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Information on EC 3.5.5.5 - Arylacetonitrilase
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3.5.5.5 ArylacetonitrilaseIUBMB Comments
Requires thiol compounds. Also hydrolyses other 4-substituted phenylacetonitriles, thien-2-ylacetonitrile, tolylacetonitriles, and, more slowly, benzyl cyanide.
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Word Map
- 3.5.5.5
- mandelonitrile
- fluorescens
- amide
-
mandelic
-
enantioselectivity
- cyanide
- arylacetonitriles
-
racemic
- alcaligenes
- phenylacetonitrile
-
enantiomeric
-
biocatalyst
-
r,s-mandelonitrile
- faecalis
-
enantiospecificity
- esculenta
-
arylacetic
-
mining
-
manihot
- benzaldehyde
- rhodochrous
-
s-hydroxynitrile
-
r--mandelic
-
nitrilase-mediated
-
r-enantiomer
-
dinitriles
-
plant-derived
-
biocatalytic
- synthesis
-
rhodococcus
- cassava
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
Arylacetonitrilase, arylacetonitrile-hydrolyzing nitrilase, arylacetonitrile-specific nitrilase, blr3397, enantioselective arylacetonitrilase, GPnor51, NIT, NitA, NitP, nitrilase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Arylacetonitrilase
arylacetonitrile-hydrolyzing nitrilase
arylacetonitrile-specific nitrilase
blr3397
enantioselective arylacetonitrilase
GPnor51
NIT
NitA
nitrilase
Nitrilase, arylaceto-
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate + NH3
-
-
-
-
4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate + NH3
reaction mechanism, overview
-
4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate + NH3
reaction mechanism, overview
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of nitriles
hydrolysis of nitriles
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
Arylacetonitrile aminohydrolase
Requires thiol compounds. Also hydrolyses other 4-substituted phenylacetonitriles, thien-2-ylacetonitrile, tolylacetonitriles, and, more slowly, benzyl cyanide.
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CAS REGISTRY NUMBER
COMMENTARY
132053-06-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2-bromophenyl)(hydroxy)acetonitrile + H2O
(2R)-(2-bromophenyl)(hydroxy)acetic acid + NH3
-
74% activity compared to phenylacetonitrile
-
-
?
(2-fluorophenyl)(hydroxy)acetonitrile + H2O
(2R)-(2-fluorophenyl)(hydroxy)acetic acid + NH3
-
439% activity compared to phenylacetonitrile
-
-
?
(3-bromophenyl)(hydroxy)acetonitrile + H2O
(2R)-(3-bromophenyl)(hydroxy)acetic acid + NH3
-
706% activity compared to phenylacetonitrile
-
-
?
(3-chlorophenyl)(hydroxy)acetonitrile + H2O
(2R)-(3-chlorophenyl)(hydroxy)acetic acid + NH3
-
810% activity compared to phenylacetonitrile
-
-
?
(3-fluorophenyl)(hydroxy)acetonitrile + H2O
(2R)-(3-fluorophenyl)(hydroxy)acetic acid + NH3
-
454% activity compared to phenylacetonitrile
-
-
?
(4-bromophenyl)(hydroxy)acetonitrile + H2O
(2R)-(4-bromophenyl)(hydroxy)acetic acid + NH3
-
680% activity compared to phenylacetonitrile
-
-
?
(4-chlorophenyl)(hydroxy)acetonitrile + H2O
(2R)-(4-chlorophenyl)(hydroxy)acetic acid + NH3
-
1083% activity compared to phenylacetonitrile
-
-
?
(4-fluorophenyl)(hydroxy)acetonitrile + H2O
(2R)-(4-fluorophenyl)(hydroxy)acetic acid + NH3
-
891% activity compared to phenylacetonitrile
-
-
?
1,2-phenylenediacetonitrile + H2O
1,2-phenylenediacetic acid + NH3
-
1.87% activity compared to phenylacetonitrile
-
-
?
1,4-dicyanobutane + H2O
adipic acid + NH3
-
47% activity compared to phenylacetonitrile
-
-
?
1-cyclohexenylacetonitrile + H2O
1-cyclohexenylacetate + NH3
-
at 3.3% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
2,4-dichlorobenzylcyanide + H2O
2,4-dichlorophenylacetic acid + NH3
-
at 6.5% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
2-acetyloxy-2-methylphenylacetonitrile + 2 H2O
2-acetyloxy-2-methylphenylacetic acid + NH3
2-acetyloxy-2-methylphenylacetonitrile + H2O
2-acetyloxy-2-methylphenylacetic acid + NH3
-
-
-
-
?
2-chlorobenzylcyanide + H2O
2-chlorophenylacetic acid + NH3
-
at 6% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
2-chloromandelonitrile + H2O
(R)-2-chloromandelic acid + H2O
-
33.75% activity compared to phenylacetonitrile
enantioselectivity ee 98.2%
-
?
2-chlorophenyl acetonitrile + H2O
2-chlorobenzoic acid + NH3
-
76.1% of the activity with mandelonitrile
-
-
ir
2-cyanopyridine + H2O
?
-
101% activity compared to phenylacetonitrile
-
-
?
2-hydroxy-2-phenylpropionitrile + H2O
2-hydroxy-2-phenylpropionic acid + 2-hydroxy-2-phenylpropionamide + NH3
-
i.e. acetophenone cyanohydrin
product ratio of about 3.4:1 for 2-hydroxy-2-phenylpropionic acid and 2-hydroxy-2-phenylpropionamide
-
?
2-hydroxy-3-butenenitrile + H2O
2-hydroxy-3-butenoic acid + NH3
-
-
-
-
?
2-methoxybenzylcyanide + H2O
2-methoxyphenylacetic acid + NH3
-
at 2% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
2-methoxyphenyl acetonitrile + H2O
2-methoxybenzoic acid + NH3
-
44.5% of the activity with mandelonitrile
-
-
ir
2-methyl-2-phenylpropionitrile + H2O
2-methyl-2-phenylpropionic acid + NH3
-
-
-
-
?
2-methylglutaronitrile + H2O
2-methylglutaric acid + NH3
-
0.12% activity compared to phenylacetonitrile
-
-
?
2-methylglutaronitrile + H2O
? + NH3
-
63% activity compared to phenylacetonitrile
-
-
?
2-phenylbutyronitrile + H2O
2-phenylbutyric acid + NH3
-
0.2% activity compared to phenylacetonitrile
-
-
?
2-phenylglycinonitrile + H2O
2-phenylalanine + NH3
-
80% of the activity with mandelonitrile. 35% enantiomeric excess for S-configuration in acid formation, 10.26% of product is amide with 92% enantiomeric excess for S-configuration
-
-
?
2-phenylglycinonitrile + H2O
2-phenylglycine + NH3
-
3% activity compared to phenylacetonitrile
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionate + NH3
-
low activity, 2% activity compared to phenylacetonitrile
-
?
2-phenylvaleronitrile + H2O
2-phenylvaleric acid + NH3
-
700% of the activity with mandelonitrile
-
-
?
2-thiophene acetonitrile + H2O
thiophene-2-carboxylic acid + NH3
-
137% of the activity with mandelonitrile
-
-
ir
2-trimethylsilyloxy-2-phenylacetonitrile + H2O
2-trimethylsilyloxy-2-phenylacetic acid + NH3
-
4% activity compared to phenylacetonitrile
-
-
?
3,4-(methylenedioxy)phenylacetonitrile + H2O
3,4-(methylendioxy)phenylacetic acid + NH3
-
at 65% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
3,4-dichlorobenzylcyanide + H2O
3,4-dichlorophenylacetic acid + NH3
-
at 14% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
3-aminopropionitrile + H2O
3-aminopropanoic acid + NH3
-
7% activity compared to phenylacetonitrile
-
-
?
