid + 2-hydroxy-2-phenylacetamide
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
hydroxy(phenyl)acetonitrile + H2O
hydroxy(phenyl)acetic acid + 2-hydroxy-2-phenylacetamide
-
Substrates: the ratio of the nitrilase and nitrile hydratase activities of the enzyme is profoundly influenced by the electronic and steric properties of the reactant
Products: -
Products: -
?
iminiodiacetonitrile + 2 H2O
iminodiacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
iminiodiacetonitrile + 2 H2O
iminodiacetic acid + NH3
Roseibium aggregatum DSM 13394
-
Substrates: -
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
Substrates: high activity
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
-
Substrates: high activity
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
Substrates: -
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
-
Substrates: 58.07% activity compared to 3-cyanopyridine
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
Substrates: 100% activity
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
Substrates: 100% activity
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
-
Substrates: 27% activity compared to 3-cyanopyridine
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
Substrates: about 25% activity compared to acrylonitrile
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
Substrates: 20% of the activity with acrylonitrile
Products: -
Products: -
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
Substrates: about 25% activity compared to acrylonitrile
Products: -
Products: -
?
iminodiacetonitrile + H2O
iminodiacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
iminodiacetonitrile + H2O
iminodiacetic acid + NH3
Substrates: -
Products: -
Products: -
?
iminodiacetonitrile + H2O
iminodiacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
iminodiacetonitrile + H2O
iminodiacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
iminodiacetonitrile + H2O
iminodiacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indol-3-acetonitrile + H2O
indol-3-acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indol-3-acetonitrile + H2O
indol-3-acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indol-3-acetonitrile + H2O
indol-3-acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indol-3-acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indol-3-acetic acid + NH3
-
Substrates: substrate for isozyme complex NIT4A/B2
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
Substrates: isozymes are involved in indole-3-acetic acid production
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
Substrates: low activity
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
Substrates: poor substrate
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
K9NKH3
Substrates: -
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
Substrates: the reaction is catalyzed by the branch 1 of the nitrilase superfamily
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
Substrates: the reaction is catalyzed by the branch 1 of the nitrilase superfamily
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
Substrates: preferred substrate of NIT2
Products: -
Products: -
?
ioxynil + H2O
?
-
Substrates: 3',5-dihalogenated 4-hydroxybenzonitrile compound
Products: -
Products: -
?
ioxynil + H2O
?
-
Substrates: 3',5-dihalogenated 4-hydroxybenzonitrile compound, strain NCIB11215
Products: -
Products: -
?
isobutylsuccinonitrile + 2 H2O
isobutylsuccinic acid + NH3
-
Substrates: the by-product (S)-3-cyano-5-methylhexanoic amide is also formed
Products: -
Products: -
?
isobutylsuccinonitrile + 2 H2O
isobutylsuccinic acid + NH3
-
Substrates: the by-product (S)-3-cyano-5-methylhexanoic amide is also formed
Products: -
Products: -
?
isonicotinonitrile + H2O
isonicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
isonicotinonitrile + H2O
isonicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
malononitrile + 2 H2O
malonate + NH3
Substrates: -
Products: -
Products: -
?
malononitrile + 2 H2O
malonate + NH3
Substrates: -
Products: -
Products: -
?
malononitrile + H2O
malonic acid + NH3
Substrates: 78.9% activity compared to iminodiacetonitrile
Products: -
Products: -
?
malononitrile + H2O
malonic acid + NH3
Substrates: activity is 78.9% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
malononitrile + H2O
malonic acid + NH3
-
Substrates: 44% of the activity as compared to acetonitrile
Products: -
Products: -
?
malononitrile + H2O
malonic acid + NH3
-
Substrates: 44% of the activity as compared to acetonitrile
Products: -
Products: -
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
Substrates: -
Products: -
Products: -
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
-
Substrates: -
Products: 95% enantiomeric excess for (R)-isoform
Products: 95% enantiomeric excess for (R)-isoform
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
-
Substrates: stereoselective nitrilase
Products: -
Products: -
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
Substrates: best substrate of strain ATCC 8750, low activity in strain JM3
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
Substrates: best substrate of strain ATCC 8750, low activity in strain JM3
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
Substrates: high activity
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
Substrates: high activity
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
Substrates: 2.38% activity compared to iminodiacetonitrile
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
Substrates: 2.38% activity compared to iminodiacetonitrile
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + H2O
?
-
Substrates: 32% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
mandelonitrile + H2O
?
-
Substrates: 32% of the activity as compared to benzoylacetonitrile
Products: -
Products: -
?
mandelonitrile + H2O
mandelic acid + NH3
Substrates: activity is 2.38% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
mandelonitrile + H2O
mandelic acid + NH3
-
Substrates: -
Products: -
Products: -
?
mandelonitrile + H2O
mandelic acid + NH3
Substrates: -
Products: -
Products: -
?
methacrylonitrile + H2O
methylacrylic acid + NH3
-
Substrates: 14% activity compared to benzonitrile
Products: -
Products: -
?
methacrylonitrile + H2O
methylacrylic acid + NH3
-
Substrates: 14% activity compared to benzonitrile
Products: -
Products: -
?
methacrylonitrile + H2O
methylacrylic acid + NH3
-
Substrates: low activity
Products: -
Products: -
?
methacrylonitrile + H2O
methylacrylic acid + NH3
-
Substrates: very low activity in resting cells and for the purified enzyme only after recovered activity by dialysis against buffer containing 50%, v/v, glycerol and 10% saturated ammonium sulfate
Products: -
Products: -
?
n-butyronitrile + H2O
n-butyric acid + NH3
-
Substrates: -
Products: -
Products: -
?
n-butyronitrile + H2O
n-butyric acid + NH3
-
Substrates: -
Products: -
Products: -
?
N-[(1R,3R)-3-cyanocyclopentyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
N-[(1R,3R)-3-cyanocyclopentyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclohexyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclohexyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclohexyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclohexyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclohexyl]benzamide + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclohexyl]benzamide + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclopentyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclopentyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclopentyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
N-[(1S,3R)-3-cyanocyclopentyl]-4-methylbenzenesulfonamide + H2O
?
-
Substrates: preferred substrate
Products: -
Products: -
?
o-chlorobenzyl cyanide + 2 H2O
(o-chlorophenyl)acetid acid + NH3
-
Substrates: -
Products: -
Products: -
?
o-chlorobenzyl cyanide + 2 H2O
(o-chlorophenyl)acetid acid + NH3
Roseibium aggregatum DSM 13394
-
Substrates: -
Products: -
Products: -
?
o-hydroxy-benzonitrile + H2O
o-hydroxy-benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
o-hydroxy-benzonitrile + H2O
o-hydroxy-benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
o-hydroxy-benzonitrile + H2O
o-hydroxy-benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
o-hydroxy-benzonitrile + H2O
o-hydroxy-benzoic acid + NH3
Prescottella equi CCTCC.M.205114
-
Substrates: -
Products: -
Products: -
?
p-aminobenzyl cyanide + H2O
?
-
Substrates: strains ATCC 8750 and JM3
Products: -
Products: -
?
p-aminobenzyl cyanide + H2O
?
-
Substrates: strains ATCC 8750 and JM3
Products: -
Products: -
?
pentanenitrile + H2O
pentanoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
pentanenitrile + H2O
pentanoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
-
Substrates: 21.59% activity compared to 3-cyanopyridine
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
-
Substrates: 21.59% activity compared to 3-cyanopyridine
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
-
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
-
Substrates: in aqueous solution
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
-
Substrates: low activity
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
-
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
Roseibium aggregatum DSM 13394
-
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetic acid + NH3
Substrates: low activity
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetic acid + NH3
Substrates: low activity with the native enzyme, poor activity with the recombinant enzyme
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + H2O
phenylacetate + NH3
-
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + H2O
phenylacetate + NH3
Pseudomonas fluorescens DSM 7155
-
Substrates: -
Products: -
Products: -
?
phenylacetonitrile + H2O
phenylacetate + NH3
-
Substrates: -
Products: -
Products: -
?
phenylbutyronitrile + H2O
phenylbutyric acid + NH3
Substrates: -
Products: -
Products: -
?
phenylbutyronitrile + H2O
phenylbutyric acid + NH3
Substrates: high activity
Products: -
Products: -
?
phenylglycinonitrile + H2O
phenylglycine + NH3
-
Substrates: -
Products: -
Products: -
?
phenylglycinonitrile + H2O
phenylglycine + NH3
-
Substrates: -
Products: -
Products: -
?
phenylglycinonitrile + H2O
phenylglycine + NH3
-
Substrates: -
Products: -
Products: -
?
phenylglycinonitrile + H2O
phenylglycine + NH3
-
Substrates: preference of the enzyme for phenylglycinonitrile and butyronitrile as substrates
Products: -
Products: -
?
phenylglycinonitrile + H2O
phenylglycine + NH3
-
Substrates: low actiity
Products: -
Products: -
?
phenylpropionitrile + 2 H2O
phenylpropionic acid + NH3
Substrates: best substrate
Products: -
Products: -
?
phenylpropionitrile + 2 H2O
phenylpropionic acid + NH3
Substrates: -
Products: -
Products: -
?
phenylpropionitrile + 2 H2O
phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
phenylpropionitrile + 2 H2O
phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
potassium cyanide + H2O
potassium carbonate + NH3
-
Substrates: -
Products: -
Products: -
?
potassium cyanide + H2O
potassium carbonate + NH3
-
Substrates: -
Products: -
Products: -
?
potassium cyanide + H2O
potassium carbonate + NH3
-
Substrates: -
Products: -
Products: -
?
potassium cyanide + H2O
potassium carbonate + NH3
Trichoderma harzianum VSL291
-
Substrates: -
Products: -
Products: -
?
propionitrile + H2O
propionic acid + NH3
Substrates: -
Products: -
Products: -
?
propionitrile + H2O
propionic acid + NH3
Substrates: low activity
Products: -
Products: -
?
propionitrile + H2O
propionic acid + NH3
-
Substrates: 6.9% activity compared to benzonitrile
Products: -
Products: -
?
propionitrile + H2O
propionic acid + NH3
Substrates: low activity
Products: -
Products: -
?
propionitrile + H2O
propionic acid + NH3
-
Substrates: 18% activity compared to benzonitrile
Products: -
Products: -
?
propionitrile + H2O
propionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
propionitrile + H2O
propionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
propionitrile + H2O
propionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
propionitrile + H2O
propionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
succinonitrile + H2O
succinate + NH3
Substrates: activity is 104.8% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
succinonitrile + H2O
succinate + NH3
-
Substrates: low activity
Products: -
Products: -
?
succinonitrile + H2O
succinic acid + NH3
-
Substrates: 97% yield
Products: -
Products: -
?
succinonitrile + H2O
succinic acid + NH3
-
Substrates: 97% yield
Products: -
Products: -
?
succinonitrile + H2O
succinic acid + NH3
-
Substrates: 64.22% activity compared to 3-cyanopyridine
Products: -
Products: -
?
succinonitrile + H2O
succinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
succinonitrile + H2O
succinic acid + NH3
-
Substrates: 21.74% activity compared to 3-cyanopyridine
Products: -
Products: -
?
succinonitrile + H2O
succinic acid + NH3
Pyrococcus sp. MC-FB
-
Substrates: 18% of the activity compared to 2-cyanopyridine
Products: -
Products: -
?
succinonitrile + H2O
succinic acid + NH3
Substrates: -
Products: -
Products: -
?
thiophen-2-acetonitrile + H2O
thiophen-2-ylacetic acid + NH3
-
Substrates: 56.1% activity compared to benzonitrile
Products: -
Products: -
?
thiophen-2-acetonitrile + H2O
thiophen-2-ylacetic acid + NH3
-
Substrates: 56.1% activity compared to benzonitrile
Products: -
Products: -
?
trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile + H2O
trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile + H2O
trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
valeronitrile + 2 H2O
valeric acid + NH3
-
Substrates: -
Products: -
Products: -
?
valeronitrile + H2O
valeric acid + NH3
-
Substrates: 19.6% activity compared to benzonitrile
Products: -
Products: -
?
valeronitrile + H2O
valeric acid + NH3
-
Substrates: 45.07% activity compared to 3-cyanopyridine
Products: -
Products: -
?
valeronitrile + H2O
valeric acid + NH3
-
Substrates: 26% activity compared to benzonitrile
Products: -
Products: -
?
valeronitrile + H2O
valeric acid + NH3
Substrates: 4.9% activity compared to iminodiacetonitrile
Products: -
Products: -
?
valeronitrile + H2O
valeric acid + NH3
Substrates: activity is 4.9% compared to activity with iminodiacetonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of immobilized and free Escherichia coli cells recombinantly expressing the Acidovorax facilis nitrilase, overview. No activity with mandelonitrile, o-methoxyphenylacetonitrile, m-methoxyphenylacetonitrile, p-methoxyphenylacetonitrile, and phenylacetonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of immobilized and free Escherichia coli cells recombinantly expressing the Acidovorax facilis nitrilase, overview. No activity with mandelonitrile, o-methoxyphenylacetonitrile, m-methoxyphenylacetonitrile, p-methoxyphenylacetonitrile, and phenylacetonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: aliphatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Acidovorax facilis ATCC 55746
-
Substrates: preferred substrates: aliphatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: preferred substrates: aliphatic, aromatic, heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not hydrolyze benzamide
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not hydrolyze benzamide
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: aromatic nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme does not hydrolyze benzamide
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyzes aliphatic, heterocyclic and aromatic nitriles with different substitutions, and is efficient in conversion of both aliphatic and aromatic nitriles. Substrate specificity in vivo is dependent on the inducer component, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyzes aliphatic, heterocyclic and aromatic nitriles with different substitutions, and is efficient in conversion of both aliphatic and aromatic nitriles. No activity with any inducer on malononitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the reactions of nitrilase, EC 3.5.5.1, and arylacetonitrilase, EC 3.5.5.5, substrate specificity and enantioselectivity, overview. Steric hindrance with amino acid residue Tyr54 impairs the binding or conversion of sterically demanding substrates, homology modelling
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: monosubstituted phenylacetonitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrate: monosubstituted phenylacetonitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrate: monosubstituted phenylacetonitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrate: substituted aliphatic nitriles, phenylacetonitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrate: substituted aliphatic nitriles, phenylacetonitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrate: substituted aliphatic nitriles, phenylacetonitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: arylacetonitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrates: arylacetonitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrates: arylacetonitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: aliphatic, heterocyclic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrates: aliphatic, heterocyclic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrates: aliphatic, heterocyclic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme catalyzes the reactions of nitrilase, EC 3.5.5.1, and arylacetonitrilase, EC 3.5.5.5, substrate specificity and enantioselectivity, overview. Steric hindrance with amino acid residue Tyr54 impairs the binding or conversion of sterically demanding substrates, homology modelling
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: substituted aliphatic nitriles, phenylacetonitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: aliphatic, heterocyclic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: preferred substrate: monosubstituted phenylacetonitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrate: substituted aliphatic nitriles, phenylacetonitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: aliphatic, heterocyclic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrates: arylacetonitriles
Products: -
Products: -
-
additional information
?
-
Substrates: substrate specificity, overview. No activity with diaminomaleonitrile, 2,3-dicyanopyrazine, 4-hydroxybenzonitrile, 2-cyano-3-phenylpropionitrile, 4-aminophthalonitrile, and 4-nitrophthalonitrile
Products: -
Products: -
?
additional information
?
-
Substrates: preferred substrates: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: isozyme NIT2 might be involved in supplying indole-3-acetic acid during seed development rather than during stratification
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme NIT2 might be involved in supplying indole-3-acetic acid during seed development rather than during stratification
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme NIT2 might be involved in supplying indole-3-acetic acid during seed development rather than during stratification
Products: -
Products: -
?
additional information
?
-
-
Substrates: isozyme NIT2 might be involved in supplying indole-3-acetic acid during seed development rather than during stratification
Products: -
Products: -
?
additional information
?
-
Substrates: broad substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: broad substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: broad substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not convert cis-5,6-dihydroxy-cyclohexa-1,3-diene-1-carbonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: no activity with: benzonitrile, (R,S)-mandelonitrile and
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows a strong diastereopreference for cis- versus trans-gamma-amino nitriles
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity and chemoselectivity of native and recombinant enzymes, no activity of both with 2-chlorobenzonitrile, 2-phenylpropionitrile, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme shows a strong diastereopreference for cis- versus trans-gamma-amino nitriles
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: arylacetonitriles
Products: -
Products: -
-
additional information
?
-
Bacillus subtilis ZJB-063
-
Substrates: preferred substrates: arylacetonitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: nitrilase bll6402 effectively hydrolyzes alpha,omega-dinitriles to omega-cyanocarboxylic acids, and the selectivity is independent of the substrate chain length
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: mandelonitrile, beta-hydroxy nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrates: mandelonitrile, beta-hydroxy nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: nitrilase bll6402 effectively hydrolyzes alpha,omega-dinitriles to omega-cyanocarboxylic acids, and the selectivity is independent of the substrate chain length
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: mandelonitrile, beta-hydroxy nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: preferred substrates: mandelonitrile, beta-hydroxy nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: 3-cyano-L-alanine is no substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 3-cyano-L-alanine is no substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview. No activity with phenylacetonitrile, 4-methoxy-phenylacetonitrile, mandelonitrile, 2-amino propionitrile, and butyronitrile
Products: -
Products: -
?
additional information
?
-
Cereibacter sphaeroides LHS-305
-
Substrates: substrate specificity, overview. No activity with phenylacetonitrile, 4-methoxy-phenylacetonitrile, mandelonitrile, 2-amino propionitrile, and butyronitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: aliphatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: no activity with mandelonitrile and geranyl nitrile
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with fumaronitrile, succinonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with fumaronitrile, succinonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not hydrolyze 3,4-pyridinedicarbonitrile and 2,3-pyrazinedicarbonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows a strong diastereopreference for cis- versus trans-gamma-amino nitriles
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly chemoselective, producing less than 2% amides as by-products
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrate: aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme is highly chemoselective, producing less than 2% amides as by-products
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrate: aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme shows a strong diastereopreference for cis- versus trans-gamma-amino nitriles
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly chemoselective, producing less than 2% amides as by-products
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: aliphatic, aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrate: aromatic, and heterocyclic nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: no activity with 2-cyanopyridine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-cyanopyridine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity detected with: benzonitrile, 3-cyanopyridine, 2,3-dicyanopyrazine
Products: -
Products: -
?
additional information
?
-
-
Substrates: stricter substrate specificity compared to nitrilases from other species, strong preference for 4-hydroxybenzonitriles
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not hydrolyzed dichlobenil (2,6-dichlorobenzonitrile)
Products: -
Products: -
?
additional information
?
-
Substrates: preferred substrates: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme does not hydrolyzed dichlobenil (2,6-dichlorobenzonitrile)
Products: -
Products: -
?
additional information
?
-
Substrates: preferred substrates: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
Substrates: no activity with benzonitrile, phenylacetonitrile, 3-cyanopyridine, glycolonitrile, and dodecanenitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with benzonitrile, phenylacetonitrile, 3-cyanopyridine, glycolonitrile, and dodecanenitrile
Products: -
Products: -
?
additional information
?
-
Substrates: the suitable substrates for the purified nitrilase were short-chain aliphatic dinitriles
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with benzonitrile, phenylacetonitrile, 3-cyanopyridine, glycolonitrile, and dodecanenitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: phenylacetonitril
Products: -
Products: -
-
additional information
?
-
Paenarthrobacter nitroguajacolicus ZJUTB06-99
-
Substrates: preferred substrates: phenylacetonitril
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: arylaminonitriles
Products: -
Products: -
-
additional information
?
-
Pseudomonas aeruginosa 10145
-
Substrates: preferred substrates: arylaminonitriles
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme catalyzes the reactions of nitrilase, EC 3.5.5.1, and arylacetonitrilase, EC 3.5.5.5, substrate specificity and enantioselectivity, overview. Steric hindrance with amino acid residue Tyr54 impairs the binding or conversion of sterically demanding substrates, homology modelling
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the reactions of nitrilase, EC 3.5.5.1, and arylacetonitrilase, EC 3.5.5.5, substrate specificity and enantioselectivity, overview. Steric hindrance with amino acid residue Tyr54 impairs the binding or conversion of sterically demanding substrates, homology modelling
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: dinitriles
Products: -
Products: -
-
additional information
?
-
Pseudomonas fluorescens DSM 7155
-
Substrates: preferred substrates: dinitriles
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme catalyzes the reactions of nitrilase, EC 3.5.5.1, and arylacetonitrilase, EC 3.5.5.5, substrate specificity and enantioselectivity, overview. Steric hindrance with amino acid residue Tyr54 impairs the binding or conversion of sterically demanding substrates, homology modelling
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the reactions of nitrilase, EC 3.5.5.1, and arylacetonitrilase, EC 3.5.5.5, substrate specificity and enantioselectivity, overview. Steric hindrance with amino acid residue Tyr54 impairs the binding or conversion of sterically demanding substrates, homology modelling
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: dinitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: no activity with isopentanenitrile, adiponitrile, 2-chloro-3-cyanopyridine, and mandelonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: arylacetonitrile
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, enzyme catalyzes a range of 2-pyridones with rates of 1-118% relative to ricinine, overview
Products: -
Products: -
?
additional information
?
-
Substrates: preferred substrates: aliphatic dinitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: no activity with molononitrile
Products: -
Products: -
?
additional information
?
-
Pyrococcus sp. MC-FB
-
Substrates: the enzyme preferentially hydrolyzes aromatic nitriles. No activity with: cyclohexanecarbonitrile, malononitrile, butyronitrile, (R,S)-mandelonitrile, 2-phenylglycinonitrile, 2-nitrobenzonitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
Rhodococcus erythropolis ZJB-0910
-
Substrates: preferred substrate: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not hydrolyzed dichlobenil (2,6-dichlorobenzonitrile)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the wild type enzyme containing Arg129 is active only for meta- and para-substituted benzonitriles with a methyl or amino group, but shows no activity for ortho-substituted benzonitriles
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrate: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrate: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrates: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrate: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme does not hydrolyzed dichlobenil (2,6-dichlorobenzonitrile)
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrates: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: preferred substrate: aliphatic and aromatic nitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: substrate specificity profile, enzyme also catalyzes the synthesis of a range of alpha-hydroxy carboxylic acids or amides from aldehydes in presence of cyanide
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not hydrolyzed dichlobenil (2,6-dichlorobenzonitrile)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the reactions of nitrilase, EC 3.5.5.1, and arylacetonitrilase, EC 3.5.5.5, substrate specificity and enantioselectivity, overview. Steric hindrance with amino acid residue Tyr54 impairs the binding or conversion of sterically demanding substrates, homology modelling
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not hydrolyzed dichlobenil (2,6-dichlorobenzonitrile)
Products: -
Products: -
?
additional information
?
-
Rhodococcus sp. (in: high G+C Gram-positive bacteria) Novo SP361
-
Substrates: substrate specificity profile, enzyme also catalyzes the synthesis of a range of alpha-hydroxy carboxylic acids or amides from aldehydes in presence of cyanide
Products: -
Products: -
?
additional information
?
-
Rhodococcus sp. NDB1165
-
Substrates: preferred substrate: aromatic nitriles, unsaturated aliphatic nitrile
Products: -
Products: -
-
additional information
?
-
-
Substrates: recombinant NIT4 isozymes NIT4A, NIT4B1, and NIT4B2 do not hydrolyze 3-cyano-L-alanine, benzonitrile, 4-hydroxybenzonitrile, butyronitrile, and 4-pentenenitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferred substrate: aliphatic mono- and dinitriles
Products: -
Products: -
-
additional information
?
-
-
Substrates: does not convert 2-phenylbutyronitrile
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the reactions of nitrilase, EC 3.5.5.1, and arylacetonitrilase, EC 3.5.5.5, substrate specificity and enantioselectivity, overview. Steric hindrance with amino acid residue Tyr54 impairs the binding or conversion of sterically demanding substrates, homology modelling
Products: -
Products: -
?
additional information
?
-
E1A0Z9
Substrates: Nit1 substrate specificity, overview. Significant activities are observed with the aromatic substrates 3-phenylpropionitrile and cinnamonitrile. To a minor degree, the heterocyclic 3-cyanopyridine is also accepted as substrate. In contrast to aliphatic dinitriles, the aliphatic mononitriles acetonitrile, propionitrile, and butyronitrile are almost not converted by Nit1, no activity on malononitrile
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with mandelonitrile, arylacetonitrile and benzonitrile. No activity with acetamide and benzamide
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dichlorophenyl acetonitrile + 2 H2O
2,4-dichlorophenyl acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-amino-4-methylbenzonitrile + 2 H2O
2-amino-4-methylbenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-amino-5-chloro-benzonitrile + 2 H2O
2-amino-5-chloro-benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-aminobenzonitrile + 2 H2O
2-aminobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3,4,5-trimethoxybenzonitrile + 2 H2O
3,4,5-trimethoxybenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-furonitrile + 2 H2O
furan 3-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4,5-dimethoxybenzonitrile + 2 H2O
4,5-dimethoxybenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-bromobenzonitrile + 2 H2O
4-bromobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + 2 H2O
4-chlorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-fluorobenzonitrile + 2 H2O
4-fluorobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-methoxy-2-nitrobenzonitrile + 2 H2O
4-methoxy-2-nitrobenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzonitrile + 2 H2O
4-methoxybenzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
bromoxynil + H2O
?