3-chlorobenzylcyanide + H2O
3-chlorophenylacetic acid + NH3
-
at 43% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
3-cyanopyridine + H2O
?
-
43.2% activity compared to phenylacetonitrile
-
-
?
3-hydroxyglutaronitrile + H2O
3-hydroxyglutaric acid + NH3
-
0.12% activity compared to phenylacetonitrile
-
-
?
3-hydroxyphenylpropionitrile + H2O
3-hydroxyphenylpropionic acid + NH3
-
0.12% activity compared to phenylacetonitrile
-
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropionic acid + NH3
-
0.07% activity compared to phenylacetonitrile
-
-
?
3-indolylacetonitrile + H2O
3-indolylacetic acid + NH3
-
2% activity compared to phenylacetonitrile
-
-
?
3-methoxyphenylacetonitrile + 2 H2O
3-methoxyphenylacetic acid + NH3
-
-
-
-
?
4-aminophenyl acetonitrile + H2O
4-aminobenzoic acid + NH3
-
502.3% of the activity with mandelonitrile
-
-
ir
4-chlorobutyronitrile + H2O
4-chlorobutyric acid + NH3
-
0.06% activity compared to phenylacetonitrile
-
-
?
4-chlorophenyl acetonitrile + H2O
4-chlorobenzoic acid + NH3
-
360.3% of the activity with mandelonitrile
-
-
ir
4-cyanopyridine + H2O
4-pyridinecarboxylic acid + NH3
-
512% of the rate with benzonitrile, cell extract
-
-
?
4-cyanopyridine + H2O
?
-
142% activity compared to phenylacetonitrile
-
-
?
4-hydroxy benzonitrile + H2O
4-hydroxybenzoate + NH3
-
23.1% of the activity with mandelonitrile
-
-
ir
4-hydroxybenzylcyanide + H2O
4-hydroxyphenylacetic acid + NH3
-
at 29% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
4-hydroxycinnamonitrile + H2O
4-hydroxycinnamic acid + NH3
-
431% activity compared to phenylacetonitrile
-
-
?
4-hydroxyphenyl acetonitrile + H2O
4-hydroxybenzoic acid + NH3
-
435% of the activity with mandelonitrile
-
-
ir
4-hydroxyphenylacetonitrile + H2O
4-hydroxyphenylacetate + NH3
-
best substrate
-
-
?
4-methoxybenzylcyanide + H2O
4-methoxyphenylacetic acid + NH3
-
at 62% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
4-methoxyphenylacetonitrile + 2 H2O
4-methoxyphenylacetic acid + NH3
-
-
-
-
?
4-methoxyphenylacetonitrile + H2O
4-methoxyphenylacetate + NH3
-
81% of the activity with 4-hydroxyphenylacetonitrile
-
-
?
4-phenylbutyronitrile + H2O
4-phenylbutyrate + NH3
-
86% activity compared to phenylacetonitrile
-
-
?
adiponitrile + H2O
adipic acid + NH3
-
17.2% of the activity with mandelonitrile
-
-
ir
allyl cyanide + NH3
3-butenoic acid + NH3
-
11% activity compared to phenylacetonitrile
-
-
?
alpha-methylphenylacetonitrile + H2O
alpha-methylphenylacetic acid + NH3
-
0.14% activity compared to phenylacetonitrile
-
-
?
Arylacetonitrile + H2O
?
-
pathway in nitrile catabolism, inducible enzyme
-
-
-
benzonitrile + H2O
crotonic acid + NH3
-
1% activity compared to phenylacetonitrile
-
-
?
cinnamonitrile + H2O
cinnamic acid + NH3
-
0.07% activity compared to phenylacetonitrile
-
-
?
crotononitrile + H2O
crotonic acid + NH3
-
4% activity compared to phenylacetonitrile
-
-
?
cyclohexane carbonitrile + H2O
cyclohexlycarboxylic acid + NH3
-
12.5% of the activity with mandelonitrile
-
-
ir
dodecanenitrile + H2O
dodecanoic acid + NH3
-
0.04% activity compared to phenylacetonitrile
-
-
?
glycolonitrile + H2O
glycolic acid + NH3
-
0.08% activity compared to phenylacetonitrile
-
-
?
heptanenitrile + H2O
heptanoic acid + NH3
-
107% activity compared to phenylacetonitrile
-
-
?
hex-5-enenitrile + H2O
hex-5-enoic acid + NH3
-
7.9% of the activity with mandelonitrile
-
-
ir
hexanenitrile + H2O
hexanoic acid + NH3
-
60% activity compared to phenylacetonitrile
-
-
?
hydroxy(2-methoxyphenyl)acetonitrile + H2O
(2R)-hydroxy(2-methoxyphenyl)acetic acid + NH3
-
178% activity compared to phenylacetonitrile
-
-
?
hydroxy(2-methylphenyl)acetonitrile + H2O
(2R)-hydroxy(2-methylphenyl)acetic acid + NH3
-
194% activity compared to phenylacetonitrile
-
-
?
hydroxy(phenyl)acetonitrile + H2O
(2R)-hydroxy(phenyl)acetic acid + NH3
-
404% activity compared to phenylacetonitrile
-
-
?
indole 3-acetonitrile + H2O
(indol-3-yl)acetic acid + NH3
-
319.9% of the activity with mandelonitrile
-
-
ir
isovaleronitrile + H2O
isovaleric acid + NH3
-
11.4% of the activity with mandelonitrile
-
-
ir
m-xylenedicyanide + H2O
?
-
at 2.7% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
methylthioacetonitrile + H2O
methylthioacetic acid + NH3
-
72% activity compared to phenylacetonitrile
-
-
?
octanedinitrile + H2O
? + NH3
-
0.14% activity compared to phenylacetonitrile
-
-
?
p-tolylacetonitrile + H2O
p-tolylacetic acid + NH3
-
at 72% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
phenoxy acetonitrile + H2O
phenoxyacetate + NH3
-
232.6% of the activity with mandelonitrile
-
-
ir
phenyl acetonitrile + H2O
benzoic acid + NH3
-
342.3% of the activity with mandelonitrile
-
-
ir
phenyl glycinenitrile + H2O
phenylalanine + NH3
-
192.5% of the activity with mandelonitrile
-
-
ir
phenyl thioacetonitrile + H2O
thiophenylacetate + NH3
-
187.7% of the activity with mandelonitrile
-
-
ir
rac 2-(methoxy)-mandelonitrile + H2O
(R)-2-(methoxy)-mandelic acid + (S)-2-(methoxy)-mandelic acid + NH3
-
-
10% activity compared to phenylacetonitrile, 92% of the product is the (R)-enantiomer when the overall conversion rate is 50%, at 85% overall conversion, the level of formed (R)-enantiomer is 27%
?
succinonitrile + H2O
succinic acid + NH3
-
0.12% activity compared to phenylacetonitrile
-
-
?
(R,S)-2-phenylpropionitrile + H2O
(S)-2-phenylpropionic acid + NH3
-
-
ee 66%
-
?
(R,S)-2-phenylpropionitrile + H2O
(S)-2-phenylpropionic acid + NH3
-
-
ee 66%
-
?
(R,S)-2-phenylpropionitrile + H2O
2-phenylpropionic acid + 2-phenylpropionamide + NH3
-
-
-
-
?
(R,S)-2-phenylpropionitrile + H2O
2-phenylpropionic acid + 2-phenylpropionamide + NH3
NitP converts (R,S)-2-phenylpropionitrile to 2-phenylpropionic acid with a slight preference for the formation of the S enantiomer
-
-
?
(R,S)-2-phenylpropionitrile + H2O
2-phenylpropionic acid + NH3
-
the enzyme produces (R)-2-phenylpropionic acid with an e.e.-value of 90% at 28% conversion
-
-
?
(R,S)-2-phenylpropionitrile + H2O
2-phenylpropionic acid + NH3
-
the enzyme produces (R)-2-phenylpropionic acid with an e.e.-value of 90% at 28% conversion
-
-
?
(R,S)-2-phenylpropionitrile + H2O
2-phenylpropionic acid + NH3
the enzyme exhibits a low degree of enantioselectivity toward this substrate (e.e. 35% for the (R)-acid at 35% conversion)
-
-
?
(R,S)-2-phenylpropionitrile + H2O
2-phenylpropionic acid + NH3
the enzyme exhibits a low degree of enantioselectivity toward this substrate (e.e. 35% for the (R)-acid at 35% conversion)
-
-
?
(R,S)-mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
-
-
the enantiomeric excess against (R)-mandelic acid is over 99%
-
?
(R,S)-mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
-
-
-
-
?
(R,S)-mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
-
-
the enantiomeric excess against (R)-mandelic acid is over 99%
-
?
(R,S)-mandelonitrile + H2O
(R)-(-)mandelic acid + NH3
-
-
-
-
?
(R,S)-mandelonitrile + H2O
(R)-mandelic acid + NH3
-
-
ee 22%
-
?
(R,S)-mandelonitrile + H2O
mandelic acid + NH3
-
the enzyme produces almost no mandelamide at pH 5 (Fig. 1a), while the R-acid is formed with a high enantiomeric excess
-
-
?
(R,S)-mandelonitrile + H2O
mandelic acid + NH3
-
the enzyme produces almost no mandelamide at pH 5 (Fig. 1a), while the R-acid is formed with a high enantiomeric excess
-
-
?
(R,S)-mandelonitrile + H2O
mandelic acid + NH3
the end product of (R,S)-mandelonitrile transformation at pH 5.0 consists of 40% mandelamide (relative to the total amount of products formed). It is observed that the production of mandelamide is delayed compared to the production of mandelic acid
-
-
?
(R,S)-mandelonitrile + H2O
mandelic acid + NH3
the end product of (R,S)-mandelonitrile transformation at pH 5.0 consists of 40% mandelamide (relative to the total amount of products formed). It is observed that the production of mandelamide is delayed compared to the production of mandelic acid
-
-
?
(S)-mandelonitrile + H2O
(S)-mandelic acid + NH3
-
the product is 94% enantiomeric pure (S)-isomer, the formation of ca 50% (S)-mandeloamide is observed
-
?
(S)-mandelonitrile + H2O
(S)-mandelic acid + NH3
-
-
the product is 94% enantiomeric pure (S)-isomer, the formation of ca 50% (S)-mandeloamide is observed
-
?
(S)-mandelonitrile + H2O
(S)-mandelic acid + NH3
-
the product is 94% enantiomeric pure (S)-isomer, the formation of ca 50% (S)-mandeloamide is observed
-
?
(S)-mandelonitrile + H2O
(S)-mandelic acid + NH3
-
-
the product is 94% enantiomeric pure (S)-isomer, the formation of ca 50% (S)-mandeloamide is observed
-
?
2 (R,S)-mandelonitrile + 2 H2O
(R)-mandelic acid + (S)-mandeloamide + NH3
-
-
-
-
?
2 (R,S)-mandelonitrile + 2 H2O
(R)-mandelic acid + (S)-mandeloamide + NH3
NitP shows only weak enantioselectivity for the formation of (R)-mandelic acid from racemic mandelonitrile
the product ratio is about 4:1
-
?
2-acetyloxy-2-methylphenylacetonitrile + 2 H2O
2-acetyloxy-2-methylphenylacetic acid + NH3
-
-
-
-
?
2-acetyloxy-2-methylphenylacetonitrile + 2 H2O
2-acetyloxy-2-methylphenylacetic acid + NH3
-
-
-
-
?
2-hydroxy-2-phenylacetonitrile + 2 H2O
2-hydroxy-2-phenylacetate + NH3
i.e. (R,S)-mandelonitrile
-
-
?
2-hydroxy-2-phenylacetonitrile + 2 H2O
2-hydroxy-2-phenylacetate + NH3
i.e. (R,S)-mandelonitrile
-
-
?
2-hydroxy-2-phenylacetonitrile + 2 H2O
2-hydroxy-2-phenylacetate + NH3
-
i.e. (R,S)-mandelonitrile
-
-
?
2-hydroxy-2-phenylacetonitrile + 2 H2O
2-hydroxy-2-phenylacetate + NH3
-
i.e. (R,S)-mandelonitrile
-
-
?
2-methoxyphenylacetonitrile + 2 H2O
2-methoxyphenylacetic acid + NH3
-
-
-
-
?
2-methoxyphenylacetonitrile + 2 H2O
2-methoxyphenylacetic acid + NH3
-
-
-
-
?
2-phenylbutyronitrile + 2 H2O
2-phenylbutyric acid + NH3
-
-
-
-
?
2-phenylpropionitrile + 2 H2O
2-phenylpropionic acid + NH3
-
-
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionic acid + NH3
-
-
12.5% of the activity with mandelonitrile. 65% enantiomeric excess for S-configuration in acid formation, 0.25% of product is amide with 6% enantiomeric excess for R-configuration
-
?
2-phenylpropionitrile + H2O
2-phenylpropionic acid + NH3
-
-
(R)-2-phenylpropionic acid is preferentially formed
-
?
2-phenylpropionitrile + H2O
2-phenylpropionic acid + NH3
-
-
(R)-2-phenylpropionic acid is preferentially formed
-
?
2-thiopheneacetonitrile + H2O
2-thiopheneacetic acid + NH3
-
ir, at 90% the rate of 4-chlorobenzylcyanide hydrolysis
not via thiopheneacetamide
-
2-thiopheneacetonitrile + H2O
2-thiopheneacetic acid + NH3
-
625% of the activity with mandelonitrile, 1.5% of product is amide
-
-
?
2-thiopheneacetonitrile + H2O
2-thiopheneacetic acid + NH3
-
625% of the activity with mandelonitrile, 1.5% of product is amide
-
-
?
3-cyanopyridine + H2O
nicotinic acid + NH3
-
208% of the rate with benzonitrile, cell extract
-
-
?
3-cyanopyridine + H2O
nicotinic acid + NH3
-
208% of the rate with benzonitrile, cell extract
-
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropanoate + NH3
-
1% activity compared to phenylacetonitrile
-
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropanoate + NH3
-
1% activity compared to phenylacetonitrile
-
-
?
3-indoleacetonitrile + H2O
3-indoleacetic acid + NH3
-
at 9% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
3-indoleacetonitrile + H2O
3-indoleacetic acid + NH3
-
at 9% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
3-phenylpropionitrile + H2O
3-phenylpropionic acid + NH3
-
at 26% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
3-pyridineacetonitrile + H2O
?
-
at 77% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
3-thiopheneacetonitrile + H2O
3-thiopheneacetic acid + NH3
-
at 24% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
3-thiopheneacetonitrile + H2O
3-thiopheneacetic acid + NH3
-
107% of the activity with mandelonitrile, 1.5% of product is amide
-
-
?
3-thiopheneacetonitrile + H2O
3-thiopheneacetic acid + NH3
-
107% of the activity with mandelonitrile, 1.5% of product is amide
-
-
?
4-aminobenzylcyanide + H2O
4-aminophenylacetic acid + NH3
-
at 44% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
4-aminobenzylcyanide + H2O
4-aminophenylacetic acid + NH3
-
high activity
-
-
?
4-aminobenzylcyanide + H2O
4-aminophenylacetic acid + NH3
-
high activity
-
-
?
4-bromobenzylcyanide + H2O
?
-
at 26% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
4-bromobenzylcyanide + H2O
?