-
Substrates: enzyme utilizes the herbicide substrate as nitrogen source
Products: -
Products: -
?
indole acetonitrile + 2 H2O
indole acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
Substrates: isozymes are involved in indole-3-acetic acid production
Products: -
Products: -
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
Substrates: -
Products: -
Products: -
?
succinonitrile + 2 H2O
succinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-amino-6-chloro-benzonitrile + 2 H2O
2-amino-6-chloro-benzoic acid + NH3
-
Substrates: good substrate, when the cells are induced by benzonitrile
Products: -
Products: -
?
2-amino-6-chloro-benzonitrile + 2 H2O
2-amino-6-chloro-benzoic acid + NH3
-
Substrates: good substrate, when the cells are induced by benzonitrile
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
2-methyl-2-phenylpropionitrile + 2 H2O
2-methyl-2-phenylpropionic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + 2 H2O
3-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
3-chlorobenzonitrile + 2 H2O
3-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: 100% activity, the enzyme is highly specific towards heterocyclic nitriles such as 3- and 4-cyanopyridine
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: 100% activity, the enzyme is highly specific towards heterocyclic nitriles such as 3- and 4-cyanopyridine
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: lower activity for the purified enzyme compared to the activity in resting cells
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
nicotinic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + 2 H2O
pyridine 3-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + 2 H2O
4-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
4-chlorobenzonitrile + 2 H2O
4-chlorobenzoate + NH3
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
-
Substrates: 69.25% activity compared to 3-cyanopyridine, the enzyme is highly specific towards heterocyclic nitriles such as 3- and 4-cyanopyridine
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
-
Substrates: 69.25% activity compared to 3-cyanopyridine, the enzyme is highly specific towards heterocyclic nitriles such as 3- and 4-cyanopyridine
Products: -
Products: -
?
4-cyanopyridine + 2 H2O
pyridine 4-carboxylic acid + NH3
Substrates: -
Products: -
Products: -
?
acetonitrile + 2 H2O
acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
acrylonitrile + 2 H2O
acrylic acid + NH3
-
Substrates: preferred substrate, acrylonitrile is also a good inducer of enzyme production
Products: -
Products: -
?
acrylonitrile + 2 H2O
acrylic acid + NH3
-
Substrates: preferred substrate, acrylonitrile is also a good inducer of enzyme production
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
Substrates: -
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: best substrate, no formation of amide
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: best substrate, no formation of amide
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: only hydrolysed after recovered activity by preincubation with benzonitrile or dialysis against buffer containing 50%, v/v, glycerol and 10% saturated ammonium sulfate
Products: -
Products: -
?
acrylonitrile + H2O
acrylic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoate + NH3
Substrates: preferred substrate
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoate + NH3
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: preferred substrate, when the cells are induced by benzonitrile
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: preferred substrate, when the cells are induced by benzonitrile
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
Substrates: low activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: only traces of activity
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: specific for nitrile groups directly attached to the benzene ring
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: best substrate
Products: -
Products: -
?
benzonitrile + 2 H2O
benzoic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indol-3-acetonitrile + H2O
indol-3-acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indol-3-acetonitrile + H2O
indol-3-acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
indol-3-acetonitrile + H2O
indol-3-acetic acid + NH3
-
Substrates: -
Products: -
Products: -
?
valeronitrile + 2 H2O
valeric acid + NH3
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyzes aliphatic, heterocyclic and aromatic nitriles with different substitutions, and is efficient in conversion of both aliphatic and aromatic nitriles. Substrate specificity in vivo is dependent on the inducer component, overview
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme NIT2 might be involved in supplying indole-3-acetic acid during seed development rather than during stratification
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme NIT2 might be involved in supplying indole-3-acetic acid during seed development rather than during stratification
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme NIT2 might be involved in supplying indole-3-acetic acid during seed development rather than during stratification
Products: -
Products: -
?
additional information
?
-
-
Substrates: isozyme NIT2 might be involved in supplying indole-3-acetic acid during seed development rather than during stratification
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cr3+
Fe2+
Mg2+
Mn2+
Ca2+
at concentrations of CaCl2 of 1.0-5.0%, the activity of nitrilase decreases sharply, higher concentration of CaCl 2 seem to have a poisoning effect on the cells
Co2+
5 mM, stimulates wild-type nitrilase 4.8fold and the mutant enzyme F168V/T201N/S192F/M191T/F192S 3.3fold
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-propanol
-
5% (v/v), about 40% loss of activity, 50% (v/v), about 95% loss of activity
acetonitrile
-
5% (v/v), about 50% loss of activity, 50% (v/v), about 95% loss of activity
benzaldehyde
-
nearly complete inhibition at 10 mM
benzyl bromide
-
strong inhibition at 10 mM
phenylacetonitrile
-
50% inhibition at 10 mM
phenylmethanesulfonyl fluoride
inhibits amide conversion more than 94% and completely suppresses nitrile hydrolysis
phenylmethylsulfonyl fluoride
-
40% inhibition at 1 mM
4-hydroxymercuribenzoic acid
-
complete inhibition at 0.1 mM, reversal by GSH
5,5'-dithiobis(2-nitrobenzoic acid)
-
complete loss of activity due to modification of Cys165
5,5'-dithiobis(2-nitrobenzoic acid)
-
complete inhibition at 1 mM
Ag+
-
strong inhibition of nitrilase activity. The effect on KCN (0.02 mmol/l) degradation is tested in the presence of Cu2+ and Ag+ ions (0.025 mmol/l to 1.0 mmol/l) and the enzymatic activity is not affected significantly at 0.025 mmol/l, 0.075 mmol/l, and 0.125 mmol/l concentrations. When both ions are combined, the activity of the enzyme decreases significantly
Benzamide
-
competitive inhibition of benzonitrile hydrolysis, Ki: 16.6 mM
Cu2+
-
benzonitrilase A: 30% inhibition at 0.1 mM, benzonitrilase B: 83% inhibition at 0.1 mM
Cu2+
-
strong inhibition of nitrilase activity. The effect on KCN (0.02 mmol/l) degradation is tested in the presence of Cu2+ and Ag+ ions (0.025 mmol/l to 1.0 mmol/l) and the enzymatic activity is not affected significantly at 0.025 mmol/l, 0.075 mmol/l, and 0.125 mmol/l concentrations. When both ions are combined, the activity of the enzyme decreases significantly
ethanol
-
a relative activity of 49% is detected in 5% (v/v) of ethanol
Hg2+
-
complete inhibition at 0.25 mM, also inhibition of enzyme association to decamers
Hg2+
-
nearly complete inactivation at 1 mM
methanol
-
the enzyme is relatively active in 5% (v/v) methanol with 60% of the enzyme activity remaining
NaCl
the enzyme loses more than 75% of its activity at NaCl concentrations higher than 2.0 mol/l
Propanol
-
a relative activity of 6% is detected in 5% (v/v) of propanol
Toluene
-
5% (v/v), about 65% loss of activity, 50% (v/v), about 85% loss of activity
additional information
-
not inhibited by L-glutathione, L-cysteine, dithiothreitol, and 8-hydroxyquinoline
-
additional information
the enzyme retains near maximal activity even in the presence of high concentrations of ZnCl2, MgSO4 and MnSO4
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
activates wild-type nitrilase and mutant enzyme F168V/T201N/S192F/M191T/F192S
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Colonic Neoplasms
Downregulation of NIT2 inhibits colon cancer cell proliferation and induces cell cycle arrest through the caspase-3 and PARP pathways.
Infections
Alternative transcription initiation of the nitrilase gene (BrNIT2) caused by infection with Plasmodiophora brassicae Woron. in Chinese cabbage (Brassica rapa L.).
Infections
Expression and localization of nitrilase during symptom development of the clubroot disease in Arabidopsis.
Infections
Proteomics and functional analyses of Arabidopsis nitrilases involved in the defense response to microbial pathogens.
Neoplasms
Downregulation of NIT2 inhibits colon cancer cell proliferation and induces cell cycle arrest through the caspase-3 and PARP pathways.
Rubella
Substrate specificity of plant nitrilase complexes is affected by their helical twist.
Starvation
A role for nitrilase 3 in the regulation of root morphology in sulphur-starving Arabidopsis thaliana.
Tuberculosis
Glutamine amidotransferase activity of NAD+ synthetase from Mycobacterium tuberculosis depends on an amino-terminal nitrilase domain.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.8
(R,S)-2-hydroxy-2-phenylacetonitrile
pH 8.0, 40°C, recombinant enzyme
0.23
3-Phenylpropionitrile
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
2.426
4-methylbenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.34
4-phenylbutyronitrile
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
0.0000000097
Cinnamonitrile
pH 7.4, 70°C, mutant enzyme K96R
0.35
heptanenitrile
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
0.88
(methylthio)acetonitrile
pH 8.0, 30°C, isozyme NIT1
1.09
(methylthio)acetonitrile
pH 8.0, 30°C, isozyme NIT2
1.31
(methylthio)acetonitrile
pH 8.0, 30°C, isozyme NIT3
280
1-cyanocyclohexaneacetonitrile
40°C, pH 7.0, enzyme ecapsulated in ethyleneamine-mediated biosilica
0.13
3-(4-chlorophenyl)pentanedinitrile
mutant F202V, sodium phosphate buffer, pH 7.0, 30°C
0.25
3-(4-chlorophenyl)pentanedinitrile
wild-type enzyme, sodium phosphate buffer, pH 7.0, 30°C
0.31
3-(4-chlorophenyl)pentanedinitrile
mutant P194A/F202V, sodium phosphate buffer, pH 7.0, 30°C
0.38
3-(4-chlorophenyl)pentanedinitrile
mutant P194A, sodium phosphate buffer, pH 7.0, 30°C
0.44
3-(4-chlorophenyl)pentanedinitrile
mutant P194A/I201A/F202V, sodium phosphate buffer, pH 7.0, 30°C
0.456
3-aminobenzonitrile
-
mutant enzyme R129K, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.483
3-aminobenzonitrile
-
mutant enzyme R129H, in 50 mM potassium phosphate (pH 7.5), at 25°C
1.863
3-aminobenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.000000103
3-anilinoproprionitrile
pH 7.4, 70°C, mutant enzyme K96R
0.000000157
3-anilinoproprionitrile
pH 7.4, 70°C, wild-type enzyme
0.55
3-methylbenzonitrile
-
mutant enzyme R129K, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.592
3-methylbenzonitrile
-
mutant enzyme R129H, in 50 mM potassium phosphate (pH 7.5), at 25°C
1.851
3-methylbenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
1.699
4-aminobenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
2.49
allyl cyanide
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
1.068
Benzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
1.468
Benzonitrile
-
mutant enzyme R129K, in 50 mM potassium phosphate (pH 7.5), at 25°C
3.13
Benzonitrile
-
mutant enzyme R129H, in 50 mM potassium phosphate (pH 7.5), at 25°C
536.2
iminodiacetonitrile
35°C, pH 7.5, mutant enzyme F168V/T201N/S192F/M191T/F192S
2.12
indole-3-acetonitrile
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
7.4
indole-3-acetonitrile
pH 8.0, 30°C, isozyme NIT2
11.1
indole-3-acetonitrile
pH 8.0, 30°C, isozyme NIT1
30.1
indole-3-acetonitrile
pH 8.0, 30°C, isozyme NIT3
8.34
mandelonitrile
-
recombinant enzyme in cross-linked enzyme aggregates
0.14
phenylacetonitrile
pH 8.0, 30°C, isozyme NIT1
0.23
phenylacetonitrile
pH 8.0, 30°C, isozyme NIT3
0.07
phenylbutyronitrile
pH 8.0, 30°C, isozyme NIT3
0.08
phenylbutyronitrile
pH 8.0, 30°C, isozyme NIT1
0.09
phenylbutyronitrile
pH 8.0, 30°C, isozyme NIT2
0.000000009
phenylglycinenitrile
pH 7.4, 70°C, mutant enzyme K96R
0.000000024
phenylglycinenitrile
pH 7.4, 70°C, wild-type enzyme
0.043
phenylpropionitrile
-
pH and temperature not specified in the publication
0.22
phenylpropionitrile
pH 8.0, 30°C, isozyme NIT1
0.42
phenylpropionitrile
pH 8.0, 30°C, isozyme NIT3
0.43
phenylpropionitrile
pH 8.0, 30°C, isozyme NIT2
0.0000000005
trichloroacetonitrile
pH 7.4, 70°C, wild-type enzyme
0.00000013
trichloroacetonitrile
pH 7.4, 70°C, mutant enzyme K96R
additional information
additional information
kinetic and chiral analysis, overview
-
additional information
additional information
-
kinetic and chiral analysis, overview
-
additional information
additional information
-
kinetic and chiral analysis, overview
-
additional information
additional information
-
kinetic and chiral analysis, overview
-
additional information
additional information
-
kinetic and chiral analysis, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
79.7
3-Phenylpropionitrile
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
0.000283