-
at 26% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
4-chlorobenzylcyanide + H2O
4-chlorophenylacetic acid + NH3
-
i.e. p-chlorophenylacetonitrile, best substrate
-
-
4-chlorobenzylcyanide + H2O
4-chlorophenylacetic acid + NH3
-
-
-
-
-
4-chlorobenzylcyanide + H2O
4-chlorophenylacetic acid + NH3
-
i.e. p-chlorophenylacetonitrile, best substrate
-
-
4-chlorobutyronitrile + H2O
4-chlorobutyrate + NH3
-
59% activity compared to phenylacetonitrile
-
-
?
4-chlorobutyronitrile + H2O
4-chlorobutyrate + NH3
-
59% activity compared to phenylacetonitrile
-
-
?
4-fluorobenzylcyanide + H2O
4-fluorophenylacetic acid + NH3
-
i.e. p-fluorophenylacetonitrile, at 96% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
4-fluorobenzylcyanide + H2O
4-fluorophenylacetic acid + NH3
-
-
-
-
-
4-fluorobenzylcyanide + H2O
4-fluorophenylacetic acid + NH3
-
i.e. p-fluorophenylacetonitrile, at 96% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
4-nitrobenzylcyanide + H2O
4-nitrophenylacetate + NH3
-
at 45% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
acrylonitrile + H2O
acrylic acid + NH3
-
121% of the rate with benzonitrile, cell extract
-
-
?
acrylonitrile + H2O
acrylic acid + NH3
-
121% of the rate with benzonitrile, cell extract
-
-
?
acrylonitrile + H2O
acrylic acid + NH3
-
0.05% activity compared to phenylacetonitrile
-
-
?
acrylonitrile + H2O
acrylic acid + NH3
-
0.05% activity compared to phenylacetonitrile
-
-
?
acrylonitrile + H2O
propenoic acid + NH3
-
at 7% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
benzonitrile + H2O
benzoic acid + NH3
-
21% activity compared to phenylacetonitrile
-
-
?
benzonitrile + H2O
benzoic acid + NH3
-
21% activity compared to phenylacetonitrile
-
-
?
benzylcyanide + H2O
phenylacetic acid + NH3
-
at 53% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
diphenylacetonitrile + H2O
diphenylacetic acid + NH3
-
-
-
?
fumaronitrile + H2O
fumaric acid + NH3
-
0.72% activity compared to phenylacetonitrile
-
-
?
fumaronitrile + H2O
fumaric acid + NH3
-
0.72% activity compared to phenylacetonitrile
-
-
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
-
0.05% activity compared to phenylacetonitrile
-
-
?
iminodiacetonitrile + 2 H2O
iminodiacetic acid + 2 NH3
-
0.05% activity compared to phenylacetonitrile
-
-
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
35% activity compared to phenylacetonitrile
-
-
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
22% of the activity with mandelonitrile, 0.1% of product is amide
-
-
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
22% of the activity with mandelonitrile, 0.1% of product is amide
-
-
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
-
-
-
?
indole-3-acetonitrile + H2O
indole-3-acetic acid + NH3
-
-
-
-
?
m-tolylacetonitrile + H2O
m-tolylacetic acid + NH3
-
at 32% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
malononitrile + H2O
malonic acid + NH3
-
3.7% activity compared to phenylacetonitrile
-
-
?
malononitrile + H2O
malonic acid + NH3
-
3.7% activity compared to phenylacetonitrile
-
-
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
-
-
99.9% enantiomeric excess for (R)-isomer
-
ir
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
racemic, enzyme hydrolizes the cyanide functionality to the corresponding carboxylic acid under ambient conditions
-
-
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
racemic, enzyme hydrolizes the cyanide functionality to the corresponding carboxylic acid under ambient conditions
-
-
?
mandelonitrile + 2 H2O
2-hydroxyphenylacetic acid + NH3
-
at 8% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
mandelonitrile + 2 H2O
mandelic acid + NH3
-
4% activity compared to phenylacetonitrile
-
-
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
4% activity compared to phenylacetonitrile
-
-
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
-
slight preference for the formation of (R)-mandelic acid
-
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
31% enantiomeric excess for R-configuration in acid formation, 19% of product is amide with 85% enantiomeric excess for S-configuration
-
-
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
31% enantiomeric excess for R-configuration in acid formation, 19% of product is amide with 85% enantiomeric excess for S-configuration
-
-
?
mandelonitrile + 2 H2O
mandelic acid + NH3
-
-
slight preference for the formation of (R)-mandelic acid
-
?
mandelonitrile + H2O
mandelic acid + NH3
-
best substrate, 164% activity compared to phenylacetonitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid + NH3
-
15% activity compared to phenylacetonitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid + NH3
-
15% activity compared to phenylacetonitrile
-
-
?
o-tolylacetonitrile + H2O
o-tolylacetic acid + NH3
-
at 4% the rate of 4-chlorobenzylcyanide hydrolysis
-
-
-
phenylacetonitrile + 2 H2O
phenylacetate + NH3
preferred substrate
-
-
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
-
-
-
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
preferred substrate
-
-
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
-
preferred substrate
-
-
?
phenylacetonitrile + H2O
phenylacetate + NH3
-
22% of the rate with benzonitrile, cell extract
-
-
?
phenylacetonitrile + H2O
phenylacetate + NH3
-
22% of the rate with benzonitrile, cell extract
-
-
?
phenylacetonitrile + H2O
phenylacetate + NH3
-
best substrate
-
?
phenylacetonitrile + H2O
phenylacetic acid + NH3
best substrate
-
-
?
phenylacetonitrile + H2O
phenylacetic acid + NH3
-
100% activity
-
-
?
phenylacetonitrile + H2O
phenylacetic acid + NH3
-
206% of the activity with mandelonitrile, 3.9% of product is amide
-
-
?
phenylpropionitrile + 2 H2O
phenylpropionate + NH3
-
-
-
?
phenylpropionitrile + H2O
phenylpropionic acid + NH3
-
-
-
-
?
phenylpropionitrile + H2O
phenylpropionic acid + NH3
-
-
-
-
?
valeronitrile + H2O
valeric acid + NH3
-
57% activity compared to phenylacetonitrile
-
-
?
valeronitrile + H2O
valeric acid + NH3
-
0.08% activity compared to phenylacetonitrile
-
-
?
valeronitrile + H2O
valeric acid + NH3
-
12.5% of the activity with mandelonitrile
-
-
?
additional information
?
-
-
very poor substrates (less than 1.5% the rate of 4-chlorobenzylcyanide hydrolysis) are 1,4-dichlorobenzylcyanide, 4-nitrobenzylcyanide, 2-pyridineacetonitrile, 2-phenylpropionitrile, 1-naphthylacetonitrile, diphenylacetonitrile, o-xylenedicyanide, acetonitrile (i.e. methylcyanide). No substrates are 2,6-dichlorobenzylcyanide, allylcyanide, propionitrile, aminoacetonitrile, iminodiacetonitrile, methacrylonitrile, crotonitrile, benzonitrile, 2- or 3-cyanopyridine, cyanopyrazine, 2-thiophenecarbonitrile or 2-furaneacrylonitrile
-
-
-
additional information
?
-
-
though the enzyme exhibits activity toward both classes of aromatic and arylacetonitriles, the nitrilase shows higher activity toward the arylacetonitriles, substrate specificity and substrate docking study, overview. No activity toward aminobutytonitrile, 2,2-dimethylcyclopropyl cyanide, and 2-amino-2,3-dimethylbutanenitrile, very low activity toward 4-aminobenzonitrile and iminodiacetonitrile, overview
-
-
-
additional information
?
-
-
very poor substrates (less than 1.5% the rate of 4-chlorobenzylcyanide hydrolysis) are 1,4-dichlorobenzylcyanide, 4-nitrobenzylcyanide, 2-pyridineacetonitrile, 2-phenylpropionitrile, 1-naphthylacetonitrile, diphenylacetonitrile, o-xylenedicyanide, acetonitrile (i.e. methylcyanide). No substrates are 2,6-dichlorobenzylcyanide, allylcyanide, propionitrile, aminoacetonitrile, iminodiacetonitrile, methacrylonitrile, crotonitrile, benzonitrile, 2- or 3-cyanopyridine, cyanopyrazine, 2-thiophenecarbonitrile or 2-furaneacrylonitrile
-
-
-
additional information
?
-
-
though the enzyme exhibits activity toward both classes of aromatic and arylacetonitriles, the nitrilase shows higher activity toward the arylacetonitriles, substrate specificity and substrate docking study, overview. No activity toward aminobutytonitrile, 2,2-dimethylcyclopropyl cyanide, and 2-amino-2,3-dimethylbutanenitrile, very low activity toward 4-aminobenzonitrile and iminodiacetonitrile, overview
-
-
-
additional information
?
-
the purified enzyme has very little activity against heterocyclic and aliphatic nitriles like 2-cyanopyridine and 4-cyanopyridine, and no activity is recorded against aromatic nitriles like benzonitrile, 4-hydroxynitrile, and tolunitrile
-
-
-
additional information
?
-
the purified enzyme has very little activity against heterocyclic and aliphatic nitriles like 2-cyanopyridine and 4-cyanopyridine, and no activity is recorded against aromatic nitriles like benzonitrile, 4-hydroxynitrile, and tolunitrile
-
-
-
additional information
?
-
-
does not use 2-(N,N-dimethylamino)-2-phenylacetonitrile, 2-phenylpropionitrile, and 2-phenylbutyronitrile as substrate
-
-
-
additional information
?
-
-
does not use 2-(N,N-dimethylamino)-2-phenylacetonitrile, 2-phenylpropionitrile, and 2-phenylbutyronitrile as substrate
-
-
-
additional information
?
-
-
enzyme converts the isomers carrying a substituent in the meta-position with higher relative activities than the corresponding para- or ortho-substituted isomers. Aliphatic substrates such as acrylonitrile and 2-hydroxy-3-butenenitrile are also hydrolysed
-
-
-
additional information
?
-
-
enzyme converts the isomers carrying a substituent in the meta-position with higher relative activities than the corresponding para- or ortho-substituted isomers. Aliphatic substrates such as acrylonitrile and 2-hydroxy-3-butenenitrile are also hydrolysed
-
-
-
additional information
?
-
-
no activity with benzonitrile, 2-cyanotoluene, 3-cyanotoluene, 3-cyanobenzothiophene, propionitrile, butyronitrile, and valeronitrile, 2-phenylbutyronitrile is a poor substrate, enzyme is enantioselective and specific for arylacetonitriles
-
?
additional information
?
-
-
enzyme acts as nitrilase and hydratase. relative amounts of amides formed from different nitriles increase with an increasing negative inductive effect of the substituent in 2-position. Acids and amides formed from chiral nitriles demonstrate mostly opposite enantiomeric excess
-
-
-
additional information
?
-
-
the nitrilase from strain EBC191 hydrolyzes a wide range of arylacetonitriles, such as 2-phenylpropionitrile (2-methylphenylacetonitrile), 2-phenylbutyronitrile, or 2-phenylvaleronitrile, and also alpha-hydroxynitriles, such as mandelonitrile, with rather high specific activities. 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
-
-
-
additional information
?
-
-
the nitrilase from strain EBC191 hydrolyzes a wide range of arylacetonitriles, such as 2-phenylpropionitrile (2-methylphenylacetonitrile), 2-phenylbutyronitrile, or 2-phenylvaleronitrile, and also alpha-hydroxynitriles, such as mandelonitrile, with rather high specific activities. 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
-
-
-
additional information
?
-
-
enzyme acts as nitrilase and hydratase. relative amounts of amides formed from different nitriles increase with an increasing negative inductive effect of the substituent in 2-position. Acids and amides formed from chiral nitriles demonstrate mostly opposite enantiomeric excess
-
-
-
additional information
?
-
-
enzyme requires an oxygen atom in para-position of the substrate. Indole-3-acetonitrile, arylcyanides, and arylpropionitriles are poor substrates
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-acetyloxy-2-methylphenylacetonitrile + 2 H2O
2-acetyloxy-2-methylphenylacetic acid + NH3
Arylacetonitrile + H2O
?
-
pathway in nitrile catabolism, inducible enzyme
-
-
-
2-acetyloxy-2-methylphenylacetonitrile + 2 H2O
2-acetyloxy-2-methylphenylacetic acid + NH3
-
-
-
-
?
2-acetyloxy-2-methylphenylacetonitrile + 2 H2O
2-acetyloxy-2-methylphenylacetic acid + NH3
-
-
-
-
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
B0LAW4
racemic, enzyme hydrolizes the cyanide functionality to the corresponding carboxylic acid under ambient conditions
-
-
?
mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
B0LAW4
racemic, enzyme hydrolizes the cyanide functionality to the corresponding carboxylic acid under ambient conditions
-
-
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
A2R6M7, A9QXE0
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
does not contain one of the following elements: Be, B, Mg, Al, Si, P, S, Cs, Ti, V, Cr, Mn, Fe, Co, Ni, Cu, Zn, Se, Sr, Zr, Mo, Pd, Ag, Cd, Sn, Sb, Ba, Ta, W, Pt, Au, Hg, Pb, La or Ce
additional information
Zn2+, Na+, and K+ show very little effect on arylacetonitrilase activity
additional information
-
enzyme does not seem to require metals for activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
little or no inhibition by Li+, Na+, Mg2+, Ca2+, Ba2+, Mn2+, Fe2+, Pb2+, Fe3+, Al3+, NaN3, NaF, cysteamine, aminoguanidine, L/D-penicillamine, 1,10-phenanthroline or EDTA
-
additional information
EDTA shows very little effect on arylacetonitrilase activity
-
additional information
-
no inhibition by KCN, EDTA, D-cycloserine, and Mn2+
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenylacetonitrile
-
absolutely required as growth nitrogen source substrate for induction of the enzyme, cannot be substituted by ammonia or epsilon-caprolactam
additional information
-
expression is induced by growing the strain in the presence of different nitriles and /or complex or inorganic nitrogen sources. The highest nitrile hydrolysing activity is observed with cells grown with 2-cyanopyridine and NaNO3
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic and chiral analysis, overview
-
11.4
2-hydroxy-2-phenylacetonitrile
pH 8.0, 30°C, recombinant enzyme; pH 8.0, 30°C, recombinant enzyme
3.4
phenylacetonitrile
pH 8.0, 30°C, recombinant enzyme; pH 8.0, 30°C, recombinant enzyme
0.8
phenylpropionitrile
pH 8.0, 30°C, recombinant enzyme; pH 8.0, 30°C, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.44
pH 8.0, in supernatant of the recombinant Escherichia coli cells, activity is highest after 6 hours of cultivation
1.26
pH 7.5, activity in enzyme preparation after purification, activity of the purified His-tagged protein was 28fold higher than the activity of the wild-type nitrilase
21.7
Effect of IPG as inducer on the growth and enzyme production by Escherichia coli in a stirred tank reactor
22.8
Effect of lactose as inducer on the growth and enzyme production by Escherichia coli in a stirred tank reactor
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
6.4 - 9.4
-
about half-maximal activity at pH 6.4 and 9.4, 2-thiopheneacetonitrile as substrate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38
40
45
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
evolution
-
the nitrilase from Neurospora crassa is related to aliphatic nitrilase, EC 3.5.5.7
evolution
-
strain ZJUTB10 nitrilase belongs to the family of arylacetonitrilases
evolution
-
strain ZJUTB10 nitrilase belongs to the family of arylacetonitrilases
-
evolution
-
the nitrilase from Neurospora crassa is related to aliphatic nitrilase, EC 3.5.5.7
-
metabolism
involved in the biosynthesis of adenosylcobalamin
metabolism
-
involved in the biosynthesis of adenosylcobalamin; involved in the biosynthesis of adenosylcobalamin; involved in the biosynthesis of adenosylcobalamin
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
NIT_ARTBC
Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
335
0
36085
Swiss-Prot
NIT_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
333
0
36804
Swiss-Prot
NIT_NECH7
Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI)
339
0
36773
Swiss-Prot
NIT_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
327
0
35582
Swiss-Prot
NIT2_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
328
0
35923
Swiss-Prot