4-aminobenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.000695
4-methylbenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
15.8
4-phenylbutyronitrile
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
19.8
allyl cyanide
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
40.8
heptanenitrile
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
0.37
3-(4-chlorophenyl)pentanedinitrile
mutant P194A, sodium phosphate buffer, pH 7.0, 30°C
0.43
3-(4-chlorophenyl)pentanedinitrile
wild-type enzyme, sodium phosphate buffer, pH 7.0, 30°C
0.7
3-(4-chlorophenyl)pentanedinitrile
mutant F202V, sodium phosphate buffer, pH 7.0, 30°C
3.48
3-(4-chlorophenyl)pentanedinitrile
mutant P194A/F202V, sodium phosphate buffer, pH 7.0, 30°C
0.00014
3-aminobenzonitrile
-
mutant enzyme R129K, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.00015
3-aminobenzonitrile
-
mutant enzyme R129H, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.000288
3-aminobenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.18
3-anilinoproprionitrile
pH 7.4, 70°C, mutant enzyme K96R
0.28
3-anilinoproprionitrile
pH 7.4, 70°C, wild-type enzyme
0.000158
3-methylbenzonitrile
-
mutant enzyme R129K, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.00018
3-methylbenzonitrile
-
mutant enzyme R129H, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.000198
3-methylbenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.000129
Benzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.000162
Benzonitrile
-
mutant enzyme R129K, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.00047
Benzonitrile
-
mutant enzyme R129H, in 50 mM potassium phosphate (pH 7.5), at 25°C
9.19
iminodiacetonitrile
35°C, pH 7.5, mutant enzyme F168V/T201N/S192F/M191T/F192S
0.29
indole-3-acetonitrile
isozyme NIT-T2, in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
0.083
mandelonitrile
-
recombinant enzyme in cross-linked enzyme aggregates
0.016
phenylglycinenitrile
pH 7.4, 70°C, mutant enzyme K96R
0.225
trichloroacetonitrile
pH 7.4, 70°C, mutant enzyme K96R
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001667
4-aminobenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.002867
4-methylbenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.97
3-(4-chlorophenyl)pentanedinitrile
mutant P194A, sodium phosphate buffer, pH 7.0, 30°C
1.69
3-(4-chlorophenyl)pentanedinitrile
wild-type enzyme, sodium phosphate buffer, pH 7.0, 30°C
5.96
3-(4-chlorophenyl)pentanedinitrile
mutant F202V, sodium phosphate buffer, pH 7.0, 30°C
11.02
3-(4-chlorophenyl)pentanedinitrile
mutant P194A/F202V, sodium phosphate buffer, pH 7.0, 30°C
11.17
3-(4-chlorophenyl)pentanedinitrile
mutant P194A/I201A/F202V, sodium phosphate buffer, pH 7.0, 30°C
0.001548
3-aminobenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.00308
3-aminobenzonitrile
-
mutant enzyme R129K, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.0032
3-aminobenzonitrile
-
mutant enzyme R129H, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.001068
3-methylbenzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.0029
3-methylbenzonitrile
-
mutant enzyme R129K, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.003
3-methylbenzonitrile
-
mutant enzyme R129H, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.0011
Benzonitrile
-
mutant enzyme R129K, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.001223
Benzonitrile
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.0015
Benzonitrile
-
mutant enzyme R129H, in 50 mM potassium phosphate (pH 7.5), at 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
0.14
mutant enzyme A198V/I290F/H135Y/Y213H/T350S/Y177C/A285T, using (R)-2-chloromandelonitrile as substrate, in 50 mM potassium phosphate buffer, at pH 7.5 and 30°C
0.24
recombinant enzyme expressed without GroEL/ES, pH 8.0, 30°C
0.28
recombinant enzyme expressed without GroEL/ES, pH 8.0, 30°C
0.4
-
enzyme in cells, substrate 2-methyl-2-phenylpropionitrile in Na/K-phosphate buffer, pH 7.0, 30°C
0.52
mutant enzyme A198V/I290F/H135Y/Y213H/T350S/Y177C/A285T, using (R)-2-chloromandelonitrile as substrate, in 50 mM potassium phosphate buffer, at pH 4.5 and 30°C
0.6
-
mutant enzyme N164A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
0.62
wild type enzyme, using (R)-2-chloromandelonitrile as substrate, in 50 mM potassium phosphate buffer, at pH 7.5 and 30°C
0.64
recombinant enzyme coexpressed with GroEL/ES, pH 8.0, 30°C
1.9
enzyme in cells, substrate 2-methyl-2-phenylpropionitrile in Na/K-phosphate buffer, pH 7.0, 30°C
10
-
mutant enzyme S188A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
10.4
-
mutant enzyme I104A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
10.7
11.6
14.1
-
enzyme in cells, substrate benzonitrile in Na/K-phosphate buffer, pH 7.0, 30°C
14.5
-
mutant enzyme R130A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
15.3
-
for benzonitrile as substrate, for benzamide as substrate very low, but significant specific acitivity
17.7
-
mutant enzyme R130A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
19
substrate mandelonitrile, purified recombinant enzyme, pH 8.0, 40°C
22.4
25.6
purified enzyme, using mandelonitrile as substrate, at 30°C and pH 8.0
26
44
enzyme activity in immobilized cells, pH and temperature not specified in the publication
5.1
-
mutant enzyme V49A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
5.2
-
mutant enzyme M114A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
7.5
-
mutant enzyme T115A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
8
-
mutant enzyme S188A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
8.2
-
mutant enzyme T115A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
8.8
9
-
mutant enzyme Q116A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
9.6
-
mutant enzyme G103A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
9.7
-
mutant enzyme N164A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
9.9
additional information
-
after 20.3fold purification, the specific activity is 144 units/mg, while the crude enzyme exhibits a specific activity of 7.1 units/mg at pH 8.0 and 45°C
0.1
the specific activity is less than 0.1 micromol/min/mg, wild type enzyme, using (R)-2-chloromandelonitrile as substrate, in 50 mM potassium phosphate buffer, at pH 4.5 and 30°C
0.1
-
enzyme in cells, substrate benzonitrile in Na/K-phosphate buffer, pH 7.0, 30°C
10.7
-
wild type enzyme, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
11.6
-
mutant enzymeV49A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
22.4
-
mutant enzyme Y142A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
26
-
mutant enzyme Y142A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
7
-
wild type enzyme, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
8.8
-
mutant enzyme G103A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
8.8
-
mutant enzyme I104A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
9.9
-
mutant enzyme M114A, using benzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
9.9
-
mutant enzyme Q116A, using 3-methylbenzonitrile as substrate, in 50 mM potassium phosphate (pH 7.5), at 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
7 - 8
7 - 9
7 - 9.5
7.5
7.6
8.5
additional information
7
soluble and enzyme ecapsulated in ethyleneamine-mediated biosilica
7
-
with substrate 2-methyl-2-phenylpropionitrile in Na/K-phosphate buffer
7
with substrate 2-methyl-2-phenylpropionitrile in Na/K-phosphate buffer
7
-
the activity in the CLEA increases with the increase in the pH of cross-linking solution and it is maximum at pH 7.0
7
-
with substrate benzonitrile in Na/K-phosphate buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
-
pH 4.0: about 40% of maximal activity, pH 11.0: about 50% of maximal activity
5 - 10
5 - 9
5.5 - 8
6 - 10
6 - 11.5
-
pH 6.0: about 55% of maximal activity, immobilized enzyme, pH 11.5: about 50% of maximal activity
6 - 7.5
Pyrococcus sp. MC-FB
-
pH 6.0: about 60% of maximal activity, pH 7.5: about 50% of maximal activity
6 - 8
6 - 9
6 - 9.5
pH 6.0: about 65% of maximal activity, pH 9.5: about 65% of maximal activity
5 - 10
-
pH 5.0: about 40% of maximal activity, pH 10.0: about 75% of maximal activity
5 - 9
pH 5.0: about 40% of maximal activity, pH 9.0: about 55% of maximal activity
6 - 10
pH 6.0: about 65% of maximal activity, pH 10.0: about 75% of maximal activity, soluble enzyme
6 - 10
pH 6.0: about 70% of maximal activity, pH 10.0: about 80% of maximal activity, enzyme ecapsulated in ethyleneamine-mediated biosilica
6 - 8
-
pH 6.0: about 70% of maximal activity, pH 8.0: about 60% of maximal activity
6 - 8
-
the enzyme retains more than 80% of its activity between pH 6.0 and pH 8.0
6 - 9
-
more than 70% of the maximum activity is retained between pH 6.0 and 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
35 - 40
40
40 - 45
45
50
55
65
40
soluble and enzyme ecapsulated in ethyleneamine-mediated biosilica
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 45
20°C: about 40% of maximal activity, 45°C: about 60% of maximal activity
20 - 50
-
the nitrilase activity gradually increases from 20°C to 45°C and is lost rapidly above 50°C
20 - 60
30 - 45
30°C: about 65% of maximal activity, 45°C: about 25% of maximal activity
30 - 50
30 - 55
30 - 60
30 - 90
-
30°C: about 60% of maximal activity, 90°C: about 50% of maximal activity
40 - 55
-
40°C: about 60% of maximal activity, 55°C: about 35% of maximal activity
5 - 40
-
nitrilase activity increases gradually from 5-40°C only, no further increase in activity is recorded above 40°C
5 - 50
-
the enzyme activity increases gradually from 5-45°C and decreases drastically at 50°C
85 - 100
Pyrococcus sp. MC-FB
-
85°C: about 45% of maximal activity, 100°C: about 50% of maximal activity
20 - 60
20°C: about 55% of maximal activity, 60°C: about 65% of maximal activity, soluble enzyme
20 - 60
20°C: about 65% of maximal activity, 60°C: about 75% of maximal activity, enzyme ecapsulated in ethyleneamine-mediated biosilica
30 - 50
30°C: about 35% of maximal activity, 50°C: about 55% of maximal activity
30 - 50
-
more than 70% activity between 30 and 50°C. A reaction temperature of 55°C leads to almost totally inactivation of the enzyme
30 - 55
-
35°C: about 40% of maximal activity, 55°C: about 40% of maximal activity, immobilized enzyme
30 - 55
-
30°C: about 50% of maximal activity, 55°C: about 50% of maximal activitysoluble enzyme
30 - 60
30°C: about 85% of maximal activity, 60°C: about 50% of maximal activity
30 - 60
-
30°C: about 60% of maximal activity, 60°C: about 60% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cereibacter sphaeroides LHS-305
-
-
-
brenda
cv. Natsumaki 13-gou kokabu, isozyme-specific genes BrNIT-T1 and BrNITT2
-
-
brenda
-
-
-
brenda
strains NCIB11215, ATCC39484, and NCIB11216
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
predominant isoform NIT2 in developing embryos
brenda
predominant isoform NIT2 in germinating seeds
brenda
additional information
-
best inducer of enzyme formation: benzonitrile
brenda
-
optimization of enzyme production, best conditions are glucose 1.0%, acrylonitrile 0.1%, pH 7.0
brenda
-
optimization of enzyme production, best conditions are glucose 1.0%, acrylonitrile 0.1%, pH 7.0
-
brenda
-
use of benzonitrile as a sole source of nitrogen and carbon
brenda
-
use of benzonitrile as a sole source of nitrogen and carbon
-
brenda
-
optimization of culture conditions for nitrilase production, overview. Fe2+ is the best metal ion, pH 7.0 and 28°Care the best conditions, phenylacetamide is the best inducer
brenda
Cereibacter sphaeroides LHS-305
-
optimization of culture conditions for nitrilase production, overview. Fe2+ is the best metal ion, pH 7.0 and 28°Care the best conditions, phenylacetamide is the best inducer
-
brenda
-
use of benzonitrile as a sole source of nitrogen and carbon
brenda
-
using bromoxynil as a sole source of nitrogen
brenda
-
use of benzonitrile as a sole source of nitrogen and carbon
brenda
-
induction of enzyme synthesis by epsilon-caprolactam- or isovaleronitrile-containing media
brenda
-
best inducer of enzyme formation: isobutyronitrile
brenda
-
high levels of aromatic nitrilase is induced after transfer of the mycelium from a rich medium into a medium with 20 mM picolinonitrile
brenda
-
high levels of aromatic nitrilase is induced after transfer of the mycelium from a rich medium into a medium with 20 mM picolinonitrile
-
brenda
-
expression of nitrilase after infection with Plasmodium brassicae during symptom development of clubroot disease
brenda
additional information
-
isoform-specific localization of transcripts of Brassica rapa nitrilase genes in clubroot tissue infected with Plasmodiophora brassicae. Isozyme BrNIT-T1 is strongly expressed in cells containing expanding secondary plasmodia of Plasmodiophora brassicae, but not in cells containing resting spores. Isozyme BrNITT2 transcripts are localized in noninfected cells rather than infected cells during the clubroot growth phase but coexist with mature resting spores at a later phase of clubroot development. In situ hybridization, overview
brenda
additional information
E1A0Z9
no growth on 4-tolunitrile or 4-hydroxybenzonitrile as sole nitrogen sources
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
Arabidopsis nit1 knockout lines display a loss in the production of deaminated glutathione with accumulation of higher levels of the glutathione breakdown products cysteinylglycine and cystathionine
metabolism
physiological function
additional information
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