NIT1_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
337
0
36949
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
44000
-
6 * 44000, Alcaligenes faecalis, SDS-PAGE, 6 * 47770, Alcaligenes faecalis, minimal value derived from amino acid composition
47770
-
6 * 44000, Alcaligenes faecalis, SDS-PAGE, 6 * 47770, Alcaligenes faecalis, minimal value derived from amino acid composition
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
homodecamer
homooctamer
homotetradecamer
additional information
hexamer
-
6 * 44000, Alcaligenes faecalis, SDS-PAGE, 6 * 47770, Alcaligenes faecalis, minimal value derived from amino acid composition
hexamer
-
6 * 44000, Alcaligenes faecalis, SDS-PAGE, 6 * 47770, Alcaligenes faecalis, minimal value derived from amino acid composition
-
homodecamer
-
10 * 34000, holoenzyme, light scattering analysis; 10 * 34500, subunit, SDS-PAGE
homodecamer
-
10 * 34000, holoenzyme, light scattering analysis; 10 * 34500, subunit, SDS-PAGE
-
additional information
-
homology modeling and docking, three-dimensional homology model of nitrilase, overview
additional information
-
homology modeling and docking, three-dimensional homology model of nitrilase, overview
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H165N
-
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
W163A
-
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
H165N
-
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
-
W163A
-
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
-
H170N
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
W168A
the mutant forms significantly increases amounts of mandelamide and 2-phenylpropionamide and demonstrates an almost complete inversion of enantioselectivity for the conversion of (R,S)-2-phenylpropionitrile (from R- to S-selectivity)
H170N
-
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
-
W168A
-
the mutant forms significantly increases amounts of mandelamide and 2-phenylpropionamide and demonstrates an almost complete inversion of enantioselectivity for the conversion of (R,S)-2-phenylpropionitrile (from R- to S-selectivity)
-
A165E
mutant with very low activities toward (R,S)-mandelonitrile and substrate (R,S)-2-phenylpropionitrile
A165F
the mutant enzyme converts racemic mandelonitrile and (R,S)-2-phenylpropionitrile to increased amounts of the R enantiomers of the corresponding acids
A165G
the mutant forms 4.3% amide and thus produces significantly more amide than the wild type enzyme with the substrate (R,S)-2-phenylpropionitrile
A165H
the mutant enzyme shows a significantly increased relative activity for mandelonitrile (compared to (R,S)-2-phenylpropionitrile)
A165R
mutant with very low activities toward (R,S)-mandelonitrile and substrate (R,S)-2-phenylpropionitrile
A165W
the mutant enzyme converts racemic mandelonitrile and (R,S)-2-phenylpropionitrile to increased amounts of the R enantiomers of the corresponding acids
A165Y
the mutant enzyme converts racemic mandelonitrile and (R,S)-2-phenylpropionitrile to increased amounts of the R enantiomers of the corresponding acids
C163A
-
the mutation results in significantly decreased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates. The mutant demonstrates no significant difference in the enzyme activity compared to the wild type, but shows an extremely low degree of enantioselectivity for the formation of (R)-mandelic acid
C163N
-
the mutation results in significantly increased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates
C163N/A165R
-
the mutant demonstrates increased amide formation capacity in comparison to the mutants carrying only single mutations
C163N/W110I
-
the mutant enzyme forms about 100fold more 2-phenylpropionamide (in relation to the total amount of (R,S)-2-phenylpropionitrile converted) than the wild type, although the relative activity of this mutant for the conversion (R,S)-2-phenylpropionitrile to 2-phenylpropionic acid is only 4% of that observed for the wild type
C163Q
-
the mutation results in significantly increased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates
C163S
-
the mutation results in significantly decreased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates. The mutant demonstrates no significant difference in the enzyme activity compared to the wild type, but shows an extremely low degree of enantioselectivity for the formation of (R)-mandelic acid
C164A
the mutant is devoid of nitrilase activity with the substrate (R,S)-2-phenylpropionitrile
E137A
-
the mutant demonstrates less than 1% of the wild type activity but is still enzymatically competent to convert mandelonitrile to mandelic acid and mandeloamide
Tyr54C
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Tyr54P
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Tyr54V
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Y54A
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Y54F
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Y54H
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Y54L
-
mutant with significantly reduced activity compared to the wild type enzyme
Y54M
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
E137A
-
the mutant demonstrates less than 1% of the wild type activity but is still enzymatically competent to convert mandelonitrile to mandelic acid and mandeloamide
-
Y54A
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
-
Y54F
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
-
Y54H
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
-
additional information
additional information
-
the C-terminally truncated nitrilase variants demonstrate that deletions up to about 30 amino acids do not significantly change the relevant characteristics of the enzyme, in contrast, longer C-terminal deletions of 47-67 amino acids result in significant decreases in enzyme activities and only about 10% of the activity is found compared with the wild type enzyme, deletion mutants Nit(del-C-20) and Nit(del-C-32) strongly resemble the wild type enzyme, mutants Nit(del-C-47) to Nit(del-C-67) demonstrate reduced nitrilase activities against 2-phenylpropionitrile and show a significant decreased stability of the nitrilase activity compared with the wild type enzyme, deletion mutants also show an increased formation of amide in relation to the acid formation (up to almost 10% compared to 0.2% with the wild type enzyme)
additional information
-
the C-terminally truncated nitrilase variants demonstrate that deletions up to about 30 amino acids do not significantly change the relevant characteristics of the enzyme, in contrast, longer C-terminal deletions of 47-67 amino acids result in significant decreases in enzyme activities and only about 10% of the activity is found compared with the wild type enzyme, deletion mutants Nit(del-C-20) and Nit(del-C-32) strongly resemble the wild type enzyme, mutants Nit(del-C-47) to Nit(del-C-67) demonstrate reduced nitrilase activities against 2-phenylpropionitrile and show a significant decreased stability of the nitrilase activity compared with the wild type enzyme, deletion mutants also show an increased formation of amide in relation to the acid formation (up to almost 10% compared to 0.2% with the wild type enzyme)
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
purified recombinant enzyme, room temperature, 2 h, 10% activity remaining; purified recombinant enzyme, room temperature, 2 h, 10% activity remaining
718670
6.5
purified recombinant enzyme, room temperature, 2 h, 50% activity remaining; purified recombinant enzyme, room temperature, 2 h, 50% activity remaining
718670
6.5 - 9
-
purified recombinant enzyme, room temperature, 2 h, 80-100% activity remaining
718670
7 - 10
purified recombinant enzyme, room temperature, 2 h, 90-100% activity remaining; purified recombinant enzyme, room temperature, 2 h, 90-100% activity remaining
718670
9.5
-
purified recombinant enzyme, room temperature, 2 h, 65% activity remaining
718670
10
-
purified recombinant enzyme, room temperature, 2 h, 20% activity remaining
718670
10.5
purified recombinant enzyme, room temperature, 2 h, 20% activity remaining; purified recombinant enzyme, room temperature, 2 h, 20% activity remaining
718670
11
11
purified recombinant enzyme, room temperature, 2 h, 50% activity remaining; purified recombinant enzyme, room temperature, 2 h, 50% activity remaining
718670
11
-
purified recombinant enzyme, room temperature, 2 h, 10% activity remaining
718670
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 55
exposure of the enzyme at 15, 25, and 35°C for 5 h causes 8%, 15%, and 28% decrease in arylacetonitrilase activity, respectively. A further increase in the temperature to 45 and 55°C results in 58% and 90% decrease in activity, respectively. The half-life of this enzyme at 15, 25, 35, 45, 50, and 55°C is 31 h, 16 h, 9 h, 4 h 30 min, 3 h 20 min, and 2 h 40 min, respectively
25 - 35
purified recombinant enzyme, pH 8.0, 1 h, stable; purified recombinant enzyme, pH 8.0, 1 h, stable
30
35 - 65
-
purified recombinant enzyme, labile at higher temperature, half-life of 57 min at 40°C, 42 min at 45°C, and 20 min at 55°C, respectively. The activity decreases markedly above 55°C
35
40
45
50 - 60
purified recombinant enzyme, pH 8.0, 1 h, about 10% activity remaining; purified recombinant enzyme, pH 8.0, 1 h, about 10% activity remaining
50 - 70
-
good thermal stability at 50°C, the enzyme completely loses its activity after heat-treatment at 70°C for 30 min
50
30
-
and below, 30 min, stable in 10 mM potassium phosphate buffer, pH 7.5
35
-
30 min, in 10 mM potassium phosphate buffer, pH 7.5, 25% loss of activity
40
purified recombinant enzyme, pH 8.0, 1 h, 60% activity remaining; purified recombinant enzyme, pH 8.0, 1 h, 60% activity remaining
45
purified recombinant enzyme, pH 8.0, 1 h, 20% activity remaining; purified recombinant enzyme, pH 8.0, 1 h, 20% activity remaining
45
-
and above, purified recombinant enzyme, pH 8.0, 1 h, no activity remaining
50
-
the enzyme retains 50% of its initial activity after incubation at 50°C for 30 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilisation on poly(ethyleneimine/polyaldehyde)dextran stabilizes
-
in citrate buffer, the activity of the enzyme increases with the increase in the pH (4.0-5.5), whereas in borate and carbonate buffers very little activity is observed
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimethyl sulfoxide
-
2.5 or 5%, up to 20% increase in activity, decrease above
Ethanol
-
5%, 63% enhancement in activity probably due to increased availibaility of substrate. Above 10% ethanol, significant decrease in activity
Methanol
Methanol
-
5%, 78% enhancement in activity probably due to increased availibaility of substrate. Above 10% methanol, significant decrease in activity
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
under argon stable for more than 40 h, in oxygen atmosphere 50% loss of activity after 40 h
-
718003
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 10 mM potassium phosphate buffer, pH 7, 10 mM DTT and 50% glycerol, at least 5 months
-
-20°C, pH 7.5, 14 days, 90% loss of activity, addition of 1 M ammonium sulfate almost completely stabilizes
-
-80°C, 0.01 M phosphate, pH 7.5, 1 mM dithiothreitol, 20% glycerol, stable
-
4°C, 0.01 M phosphate, pH 7.5, 1 mM dithiothreitol, rapid loss of activity, presence of 20% glycerol stabilizes
-
4°C, in 10 mM potassium phosphate buffer, pH 7, 10 mM DTT and 50% glycerol, at least 2 months, without glycerol 60% loss of activity within 1 week
-
4°C, in the presence of 60% saturated ammonium sulfate, 2 M NaCl or 30% w/v propanediol, only about 5% loss of activity within 1 week
-
5°C, in 0.02 M citrate buffer, pH 7-8, 10 days, about 50% loss of activity in 0.02 M Tris-HCl buffer, pH 9.3 within 10 days
-
8°C, pH 7.5, 14 days, 75% loss of activity, addition of 1 M ammonium sulfate almost completely stabilizes
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Sephacryl S-300 gel filtration
cells of bacteria culture are disrupted and centrifugation and the enzyme in the soluble fraction is purified using Ni-NTA affinity chromatography
DEAE Sepharose Fast Flow column chromatography and Sephacryl S-300 gel filtration
-
recombinant enzyme 2.4fold from Escherichia coli strain BL21-Gold(DE3) to near homogeneity
-
recombinant enzyme 3fold from Escherichia coli strain BL21-Gold(DE3) to near homogeneity; recombinant enzyme 3fold from Escherichia coli strain BL21-Gold(DE3) to near homogeneity
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison, cloning and expression as His-tagged protein in Escherichia coli strains JM109 and BL21(DE3)
-
expressed in Escherichia coli JM109 cells
expression in Escherichia coli JM 109, simultanuously with cassava (Manihot esculenta) oxynitrilase
-
expression in Escherichia coli strain BL21-Gold (DE3); expression in Escherichia coli strain BL21-Gold (DE3)
expression under the control of a rhamnose-inducible promoter in Escherichia coli strain JM109
-
recombinant functional expression of the enzyme in the cell envelope of Escherichia coli, where it is accessible for externally added protease
-
The nitrilase gene from Pseudomonas putida is cloned in plasmid pET 21b(+) and over-expressed as histidine-tagged protein in Escherichia coli strain BL21 (DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the nitrilase activity from Alcaligenes faecalis ECU0401 increases 4.5fold when the cells are permeabilized with 0.3% (w/v) cetyltrimethylammonium bromide for 20 min at 25°C and pH 6.5
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
synthesis
synthesis
-
recombinant cells expressing the enzyme are promising catalysts for the synthesis of stable chiral quaternary carbon centers from ketones
synthesis
-
nitrilases are important industrial enzymes that convert nitriles directly into the corresponding carboxylic acids
synthesis
-
nitrilases are important industrial enzymes that convert nitriles directly into the corresponding carboxylic acids
-
synthesis
-
recombinant cells expressing the enzyme are promising catalysts for the synthesis of stable chiral quaternary carbon centers from ketones
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mauger, J.; Nagasawa, T.; Yamada, H.
Occurrence of a novel nitrilase, arylacetonitrilase, in Alcaligenes faecalis JM3
Arch. Microbiol.
155
1-6
1990
Alcaligenes faecalis, Alcaligenes faecalis JM3
-
brenda
Nagasawa, T.; Mauger, J.; Yamada, H.
A novel nitrilase, arylacetonitrilase, of Alcaligenes faecalis JM3. Purification and characterization
Eur. J. Biochem.
194
765-772
1990
Alcaligenes faecalis, Alcaligenes faecalis JM3
brenda
Layh, N.; Parratt, J.; Willetts, A.
Characterization and partial purification of an enantioselective arylacetonitrilase from Pseudomonas fluorescens DSM 7155
J. Mol. Catal. B
5
467-474
1998
Pseudomonas fluorescens
-
brenda
Banerjee, A.; Kaul, P.; Banerjee, U.C.
Purification and characterization of an enantioselective arylacetonitrilase from Pseudomonas putida
Arch. Microbiol.
184
407-418
2006
Pseudomonas putida
brenda
Kiziak, C.; Conradt, D.; Stolz, A.; Mattes, R.; Klein, J.
Nitrilase from Pseudomonas fluorescens EBC191: cloning and heterologous expression of the gene and biochemical characterization of the recombinant enzyme
Microbiology
151
3639-3648
2005
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
brenda
Rustler, S.; Motejadded, H.; Altenbuchner, J.; Stolz, A.
Simultaneous expression of an arylacetonitrilase from Pseudomonas fluorescens and a (S)-oxynitrilase from Manihot esculenta in Pichia pastoris for the synthesis of (S)-mandelic acid
Appl. Microbiol. Biotechnol.
80
87-97
2008
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
brenda
Zhu, D.; Mukherjee, C.; Yang, Y.; Rios, B.E.; Gallagher, D.T.; Smith, N.N.; Biehl, E.R.; Hua, L.
A new nitrilase from Bradyrhizobium japonicum USDA 110. Gene cloning, biochemical characterization and substrate specificity
J. Biotechnol.
133
327-333
2008
Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110
brenda
Kiziak, C.; Klein, J.; Stolz, A.