B9BCZ1
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
A6T0X3
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
Methanosarcina mazei BAA-159
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
Drepanopeziza brunnea MB_m1
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
Ectopseudomonas oleovorans CECT:5344
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
metabolism
-
use of script based method for classification of aliphatic and aromatic group of nitrilases. The algorithm can be used as a tool to classify nitrilases as aliphatic and aromatic class. The overall accuracy achieved is 95.00%. These machine learning techniques can be used to predict different features of the gene/protein and selection of these algorithms for the prediction of gene/protein function
-
physiological function
the enzyme has profound effects on root morphogenesis in early seedling development
physiological function
the enzyme functions as a metabolite repair enzyme that removes deaminated glutathione from the cytoplasm and plastids
additional information
native and recombinant Escherichia coli-expressed enzymes differ in substrate specificity, acid/amide ratio, reaction optima and stability
additional information
generation of a model of the nitrilase by homology modeling, overview
additional information
-
generation of a model of the nitrilase by homology modeling, overview
additional information
-
generation of a model of the nitrilase by homology modeling, overview
additional information
-
generation of a model of the nitrilase by homology modeling, overview
additional information
-
generation of a model of the nitrilase by homology modeling, overview
additional information
close-to-atomic structure of a full-length active helical NIT using cryo-electron microscopy at a resolution of 3.4 A
additional information
-
native and recombinant Escherichia coli-expressed enzymes differ in substrate specificity, acid/amide ratio, reaction optima and stability
-
additional information
-
generation of a model of the nitrilase by homology modeling, overview
-
additional information
-
generation of a model of the nitrilase by homology modeling, overview
-
Show AA Sequence and Transmembrane Helices (1787 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
32000
340000
36700
37000
376000
38000
38500
40000
41000
410000
412000
42000
42700
x * 42700, recombinant enzyme, SDS-PAGE, x * 38500, native enzyme, SDS-PAGE, the multimeric nitrilase is composed of 12-16 subunits, mass spectrometry, analytical centrifugation, and dynamic light scattering, modelling
43000
45000
450000
46000
-
gel filtration, aggregation to 560 kDa in the presence of benzonitrile
460000
550000
560000
580000
60000
600000
620000
650000
76000
80000
38500
x * 42700, recombinant enzyme, SDS-PAGE, x * 38500, native enzyme, SDS-PAGE, the multimeric nitrilase is composed of 12-16 subunits, mass spectrometry, analytical centrifugation, and dynamic light scattering, modelling
40000
-
10 * 40000, SDS-PAGE, hydrolysis of both benzonitrile and acrylonitrile after recovery conditions for acrylonitrile hydrolysis
412000
-
sedimentation equilibrium analysis, after recovery conditions for hydrolysis of acrylonitrile
43000
wild-type enzyme and mutant enzyme F168V/T201N/S192F/M191T/F192S, SDS-PAGE
45000
-
substrate, temperature and pH dependent association of 12 subunits, 12 * 45000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
dimer
dodecamer
eicosamer
hexamer
homodecamer
homodecamer or homododecamer
homododecamer
homohexadecamer
homooctamer
homooligomer
homotetradecamer
monomer
multimer
octamer
tetradecamer
tetramer
additional information
?
x * 43000, wild-type enzyme and mutant enzyme F168V/T201N/S192F/M191T/F192S, SDS-PAGE
decamer
-
10 * 40000, SDS-PAGE, hydrolysis of both benzonitrile and acrylonitrile after recovery conditions for acrylonitrile hydrolysis
dodecamer
-
substrate, temperature and pH dependent association of 12 subunits, 12 * 45000, SDS-PAGE
homohexadecamer
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16 * 35790, calculated from amino acid sequence
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multimer
x * 42700, recombinant enzyme, SDS-PAGE, x * 38500, native enzyme, SDS-PAGE, the multimeric nitrilase is composed of 12-16 subunits, mass spectrometry, analytical centrifugation, and dynamic light scattering, modelling
multimer
-
x * 42700, recombinant enzyme, SDS-PAGE, x * 38500, native enzyme, SDS-PAGE, the multimeric nitrilase is composed of 12-16 subunits, mass spectrometry, analytical centrifugation, and dynamic light scattering, modelling
-
additional information
homology modelling and molecular dynamics, overview
additional information
-
homology modelling and molecular dynamics, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
side-chain modification
under stress conditions the enzyme undergoes spontaneous thiolation with GSSG-biotin through modification of the active-site cysteines
proteolytic modification
the mature enzyme is reduced in size by about 4 kDa compared to the unprocessed enzyme, cleavage of the C-terminal peptide
proteolytic modification
-
the mature enzyme is reduced in size by about 4 kDa compared to the unprocessed enzyme, cleavage of the C-terminal peptide
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proteolytic modification
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the recombinant enzyme undergoes posttranslational cleavage at approximately residue 327, resulting in the formation of active, helical homo-oligomers
proteolytic modification
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the recombinant enzyme undergoes posttranslational cleavage at approximately residue 327, resulting in the formation of active, helical homo-oligomers
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform Nit2, to 1.4 A resolution. Modeling of activity-based proteomics probes Leu-Arg-alpha-chloroacetamide and Leu-Glu-alpha-chloroacetamide probes into the mNit2 active site
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F168I/L201E
-
4.6fold increased specific activity compared to the wild type enzyme
F168K
F168M
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3fold increased specific activity compared to the wild type enzyme
F168T
-
1.7fold increased specific activity compared to the wild type enzyme
F168T/L201Q
-
3.1fold increased specific activity compared to the wild type enzyme
F168V
F168V/L201N
-
15.3fold increased specific activity compared to the wild type enzyme
F168V/T201N/S192F/M191T/F192S
L201A
-
1.9fold increased specific activity compared to the wild type enzyme
L201G
-
1.5fold increased specific activity compared to the wild type enzyme
L201H
-
2.7fold increased specific activity compared to the wild type enzyme
L201K
-
3.5fold increased specific activity compared to the wild type enzyme
L201N
-
5.5fold increased specific activity compared to the wild type enzyme
L201Q
-
4.9fold increased specific activity compared to the wild type enzyme
L201S
-
2.2fold increased specific activity compared to the wild type enzyme
L201T
-
2fold increased specific activity compared to the wild type enzyme
Q339K
t1/2 at 45°C is 16.4 min, compared to 12.5 min for the wild-type enzyme
Q343K
t1/2 at 45°C is 22.8 min, compared to 12.5 min for the wild-type enzyme
T201F
t1/2 at 45°C is 169 min, compared to 12.5 min for the wild-type enzyme
T201F/Q339K/Q343K
T201I
t1/2 at 45°C is 55 min, compared to 12.5 min for the wild-type enzyme
T201L
t1/2 at 45°C is 119 min, compared to 12.5 min for the wild-type enzyme
T201W
t1/2 at 45°C is 135 min, compared to 12.5 min for the wild-type enzyme
F168K
F168T
-
1.7fold increased specific activity compared to the wild type enzyme
-
F168V
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4.1fold increased specific activity compared to the wild type enzyme
-
L201N
-
5.5fold increased specific activity compared to the wild type enzyme
-
F168V/L201N/S192F
Acidovorax facilis ATCC 55746
-
mutant enzyme shows 2.4fold improvement in kcat/Km
-
F168V/T201N/S192F/M191T/F192S
Acidovorax facilis ATCC 55746
-
mutant enzyme shows 136% improvement in specific activity
-
T201F/Q339K/Q343K
Acidovorax facilis ATCC 55746
-
mutant enzyme showes about 14fold longer half-life at 45°C
-
Q339K
Acidovorax facilis ZJB09122
-
t1/2 at 45°C is 16.4 min, compared to 12.5 min for the wild-type enzyme
-
T201F
Acidovorax facilis ZJB09122
-
t1/2 at 45°C is 169 min, compared to 12.5 min for the wild-type enzyme
-
T201I
Acidovorax facilis ZJB09122
-
t1/2 at 45°C is 55 min, compared to 12.5 min for the wild-type enzyme
-
T201L
Acidovorax facilis ZJB09122
-
t1/2 at 45°C is 119 min, compared to 12.5 min for the wild-type enzyme
-
T201W
Acidovorax facilis ZJB09122
-
t1/2 at 45°C is 135 min, compared to 12.5 min for the wild-type enzyme
-
A198V
the mutant enzyme shows 2.4fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 compared to the wild type enzyme
A198V/I290F
the mutant enzyme shows 1.2fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 and 140% activity at pH 4.5 compared to the wild type enzyme
A198V/I290F/H135Y
the mutant enzyme shows 1.7fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 and 150% activity at pH 4.5 compared to the wild type enzyme
A198V/I290F/H135Y/Y213H/T350S/Y177C/A285T
the mutant enzyme shows 2.8fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 and 740% activity at pH 4.5 compared to the wild type enzyme
A198V/I290F/Y177C/A285T
the mutant enzyme shows 0.9fold conversion rate of 2-phenylpropionitrile at pH 7.5 and 240% activity at pH 4.5 compared to the wild type enzyme
A198V/I290F/Y213H/T350S
the mutant enzyme shows 2fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 and 200% activity at pH 4.5 compared to the wild type enzyme
A198V/Q197H
the mutant enzyme shows 2.9fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 compared to the wild type enzyme
A198V/Q197H/L176M
the mutant enzyme shows 6.5fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 compared to the wild type enzyme
A198V/Q197H/L176M/V306I
the mutant enzyme shows 8fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 compared to the wild type enzyme
I290F/Q3L
the mutant enzyme shows 2.3fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 and 100% activity at pH 4.5 compared to the wild type enzyme
A198V
-
the mutant enzyme shows 2.4fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 compared to the wild type enzyme
-
A198V/Q197H
-
the mutant enzyme shows 2.9fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 compared to the wild type enzyme
-
A198V/Q197H/L176M
-
the mutant enzyme shows 6.5fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 compared to the wild type enzyme
-
A198V/Q197H/L176M/V306I
-
the mutant enzyme shows 8fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 compared to the wild type enzyme
-
I290F/Q3L
-
the mutant enzyme shows 2.3fold increased conversion rate of 2-phenylpropionitrile at pH 7.5 and 100% activity at pH 4.5 compared to the wild type enzyme
-
C179A
site-directed mutagenesis, completely inactive mutant, determined with substrate indole-3-acetonitrile
C179N
site-directed mutagenesis, completely inactive mutant, determined with substrate indole-3-acetonitrile
C180A
site-directed mutagenesis, completely inactive mutant, determined with substrate indole-3-acetonitrile
C180N
site-directed mutagenesis, completely inactive mutant, determined with substrate indole-3-acetonitrile
C186A
site-directed mutagenesis, completely inactive mutant, determined with substrate indole-3-acetonitrile
C186N
site-directed mutagenesis, completely inactive mutant, determined with substrate indole-3-acetonitrile
H101Q/C239S/D246E
-
47% increased activity compared to the wild type enzyme
P172S/C236S/V291I
-
84% increased activity compared to the wild type enzyme
R95T/L169A/S224Q
the mutant has a reduced helical twist. Wild-type enzyme shows no nitrilase activity against any of the listed substrates except for beta-cyano-L-alanine. The mutant showed high activity against potassium cyanide, 2-cyanopyridine and 2-furonitrile and moderate activity against fluoroacetonitrile and 4-cyanopyridine
L223Q/H263D/Q279E
-
development of a robust nitrilase by fragment swapping and semi-rational design for efficient biosynthesis of pregabalin precursor. A chimera (BaNIT) harboring 12 amino acid substitutions is obtained using nitrilase from Arabis alpine (AaNIT) and Brassica rapa (BrNIT) as parent enzymes, which exhibits higher enantioselectivity and activity toward isobutylsuccinonitrile for the biosynthesis of pregabalin precursor. Semi-rational design is executed on BaNIT to further generate variant BaNIT/L223Q/H263D/Q279E with the concurrent improvement of activity, enantioselectivity, and solubility. The robust nitrilase displays a 5.4fold, 3.3fold, and 2.8fold increase in whole-cell activity, catalytic efficiency, and solubility, respectively
M127I/C237S
-
mutation leads to nearly 3.9fold improvement in catalytic activity
V82A/M127I/C237S
-
29.1% relative activity as compared to mutant enzyme M127I/C237S
V82C/M127I/C237S
-
122.2% relative activity as compared to mutant enzyme M127I/C237S
V82F/M127I/C237S
-
74.2% relative activity as compared to mutant enzyme M127I/C237S
V82I/M127I/C237S
-
82.9% relative activity as compared to mutant enzyme M127I/C237S
V82L/M127I/C237S
V82M/M127I/C237S
-
174.6% relative activity as compared to mutant enzyme M127I/C237S
V82Y/M127I/C237S
-
8.2% relative activity as compared to mutant enzyme M127I/C237S
E327G/Q86R/E96G/D254E/E35K/Q322R/E327G/Q86R/E6G/D254E/E327G
mutamt enzyme shows activity at pH 10. The wild-type enzyme exhibits the optimum activity at pH 8 and is not able to hydrolyze HCN at pH higher than 9. However, cyanide wastes should be maintained at alkaline pH to prevent HCN release. Therefore, the CynD from Bacillus pumilus was engineered for an increased activity under these conditions (pH 9-10), and several mutants were shown to meet this requirement
L223Q/H263D/Q279E
-
development of a robust nitrilase by fragment swapping and semi-rational design for efficient biosynthesis of pregabalin precursor. A chimera (BaNIT) harboring 12 amino acid substitutions is obtained using nitrilase from Arabis alpine (AaNIT) and Brassica rapa (BrNIT) as parent enzymes, which exhibits higher enantioselectivity and activity toward isobutylsuccinonitrile for the biosynthesis of pregabalin precursor. Semi-rational design is executed on BaNIT to further generate variant BaNIT/L223Q/H263D/Q279E with the concurrent improvement of activity, enantioselectivity, and solubility. The robust nitrilase displays a 5.4fold, 3.3fold, and 2.8fold increase in whole-cell activity, catalytic efficiency, and solubility, respectively
M127I/C237S
-
mutation leads to nearly 3.9fold improvement in catalytic activity
V82A/M127I/C237S
-
29.1% relative activity as compared to mutant enzyme M127I/C237S
V82C/M127I/C237S
-
122.2% relative activity as compared to mutant enzyme M127I/C237S
V82F/M127I/C237S
-
74.2% relative activity as compared to mutant enzyme M127I/C237S
V82I/M127I/C237S
-
82.9% relative activity as compared to mutant enzyme M127I/C237S
V82L/M127I/C237S
V82M/M127I/C237S
-
174.6% relative activity as compared to mutant enzyme M127I/C237S
V82Y/M127I/C237S
-
8.2% relative activity as compared to mutant enzyme M127I/C237S
F80H
a single amino acid residue in position 80 (H80 in isoenzyme CrNIT1 and F80 in isoenzyme CrNIT2) is identified, that when exchanged, leads to an almost complete switch in substrate preference ratio. Position 80 exerts an influence on the helical twist
H80F
a single amino acid residue in position 80 (H80 in isoenzyme CrNIT1 and F80 in isoenzyme CrNIT2) is identified, that when exchanged, leads to an almost complete switch in substrate preference ratio. Position 80 exerts an influence on the helical twist
Y54A
site-directed mutagenesis, the mutant enzyme converts 2-hydroxy-2-phenylpropionitrile with about the same activity as that of the wild-type enzyme, but forms significantly reduced amounts of amides from mandelonitrile and acetophenone cyanohydrin, it shows different kinetics of acetophenone cyanohydrin conversion and product formation compared to the wild-type
Y54F
site-directed mutagenesis, altered substrate specificity and enantioselectivity compared to the wild-type enzyme, overview
Y54M
site-directed mutagenesis, altered substrate specificity and enantioselectivity compared to the wild-type enzyme, overview
Y54P
site-directed mutagenesis, altered substrate specificity and enantioselectivity compared to the wild-type enzyme, overview
Y54V
site-directed mutagenesis, altered substrate specificity and enantioselectivity compared to the wild-type enzyme, overview
Y54A
-
site-directed mutagenesis, the mutant enzyme converts 2-hydroxy-2-phenylpropionitrile with about the same activity as that of the wild-type enzyme, but forms significantly reduced amounts of amides from mandelonitrile and acetophenone cyanohydrin, it shows different kinetics of acetophenone cyanohydrin conversion and product formation compared to the wild-type
-
Y54F
-
site-directed mutagenesis, altered substrate specificity and enantioselectivity compared to the wild-type enzyme, overview
-
Y54M
-
site-directed mutagenesis, altered substrate specificity and enantioselectivity compared to the wild-type enzyme, overview
-
Y54P
-
site-directed mutagenesis, altered substrate specificity and enantioselectivity compared to the wild-type enzyme, overview
-
Y54V
-
site-directed mutagenesis, altered substrate specificity and enantioselectivity compared to the wild-type enzyme, overview
-
C165A
C165S
G103A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
I104A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
M114A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
N164A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
Q116A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
R129A
R129H
-
the mutant enzyme is active only for meta-substituted benzonitriles
R129K
-
the mutant enzyme is active only for meta-substituted benzonitriles
R130A
-
the mutant exhibits increased specific activity with 3-methylbenzonitrile and benzonitrile compared to the wild type enzyme
S188A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
T115A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
V49A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
Y142A
Y142F
-
mutant shows slightly lower kcat/Km values compared to the wild type enzyme
Y142S
-
mutant exhibits slightly higher kcat/Km values for aromatic nitriles and shows no activity toward aliphatic nitriles
G103A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
-
I104A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
-
R129H
-
the mutant enzyme is active only for meta-substituted benzonitriles
-
R129K
-
the mutant enzyme is active only for meta-substituted benzonitriles
-
V49A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
-
K96R
F202V
the mutant enzyme shows 6.25fold improvement in activity towards 3-(4-chlorophenyl) glutaronitrile relative to that of wild-type enzyme
H141A
fold increase in activity as compared to wild-type enzyme. No tradeoff occurred in stereoselectivity
I201A
fold increase in activity as compared to wild-type enzyme. No tradeoff occurred in stereoselectivity
M197A
fold increase in activity as compared to wild-type enzyme. No tradeoff occurred in stereoselectivity
P194A
fold increase in activity as compared to wild-type enzyme. No tradeoff occurred in stereoselectivity
P194A/I201A/F202V
the mutant enzyme with a larger substrate-binding pocket displays significantly enhanced catalytic activity and enantioselectivity (S, 99% ee) toward 3-(4-chlorophenyl) glutaronitrile and other 3-substituted glutaronitriles
P202A
fold increase in activity as compared to wild-type enzyme. No tradeoff occurred in stereoselectivity
V198A
lower activity as compared to wild-type enzyme. The enantiomeric excess value of mutant enzyme V198A is 75% (S)
S190G
mutant enzyme exhibits 3fold higher specific activity toward mandelonitrile compared with that of wild-type
additional information
F168K
-
3.1fold increased specific activity compared to the wild type enzyme
F168V
-
4.1fold increased specific activity compared to the wild type enzyme
F168V/T201N/S192F/M191T/F192S
the mutant enzyme shows 136% improvement in specific activity. Vmax and kcat are enhanced 1.23fold and 1.23fold, while the Km is decreased 1.53fold
F168V/T201N/S192F/M191T/F192S
-
mutant enzyme shows 136% improvement in specific activity
T201F/Q339K/Q343K
t1/2 at 45°C is 180 min, compared to 12.5 min for the wild-type enzyme. The mutant enzyme exhibits about 14fold longer half-life at 45°C compared to the wild-type enzyme
T201F/Q339K/Q343K
-
mutant enzyme showes about 14fold longer half-life at 45°C
F168K
-
3.1fold increased specific activity compared to the wild type enzyme
-
V82L/M127I/C237S
-
the variant displays higher enantioselectivity, increased enzyme activity (5.4fold) and reduced amide formation (from 15.8% to 1.9%) compared with BaNIT
V82L/M127I/C237S
-
139.7% relative activity as compared to mutant enzyme M127I/C237S
V82L/M127I/C237S
-
the variant displays higher enantioselectivity, increased enzyme activity (5.4fold) and reduced amide formation (from 15.8% to 1.9%) compared with BaNIT
V82L/M127I/C237S
-
139.7% relative activity as compared to mutant enzyme M127I/C237S
R129A
-
the mutant exhibits no activity with 3-methylbenzonitrile and benzonitrile
Y142A
-
mutant exhibits slightly higher kcat/Km values for aromatic nitriles and shows no activity toward aliphatic nitriles
Y142A
-
the mutant exhibits decreased specific activity with 3-methylbenzonitrile and increased specific activity with benzonitrile compared to the wild type enzyme
K96R
retains the ability to hydrolyse amides but hydrolyses nitriles more efficiently than the wild-type enzyme
K96R
-
retains the ability to hydrolyse amides but hydrolyses nitriles more efficiently than the wild-type enzyme
-
additional information
immobilization and stabilization of Escherichia coli cells in 8.0% polyvinyl alcohol and 1.0% sodium alginate copolymer recombinantly expressing the Acidovorax facilis nitrilase for stable production of iminoacetic acid, method optimization, overview. Maximum relative nitrilase activity with 1.0% CaCl2, and 5.0% wet cells, with 1.0% iminodiacetonitrile in distilled water at 40°C. Substrate specificity of immobilized and free cells, overview. Ca2+ can stabilize the cells, but is toxic at concentrations above 1% leading to a sharp decrease in nitrilase activity of immobilized cells. Immobilized and free cells display different sensitivity towards temperatures ranging from 25°C to 70°C, with optimal tempartures of 40°C and 45°C, respectively. Comparison of operational and storage stability of free and immobilized cells, overview
additional information
-
immobilization and stabilization of Escherichia coli cells in 8.0% polyvinyl alcohol and 1.0% sodium alginate copolymer recombinantly expressing the Acidovorax facilis nitrilase for stable production of iminoacetic acid, method optimization, overview. Maximum relative nitrilase activity with 1.0% CaCl2, and 5.0% wet cells, with 1.0% iminodiacetonitrile in distilled water at 40°C. Substrate specificity of immobilized and free cells, overview. Ca2+ can stabilize the cells, but is toxic at concentrations above 1% leading to a sharp decrease in nitrilase activity of immobilized cells. Immobilized and free cells display different sensitivity towards temperatures ranging from 25°C to 70°C, with optimal tempartures of 40°C and 45°C, respectively. Comparison of operational and storage stability of free and immobilized cells, overview
additional information
Helical twist and substrate size correlate and when binding pocket residues are exchanged between two nitrilases that show the same twist but different specificities, their specificities change
additional information
Helical twist and substrate size correlate and when binding pocket residues are exchanged between two nitrilases that show the same twist but different specificities, their specificities change
additional information
-
Helical twist and substrate size correlate and when binding pocket residues are exchanged between two nitrilases that show the same twist but different specificities, their specificities change
additional information
-
Nit1-deficient T-lymphocytes of knock-out mice can undergo apoptosis induced by DNA damage due to irradiation and chemical treatment. Apoptosis induced by Fas or Ca2+ signals appears to be compromised. Nit1 deficiency results in T-lymphocyte hyperproliferative responses induced by T-lymphocyte receptor stimulation. The expressions of T-lymphocyte activation markers are elevated in Nit1-/- T-lymphocytes. There is a spontaneous cell cycle entry and enhanced cell cycle progression in Nit1-/- T-lymphocytes
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11.5
purified recombinant enzyme, room temperature, 2 h, no activity remaining
4 - 7.5
the wild type enzyme shows no activity after 30 min incubation at pH 4.5, about 10% activity after 30 min incubation at pH 5.0, about 20% activity after 30 min incubation at pH 5.5, about 60% activity after 30 min incubation at pH 6.0, and 100% activity after 30 min incubation at pH 6.5-7.5
5 - 11
-
the enzyme shows 5%, 39% and 29% of the maximum activity at pH 5, 6 and 10, respectively, and it is nearly inactive at pH 11
5.5
purified recombinant enzyme, room temperature, 2 h, 60% activity remaining
5.5 - 10
-
a sharp activity decrease is observed at slightly acidic pH values, only a trace activity being observed at pH 5.5, 70% and 17% of the activity being retained at pH 9 and 10, respectively
6
purified recombinant enzyme, room temperature, 2 h, 80% activity remaining
6 - 7
-
relative enzyme activity is retained at pH 6.0 and 7.0 after incubating for 12 h at 4°C
6.5 - 11
purified recombinant enzyme, room temperature, 2 h, 90-100% activity remaining
6.5 - 8.7
recombinant enzyme in cell-free extract, room temperature, 2 h, 70% activity remaining at pH 6.5 and pH 8.7, profile overview
9.5
additional information
7
purified recombinant enzyme, room temperature, 2 h, completely stable
9.5
and above, purified recombinant enzyme, room temperature, 2 h, no activity remaining
additional information
sharp drop in activity between pH 11.0 and pH 11.5, profile overview
additional information
-
sharp drop in activity between pH 11.0 and pH 11.5, profile overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-70
-
after five freeze-thaw cycles and subsequent storage for 5 days at -70°C, the activity of the enzyme decreases to about one-fifth of the original activity
20 - 60
the yield of product decreases sharply after the enzyme is heat-treated at 40°C for 30 min and 1 h. The enzyme completely loses its activity after heat-treatment at 60°C for 30 min. However, this enzyme is relatively stable from 20 to 30°C
25 - 35
recombinant enzyme in cell-free extract, pH 8.0, 1 h, stable
30
30 - 50