Influence of different carboxy-terminal mutations on the substrate-, reaction- and enantiospecificity of the arylacetonitrilase from Pseudomonas fluorescens EBC191
Protein Eng. Des. Sel.
20
385-396
2007
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
brenda
Banerjee, A.; Dubey, S.; Kaul, P.; Barse, B.; Piotrowski, M.; Banerjee, U.C.
enantioselective nitrilase from Pseudomonas putida: cloning, heterologous expression, and bioreactor studies
Mol. Biotechnol.
41
35-41
2008
Pseudomonas putida (B0LAW4), Pseudomonas putida MTCC 5110 (B0LAW4)
brenda
Agerbirk, N.; Warwick, S.I.; Hansen, P.R.; Olsen, C.E.
Sinapis phylogeny and evolution of glucosinolates and specific nitrile degrading enzymes
Phytochemistry
69
2937-2949
2008
Sinapis alba
brenda
Rustler, S.; Chmura, A.; Sheldon, R.A.; Stolz, A.
Characterisation of the substrate specificity of the nitrile hydrolyzing system of the acidotolerant black yeast Exophiala oligosperma R1
Stud. Mycol.
61
165-174
2008
Exophiala oligosperma, Exophiala oligosperma R1
brenda
Kiziak, C.; Stolz, A.
Identification of amino acid residues responsible for the enantioselectivity and amide formation capacity of the arylacetonitrilase from Pseudomonas fluorescens EBC191
Appl. Environ. Microbiol.
75
5592-5599
2009
Pseudomonas fluorescens, Pseudomonas fluorescens (Q5EG61)
brenda
Sosedov, O.; Baum, S.; Buerger, S.; Matzer, K.; Kiziak, C.; Stolz, A.
Construction and application of variants of the Pseudomonas fluorescens EBC191 arylacetonitrilase for increased production of acids or amides
Appl. Environ. Microbiol.
76
3668-3674
2010
Pseudomonas fluorescens
brenda
Thuku, R.; Brady, D.; Benedik, M.; Sewell, B.
Microbial nitrilases: Versatile, spiral forming, industrial enzymes
J. Appl. Microbiol.
106
703-727
2009
Alcaligenes faecalis, Alcaligenes faecalis ATCC 8750
brenda
He, Y.C.; Zhang, Z.J.; Xu, J.H.; Liu, Y.Y.
Biocatalytic synthesis of (R)-(-)-mandelic acid from racemic mandelonitrile by cetyltrimethylammonium bromide-permeabilized cells of Alcaligenes faecalis ECU0401
J. Ind. Microbiol. Biotechnol.
37
741-750
2010
Alcaligenes faecalis
brenda
Howden, A.J.; Rico, A.; Mentlak, T.; Miguet, L.; Preston, G.M.
Pseudomonas syringae pv. syringae B728a hydrolyses indole-3-acetonitrile to the plant hormone indole-3-acetic acid
Mol. Plant Pathol.
10
857-865
2009
no activity in no activity in Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. syringae, Pseudomonas syringae pv. syringae B728a
brenda
Sosedov, O.; Matzer, K.; Buerger, S.; Kiziak, C.; Baum, S.; Altenbuchner, J.; Chmura, A.; van Rantwijk, F.; Stolz, A.
Synthesis of enantiomerically pure (S)-mandelic acid using anoxynitrilase–nitrilase bienzymatic cascade: a nitrilase surprisingly shows nitrile hydratase activity
Adv. Synth. Catal.
351
1531 - 1538
2009
Pseudomonas fluorescens (Q5EG61), Pseudomonas fluorescens EBC191 (Q5EG61)
-
brenda
Mateo, C.; Fernandes, B.; van Rantwijk, F.; Stolz, A.; Sheldon, R.A.
Stabilisation of oxygen-labile nitrilases via co-aggregation with poly(ethyleneimine)
J. Mol. Catal. B
38
154-157
2006
Pseudomonas fluorescens (Q5EG61), Pseudomonas fluorescens EBC191 (Q5EG61)
-
brenda
Mateo, C.; Chmura, A.; Rustler, S.; van Rantwijk, F.; Stolz, A.; Sheldon, R.A.
Synthesis of enantiomerically pure (S)-mandelic acid using anoxynitrilase–nitrilase bienzymatic cascade: a nitrilase surprisingly shows nitrile hydratase activity
Tetrahedron Asymmetry
17
320-323
2006
Pseudomonas fluorescens (Q5EG61), Pseudomonas fluorescens EBC191 (Q5EG61)
-
brenda
Baum, S.; Williamson, D.S.; Sewell, T.; Stolz, A.
Conversion of sterically demanding alpha,alpha-disubstituted phenylacetonitriles by the arylacetonitrilase from Pseudomonas fluorescens EBC191
Appl. Environ. Microbiol.
78
48-57
2012
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
brenda
Petrickova, A.; Vesela, A.B.; Kaplan, O.; Kubac, D.; Uhnakova, B.; Malandra, A.; Felsberg, J.; Rinagelova, A.; Weyrauch, P.; K?en, V.; Bezouska, K.; Martinkova, L.
Purification and characterization of heterologously expressed nitrilases from filamentous fungi
Appl. Microbiol. Biotechnol.
93
1553-1561
2012
Aspergillus niger (A2R6M7), Aspergillus niger (A9QXE0), Aspergillus niger CBS 513.88 (A2R6M7), Aspergillus niger CBS 513.88 (A9QXE0), Neurospora crassa, Neurospora crassa OR74A
brenda
Detzel, C.; Maas, R.; Jose, J.
Autodisplay of nitrilase from Alcaligenes faecalis in E. coli yields a whole cell biocatalyst for the synthesis of enantiomerically pure (R)-mandelic Acid
ChemCatChem
3
719-725
2011
Alcaligenes faecalis, Alcaligenes faecalis ATCC 8750
-
brenda
Liu, Z.Q.; Dong, L.Z.; Cheng, F.; Xue, Y.P.; Wang, Y.S.; Ding, J.N.; Zheng, Y.G.; Shen, Y.C.
Gene cloning, expression, and characterization of a nitrilase from Alcaligenes faecalis ZJUTB10
J. Agric. Food Chem.
59
11560-11570
2011
Alcaligenes faecalis, Alcaligenes faecalis ZJUTB10
brenda
Sosedov, O.; Stolz, A.
Improvement of the amides forming capacity of the arylacetonitrilase from Pseudomonas fluorescens EBC191 by site-directed mutagenesis
Appl. Microbiol. Biotechnol.
99
2623-2635
2015
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
brenda
Bhatia, S.; Mehta, P.; Bhatia, R.; Bhalla, T.
Purification and characterization of arylacetonitrile-specific nitrilase of Alcaligenes sp. MTCC 10675
Biotechnol. Appl. Biochem.
61
459-465
2014
Alcaligenes sp. (L7RY40), Alcaligenes sp. MTCC 10675 (L7RY40)
brenda
Sun, H.; Gao, W.; Fan, H.; Wang, H.; Wei, D.
Cloning, purification and evaluation of the enzymatic properties of a novel arylacetonitrilase from Luminiphilus syltensis NOR5-1B: a potential biocatalyst for the synthesis of mandelic acid and its derivatives
Biotechnol. Lett.
37
1655-1661
2015
Luminiphilus syltensis, Luminiphilus syltensis NOR5-1B
brenda
Petrickova, A.; Sosedov, O.; Baum, S.; Stolz, A.; Martinkova, L.
Influence of point mutations near the active site on the catalytic properties of fungal arylacetonitrilases from Aspergillus niger and Neurospora crassa
J. Mol. Catal. B
77
74-80
2012
Aspergillus niger (A2R6M7), Aspergillus niger CBS 513.88 (A2R6M7), Neurospora crassa (V5IPE4), Neurospora crassa DSM 1257 (V5IPE4)
-
brenda
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