30 - 55
-
stable at 30°C, highly active at 48°C (with 92% of maximum activity), but its activity declines sharply at higher temperatures (to 53% and 19% at 50°C and 55°C, respectively), at 30°C and pH 7.2-9.0 the enzyme half-life is about 11 h, at 35°C and 40°C, the half-life decreases to 6.2 h and 2.8 h, respectively
35
35 - 55
-
the nitrilase half-life is 277 min and 10.5 h at 35°C and 45°C, respectively, the enzyme is active at up to 50°C, the enzyme shows only traces of activity at 55°C
4
-
activity of cross-linked enzyme aggregate preparation remains stable up to 75 h at 4°C while the free enzyme loses 90% activity at this temperature in 75 h
40
45
50
55
60
70
30 - 50
-
soluble recombinant nitrilase has a half-life of 1732.5 min at 30°C and 128.3 min at 50°C
30 - 50
the enzyme is quite stable at 30°C, with half-life of 63 h, the enzyme is labile at higher temperatures as revealed by half-lives of 35 h and 22 h at 40°C and 50°C, respectively
30 - 50
-
the half-lives of alginate-immobilized cells at 30, 40 and 50°C are 315, 117.5 and 10.9 h, respectively
35
half-life of mutant enzyme F168V/T201N/S192F/M191T/F192S: 17.39 h. Half-life of wild-type enzyme 14.51 h
35
-
constant activity for 30 min, after partial purification stable for 10 h
40
-
irreversible inactivation by preincubation above
40
recombinant enzyme in cell-free extract, pH 8.0, 1 h, 20% activity remaining
45
wild-type nitrilase and mutant enzyme F168V/T201N/S192F/M191T/F192S are not thermally stable at temperatures higher than 45°C
45
purified recombinant enzyme, pH 8.0, 1 h, 90% activity remaining
45
-
the enzyme activity decreases up to 5 h at 45°c with no further detectable enzyme activity
45
-
incubation at 45°C does not affect the activity of nitrilase enzyme. A gradual decrease in benzonitrile hydrolyzing activity is observed up to 4 h of pre-incubation at 45°C followed by no detectable enzyme activity
50
purified recombinant enzyme, pH 8.0, 1 h, 50% activity remaining
50
E1A0Z9
purified recombinant His-tagged Nit1, 30 min, loss of 50% activity
50
1 min, about 25% loss of activity. 60 min, about 85% loss of activity
55
and above, purified recombinant enzyme, pH 8.0, 1 h, no activity remaining
55
and above, recombinant enzyme in cell-free extract, pH 8.0, 1 h, no activity remaining
60
2 h, soluble enzyme loses 82.5% of its activity. The enzyme ecapsulated in ethyleneamine-mediated biosilica retains 77.7% of its initial activity
60
E1A0Z9
purified recombinant His-tagged Nit1, 10 in, complete inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
efficient biocatalyst recycling is achieved as a result of immobilization with immobilized cells exhibiting 88% conversion even after 20 batch recycles
-
for immobilization of cells with nitrilase activity a variety of sol-gel silica hybrids are tested for entrapment and adsorption of bacterial cells as well as chemical binding on polysulphone membranes. Activation of the matrix surface with formaldehyde leads to an increase in immobilization efficiency and operational stability of the biocatalyst. Among the supports screened, membranes give the best result for enzyme activity and especially operational stability, with retention of 100% activity after eight reaction cycles
-
high recycling efficiency of enzyme ecapsulated in ethyleneamine-mediated biosilica. The residual activity of the enzyme ecapsulated in ethyleneamine-mediated biosilica retains 94.2% of its initial activity after 16 cycles of reaction. Even after 20 cycles, its residual activity keeps approximately 77.1% of its initial activity
maximal nitrilase activity of alginate-immobilized cells is obtained under conditions of 2% (w/v) alginate, 0.6% (w/v) CaCl2, 0.4 g cell/g alginate, and 1.8 mm bead size
-
more resistant to thermal inactivation if cells immobilized in calcium alginate beads, stabilizing effect of 3-cyanopyridine
-
nitrilase aggregates are prepared using ammonium sulfate (35%) precipitation followed by cross-linking with glutaraldehyde (125 mM) which renders 70% activity retention
-
the enzyme ecapsulated in ethyleneamine-mediated biosilica has significantly improved temperature tolerance
the enzyme stability is markedly improved in the presence of D-sorbitol and xylitol (20% w/v), or myo-inositol (10% w/v)
-
the nitrilase activity in cross-linked enzyme aggregates is at 30°C and 60°C about 5times more stable than in soluble preparations
-
the purified native and recombinant enzyme are stabilized by glycine at 1% w/v, sucrose at 10% w/v, D-glucose at 10% w/v, trehalose at 10% w/v, D-sorbitol at 10% w/v, xylitol at 10% w/v, D-myo-inositol at 10%, D-glycerol at 10% w/v, and bovine serum albumin at 0.1-1.0% w/v, in different extents, overview
the recombinant nitrilase (from Escherichia coli strain JM109/pNLE) is quite stable, the residual activity after 10 cycles of reaction is still over 40% of the initial activity
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-propanol
-
the enzyme shows more than 30% of the control activity with 5% 2-propanol
Acetone
acetonitrile
dichloromethane
-
the enzyme shows more than 30% of the control activity with 5% dichloromethane
dimethyl acetamide
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced at 5%
dimethyl formamide
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-25%
dimethyl sulfoxide
dimethylsulfoxide
-
the enzyme shows more than 30% of the control activity with 5-10% of dimethylsulfoxide
dioxane
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-10%
DMSO
Ethanol
Ethyl acetate
-
the enzyme shows more than 30% of the control activity with 5% ethyl acetate
isopropanol
Methanol
n-heptane
n-hexane
n-propanol
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-15%
toluene
xylene
additional information
Acetone
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-15%
Acetone
-
the enzyme shows more than 30% of the control activity with 5% acetone
acetonitrile
-
the enzyme shows more than 30% of the control activity with 5% acetonitrile
dimethyl sulfoxide
-
signifantly enhances the synthetic potential of the enzyme as well as its enantioselectivity. Extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 525%
dimethyl sulfoxide
-
signifantly enhances the synthetic potential of the enzyme as well as its enantioselectivity. Extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 525%
-
Ethanol
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-20%
Ethanol
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-20%
-
isopropanol
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-15%
isopropanol
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-15%
-
Methanol
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-20%
Methanol
-
extent of nitrile hydrolysis and enantiomeric purity of product are significantly enhanced in the range of 5-20%
-
Methanol
-
the enzyme shows more than 30% of the control activity with 5-10% of methanol
n-heptane
-
more than half of activity is preserved at up to 50% of n-heptane
toluene
-
the enzyme shows more than 30% of the control activity with 5-10% of toluene
toluene
-
the enzyme shows more than 30% of the control activity with 5-10% of toluene
-
xylene
-
more than half of activity is preserved at up to 15% of xylene, the enzyme shows more than 30% of the control activity with 5-10% of xylene
xylene
-
more than half of activity is preserved at up to 15% of xylene, the enzyme shows more than 30% of the control activity with 5-10% of xylene
-
additional information
-
addition of organic solvent up to 10%-20% leads to an enhancement in reaction rate, any further increase beyond the critical concentration in the latter leads to the decrease in catalytic efficiency of the enzyme. The solvent dielectric constant shows a linear correlation with the critical concentration of the solvent used and the extent of nitrile hydrolysis. Unlike alcohols, the reaction rate in case of aprotic solvents can be linearly correlated to solvent log P. The affinity of the enzyme for its substrate is highly dependent upon the aprotic solvent used
additional information
-
addition of organic solvent up to 10%-20% leads to an enhancement in reaction rate, any further increase beyond the critical concentration in the latter leads to the decrease in catalytic efficiency of the enzyme. The solvent dielectric constant shows a linear correlation with the critical concentration of the solvent used and the extent of nitrile hydrolysis. Unlike alcohols, the reaction rate in case of aprotic solvents can be linearly correlated to solvent log P. The affinity of the enzyme for its substrate is highly dependent upon the aprotic solvent used
-
additional information
-
when 20% (v/v) of organic solvent is used, the enzyme activity sharply decreases and only can be detected with very low activity except that in methanol and 2-chloromethane (40% and 10% of activity retaining, respectively)
additional information
-
when 20% (v/v) of organic solvent is used, the enzyme activity sharply decreases and only can be detected with very low activity except that in methanol and 2-chloromethane (40% and 10% of activity retaining, respectively)
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, in presence of 2% (w/v) sucrose as a stabilizer, 2 months, 8% loss of activity
-
-80°C, 0.1 M potassium phosphate, pH 7.0, 5 mM EDTA, stored as packed cells, no loss of activity
-
-80°C, in presence of 2% (w/v) sucrose as a stabilizer, 2 months, no significant loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, butyl-Sepharose column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
-
ammonium sulfate precipitation, Hi-Prep Sephacryl S-200 gel filtration, and Hi-Prep 16/10 Q-Sepharose column chromatography
-
Hi-Prep 16/10 Phenyl FF column chromatography, Q Sepharose column chromatography, Sephacryl S-200 gel filtration, and Superdex 200 gel filtration
-
Hiprep 16/10 Q XL column chromatography and Sephacryl S-300 gel filtration
ion exchange and hydrophobic and hydrophobic interaction chromatography
Ni-NTA column chromatography
Ni-Sepharose Fast Flow column chromatography and Sephadex G-15 gel filtration
partial
phenyl Sepharose column chromatography, Sephacryl S-200 gel filtration, and Q-Sepharose column chromatography
-
Q-Sepharose column chromatography and Sephacryl S-400 gel filtration
-
recombinant enzyme
recombinant enzyme 2fold from Escherichia coli strain BL21-Gold(DE3)/pOK101/pTf16, further purification of the refolded recombinant enzyme after 1 month storage by gel filtration
recombinant enzyme 4fold from Escherichia coli strain BL21-Gold (DE3), co-purifiication with GroEL
recombinant enzyme 9fold from Escherichia coli strain BL21-Gold (DE3) co-purifiication with GroEL, the two proteins are further separated by gel filtration
recombinant His-tagged Nit1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
E1A0Z9
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)/pSH by nickel affinity chromatography
to homogeneity, 2step ammonium phosphate precipitation, calcium phosphate gel
-
to homogeneity, chromatography techniques
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a recombinant Escherichia coli BL21(DE3)/pET28a-cyc705 was constructed to achieve the heterologous expression of cyc705
cloned into expression vector pET-28a and expressed in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3) under the control of T7 lac promoter using pET-28a to give pET-Nit, lactose is best as inducer in different media, method optimization
DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli strain BL21-Gold(DE3)/pOK101/pTf16, no cleavage of the C-terminal peptide of the enzyme in the recombinant bacteria
DNA and amino acid sequence determination, genes of the 3 isozymes are clustered on chromosome 3
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli Rosetta-gami (DE3) cells
expressed in Escherichia coli strains BL21 (DE3), BRLplys (DE3), Rosetta (DE3), and Tuner (DE3)
-
expressed, identified and displayed on the surface of Bacillus subtilis spores by using the spore coat protein G of Bacillus subtilis as an anchoring motif
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21(DE3)/pET28a-cyc705 with a recombinant plasmid pET28a-cyc705
-
expression in Escherichia coli strain BL21-Gold (DE3), co-expression of GroEL/ES
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)/pSH
expression of the recombinant protein with His6-tag in Escherichia coli strain BL21
expression under the control of a rhamnose-inducible promoter in Escherichia coli strain JM109
gene nit1, DNA and amino acid sequence determination and analysis, expression of His-tagged Nit1 in Escherichia coli strain BL21(DE3)
E1A0Z9
Pichia pastoris is a good heterologous host for the production of a nitrilase whole cell catalyst. The optimized Pichia pastoris strain, compared with the Escherichia coli nitrilase whole cell catalyst, shows greatly improved levels of reusability and thermostability while has a similar high substrate tolerance
expression under the control of a rhamnose-inducible promoter in Escherichia coli strain JM109
-
expression under the control of a rhamnose-inducible promoter in Escherichia coli strain JM109
expression under the control of a rhamnose-inducible promoter in Escherichia coli strain JM109
-
expression under the control of a rhamnose-inducible promoter in Escherichia coli strain JM109
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of Co2+, Mn2+ and Cu2+ to the grwoth medium of Pseudomonas aeruginosa RZ44 inhibits cell growth and enzyme production
downregulation in cell culture by addition of 3-cyanopyridine, nicotinic acid, urea, phenylacetic acid, phenylacetonitrile, benzoic acid, acrylic acid, and slightly by nicotinamide
inducible by 2-cyanopyridine
inducible by 3-cyanopyridine
inducible by acrylonitrile and benzonitrile
inducible by benzonitrile
inducible by isovaleronitrile
inducible by n-butyronitrile
inducible by propionitrile
inducible epsilon-caprolactam
induction by epsilon-caprolactam, 3-cyanopyridine, acrylonitrile, and benzonitrile
nitrilase production increases in the pH range 5.0 to 7.0 and then starts decreasing. Addition of Mg2+, Fe2+ and Na+ to the grwoth medium of Pseudomonas aeruginosa RZ44 supports the biomass and nitrilase production
upregulation in cell culture by addition of acetonitrile, phenylacetamide, and benzonitrile
addition of Co2+, Mn2+ and Cu2+ to the grwoth medium of Pseudomonas aeruginosa RZ44 inhibits cell growth and enzyme production
-
addition of Co2+, Mn2+ and Cu2+ to the grwoth medium of Pseudomonas aeruginosa RZ44 inhibits cell growth and enzyme production
-
-
downregulation in cell culture by addition of 3-cyanopyridine, nicotinic acid, urea, phenylacetic acid, phenylacetonitrile, benzoic acid, acrylic acid, and slightly by nicotinamide
-
downregulation in cell culture by addition of 3-cyanopyridine, nicotinic acid, urea, phenylacetic acid, phenylacetonitrile, benzoic acid, acrylic acid, and slightly by nicotinamide
Cereibacter sphaeroides LHS-305
-
-
induction by epsilon-caprolactam, 3-cyanopyridine, acrylonitrile, and benzonitrile
-
induction by epsilon-caprolactam, 3-cyanopyridine, acrylonitrile, and benzonitrile
-
-
nitrilase production increases in the pH range 5.0 to 7.0 and then starts decreasing. Addition of Mg2+, Fe2+ and Na+ to the grwoth medium of Pseudomonas aeruginosa RZ44 supports the biomass and nitrilase production
-
nitrilase production increases in the pH range 5.0 to 7.0 and then starts decreasing. Addition of Mg2+, Fe2+ and Na+ to the grwoth medium of Pseudomonas aeruginosa RZ44 supports the biomass and nitrilase production
-
-
upregulation in cell culture by addition of acetonitrile, phenylacetamide, and benzonitrile
-
upregulation in cell culture by addition of acetonitrile, phenylacetamide, and benzonitrile
Cereibacter sphaeroides LHS-305
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme is fully denatured in 6 M guanidine-HCl and 2 M Tris-carboxyethylphosphine and refolded in vitro
release from insoluble inclusion bodies after treatment with Triton X-114
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
pharmacology
synthesis
industry
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
industry
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
industry
the purified enzyme reveales its selectivity towards dinitriles, which suggests a possible industrial application in the synthesis of cyanocarboxylic acids
industry
-
the high-level production of Arthrobacter aurescens CYC705 nitrilase will meet the need of industrial biosynthesis of iminodiacetic acid
industry
spore surface display of nitrilases is an effective approach for enzyme immobilization in biochemical engineering on an industrial scale
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases in the near future
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
Halomonas sp. IIIMB2797
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
Rhodococcus sp. NDB1165
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases in the near future
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases in the near future
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases in the near future
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
-
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
-
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
the high-level production of Arthrobacter aurescens CYC705 nitrilase will meet the need of industrial biosynthesis of iminodiacetic acid
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
Roseibium aggregatum DSM 13394
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
Acidovorax facilis ATCC 55746
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
Paenarthrobacter nitroguajacolicus ZJUTB06-99
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
Bacillus subtilis ZJB-063
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
Pseudomonas aeruginosa 10145
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
Pseudomonas fluorescens DSM 7155
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
industry
Rhodococcus erythropolis ZJB-0910
-
nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases
-
pharmacology
1-cyanocyclohexaneacetic acid is a critical intermediate for the synthesis of the antiepileptic agent gabapentin. A manufacturing route is established for 1-cyanocyclohexaneacetic acid through bioconversion catalyzed by an nitrilase whole cell catalyst. Pichia pastoris is a good heterologous host for the production of a nitrilase whole cell catalyst. The optimized Pichia pastoris strain, compared with the Escherichia coli nitrilase whole cell catalyst, shows greatly improved levels of reusability and thermostability while has a similar high substrate tolerance
pharmacology
Acidovorax facilis ZJB09122
-
1-cyanocyclohexaneacetic acid is a critical intermediate for the synthesis of the antiepileptic agent gabapentin. A manufacturing route is established for 1-cyanocyclohexaneacetic acid through bioconversion catalyzed by an nitrilase whole cell catalyst. Pichia pastoris is a good heterologous host for the production of a nitrilase whole cell catalyst. The optimized Pichia pastoris strain, compared with the Escherichia coli nitrilase whole cell catalyst, shows greatly improved levels of reusability and thermostability while has a similar high substrate tolerance
-
synthesis
nitrilase products are intermediates in the synthesis of nylon
synthesis
-
preparing carboxylic acids from readily available nitrile analogues
synthesis
-
enzyme can be used as a biocatalyst for the synthesis of a range of alpha-hydroxy carboxylic acids or amides from aldehydes in presence of cyanide, halting of the reaction at the amide intermediate by use of specific inhibitors is possible
synthesis
-
biotransformation of trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile to trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylic acid with isolated enzyme, immobilized enzyme and with recombinant cells containing AtNIT1
synthesis
-
biotransformation of trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile to trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylic acid with isolated enzyme, immobilized enzyme and with recombinant cells containing AtNIT1
synthesis
-
biotransformation of benzonitrile to benzoic acid. The effect of whole cell immobilisation on the biotransformation of benzonitrile and the use of direct electric current for enhanced product removal
synthesis
-
production of (R)-mandelic acid from racemic mandelonitrile using free and immobilized cells of Pseudomonas putida
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
synthesis
-
synthesis of (R)-mandelic acid from (R,S)-mandelonitrile by use of Escherichia coli overexpressing the enzyme in a bioreactor. After a single batch reaction, (R)-mandelic acid can be obtained with 87% yield and 99.99% enantiomeric excess
synthesis
-
synthesis of beta-hydroxy carboxylic acids with high yield and optical purity by reudction of aromatic beta-ketonitriles with recombinant carbonyl reductase and nitrilase-catalyzed hydrolysis
synthesis
-
nitrilases are useful biocatalysts for the hydrolysis of nitriles in a mild and environmentally friendly manner assuring a clean process and specificity with high yield
synthesis
recombinant cells expressing the enzyme are promising catalysts for the synthesis of stable chiral quaternary carbon centers from ketones
synthesis
-
recombinant cells expressing the enzyme are promising catalysts for the synthesis of stable chiral quaternary carbon centers from ketones
synthesis
-
recombinant cells expressing the enzyme are promising catalysts for the synthesis of stable chiral quaternary carbon centers from ketones
synthesis
-
recombinant cells expressing the enzyme are promising catalysts for the synthesis of stable chiral quaternary carbon centers from ketones
synthesis
the enzyme is useful fpr synthesis of iminodiacetic acid, which is widely used as an intermediate in the manufacture of chelating agents, glyphosate herbicides and surfactants
synthesis
the purified enzyme reveales its selectivity towards dinitriles, which suggests a possible industrial application in the synthesis of cyanocarboxylic acids
synthesis
-
the broad range of substrate specificity, the high activity towards aliphatic, aromatic, and arylacetonitriles, and the highly stability, in terms of temperature, pH, and metal ions make the enzyme a promising biocatalyst for mild nitrile hydrolysis
synthesis
-
Pseudomonas aeruginosa RZ44 has the potential to be applied in the biotransformation of nitrile compounds
synthesis
-
a cascade reaction for the synthesis of optically pure (S)-beta-phenylalanine from benzoylacetonitrile was developed by coupling HpN with an omega-transaminase from Polaromonas sp. JS666 in toluene-water biphasic reaction system using beta-alanine as an amino donor. Various (S)-beta-amino acids can be produced from benzoylacetonitrile derivatives with moderate to high conversions (73-99%) and excellent enantioselectivity (above 99% enantiomeric exess). Great potential of this cascade reaction for the practical synthesis of (S)-beta-phenylalanine
synthesis
-
the strain mut-D3, with higher toxic substrate tolerance and enhanced robustness to extraneous factors is obtained via several rounds of screening. The free or immobilized catalysts of mut-D3 could serve as a good choice for nicotinic acid production from 3-cyanopyridine
synthesis
-
the high-level production of Arthrobacter aurescens CYC705 nitrilase will meet the need of industrial biosynthesis of iminodiacetic acid
synthesis
mutant nitrilase F168V/T201N/S192F/M191T/F192S is promising in applications for the upscale production of iminodiacetic acid
synthesis
Nitrilase-catalyzed regioselective hydrolysis of 1-cyanocyclohexaneacetonitrile is a green and efficient approach for the preparation of 1-cyanocyclohexaneacetic acid, a key precursor for the synthesis of gabapentin. The enzyme ecapsulated in ethyleneamine-mediated biosilica an be used as a biocatalyst for the development of an efficient biotransformation process for the synthesis of 1-cyanocyclohexaneacetic acid
synthesis
the use of mutant enzyme P194A/I201A/F202V is feasible for application in the production of (S)-3-(4-chlorophenyl)-4-cyanobutanoic acid en route to (R)-baclofen
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
-
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
-
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
-
synthesis
-
synthesis of beta-hydroxy carboxylic acids with high yield and optical purity by reudction of aromatic beta-ketonitriles with recombinant carbonyl reductase and nitrilase-catalyzed hydrolysis
-
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
-
synthesis
-
attractive as green, mild, and selective catalysts for setting stereogenic centers in fine-chemical synthesis and enantiospecific synthesis of a variety of carboxylic acid derivatives
-
synthesis
-
recombinant cells expressing the enzyme are promising catalysts for the synthesis of stable chiral quaternary carbon centers from ketones
-
synthesis
Rhodococcus sp. (in: high G+C Gram-positive bacteria) Novo SP361
-
enzyme can be used as a biocatalyst for the synthesis of a range of alpha-hydroxy carboxylic acids or amides from aldehydes in presence of cyanide, halting of the reaction at the amide intermediate by use of specific inhibitors is possible
-
synthesis
-
recombinant cells expressing the enzyme are promising catalysts for the synthesis of stable chiral quaternary carbon centers from ketones
-
synthesis
Cereibacter sphaeroides LHS-305
-
nitrilases are useful biocatalysts for the hydrolysis of nitriles in a mild and environmentally friendly manner assuring a clean process and specificity with high yield
-
synthesis
-
a cascade reaction for the synthesis of optically pure (S)-beta-phenylalanine from benzoylacetonitrile was developed by coupling HpN with an omega-transaminase from Polaromonas sp. JS666 in toluene-water biphasic reaction system using beta-alanine as an amino donor. Various (S)-beta-amino acids can be produced from benzoylacetonitrile derivatives with moderate to high conversions (73-99%) and excellent enantioselectivity (above 99% enantiomeric exess). Great potential of this cascade reaction for the practical synthesis of (S)-beta-phenylalanine
-
synthesis
-
the high-level production of Arthrobacter aurescens CYC705 nitrilase will meet the need of industrial biosynthesis of iminodiacetic acid
-
synthesis
-
the broad range of substrate specificity, the high activity towards aliphatic, aromatic, and arylacetonitriles, and the highly stability, in terms of temperature, pH, and metal ions make the enzyme a promising biocatalyst for mild nitrile hydrolysis
-
synthesis
-
Pseudomonas aeruginosa RZ44 has the potential to be applied in the biotransformation of nitrile compounds
-
EXTERNAL LINKS (specific for EC-Number 3.5.5.1)
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Release 2026.1 (March 2026)
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