4.2.1.84: nitrile hydratase
This is an abbreviated version!
For detailed information about nitrile hydratase, go to the full flat file.
Word Map on EC 4.2.1.84
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4.2.1.84
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rhodococcus
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amidase
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acrylamide
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rhodochrous
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erythropolis
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synthesis
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feiii
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low-spin
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fe-type
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non-heme
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sulfenic
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benzonitrile
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pseudonocardia
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sulfinate
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propionamide
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cysteine-sulfinic
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neonicotinoid
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ruber
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propionitrile
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cgmcc
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thiacloprid
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carboxamido
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aldoxime
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indole-3-acetonitrile
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chlororaphis
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metallochaperone
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industry
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pharmacology
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degradation
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environmental protection
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analysis
- 4.2.1.84
- rhodococcus
- amidase
- acrylamide
- rhodochrous
- erythropolis
- synthesis
-
feiii
-
low-spin
-
fe-type
-
non-heme
-
sulfenic
- benzonitrile
- pseudonocardia
-
sulfinate
- propionamide
-
cysteine-sulfinic
-
neonicotinoid
- ruber
- propionitrile
-
cgmcc
- thiacloprid
-
carboxamido
- aldoxime
- indole-3-acetonitrile
- chlororaphis
-
metallochaperone
- industry
- pharmacology
- degradation
- environmental protection
- analysis
Reaction
Synonyms
3-cyanopyridine hydratase, acrylonitrile hydratase, aliphatic nitrile hydratase, ANHase, Co-type NHase, Co-type nitrile hydratase, cobalt-containing nitrile hydratase, CoIII-NHase, CtNHase, Fe-NHase, H-NHase, H-nitrilase, high-molecular mass nitrile hydratase, high-molecular weight nitrile hydratase, hydratase, nitrile, iron-type nitrile hydratase, L-Nhase, L-nitrilase, low-molecular mass nitrile hydratase, low-molecular weight nitrile hydratase, MbNHase, NHase, NHaseK, NI1 NHase, NilCo, NilFe, nitrilase, nitrile hydratase, NthAB, PaNit, ppNHase, ReNHase, TNHase, toyocamycin nitrile hydratase
ECTree
4.2.1.84 nitrile hydrataseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 4.2.1.84 - nitrile hydratase
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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
indole-3-nitrile + H2O
indole-3-acetamide
-
the nitrile hydratase produces only indole-3-acetamide, no indole-3-acetic acid
-
?
(R)-mandelonitrile + H2O
(R)-mandelamide
wild-type enzyme catalyzes the conversion of rac-mandelonitrile to (S)-mandelamide with an enantiomeric excess of 52.6%
-
-
?
(R)-mandelonitrile + H2O
(R)-mandelamide
wild-type enzyme catalyzes the conversion of rac-mandelonitrile to (S)-mandelamide with an enantiomeric excess of 52.6%
-
-
?
(S)-mandelonitrile + H2O
(S)-mandelamide
wild-type enzyme catalyzes the conversion of rac-mandelonitrile to (S)-mandelamide with an enantiomeric excess of 52.6%
-
-
?
(S)-mandelonitrile + H2O
(S)-mandelamide
wild-type enzyme catalyzes the conversion of rac-mandelonitrile to (S)-mandelamide with an enantiomeric excess of 52.6%
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
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-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
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-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
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-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
Rhodococcus sp. N595
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-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
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NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
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a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
3-cyanopyridine + H2O
nicotinamide
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a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
benzonitrile + H2O
benzamide
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
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-
?
benzonitrile + H2O
benzamide
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
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performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
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performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
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performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
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performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
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-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
additional information
?
-
-
substrate specificity of strain 38.1.2, no activity with 4-tolunitrile, overview
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-
?
additional information
?
-
-
substrate specificity of strain 38.1.2, no activity with 4-tolunitrile, overview
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-
?
additional information
?
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-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide, no or reduced activity in NhpR transcriptional regulator defective mutants
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-
?
additional information
?
-
-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide, no or reduced activity in NhpR transcriptional regulator defective mutants
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-
?
additional information
?
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine
-
-
?
additional information
?
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine
-
-
?
additional information
?
-
-
the thermoactive nitrilase from Pyrococcus abyssi hydrolyses small aliphatic nitriles like fumaro- and malononitril, docking calculations for fumaro- and malononitriles, modelling, overview
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-
?
additional information
?
-
-
substrate specificity of strain 77.1, no activity with 4-tolunitrile and 3-chlorobenzonitrile, overview
-
-
?
additional information
?
-
-
substrate specificity of strain 77.1, no activity with 4-tolunitrile and 3-chlorobenzonitrile, overview
-
-
?
additional information
?
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
?
additional information
?
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
?
additional information
?
-
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
?
additional information
?
-
-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE
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-
?
additional information
?
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-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE
-
-
?
additional information
?
-
-
NHase is a non-heme iron enzyme catalyzing the hydration of various nitriles to the corresponding amides
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-
?
additional information
?
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-
NHase is a non-heme iron enzyme catalyzing the hydration of various nitriles to the corresponding amides
-
-
?
additional information
?
-
-
the nitrile hydratase can hydrate aliphatic, aromatic and heterocyclic nitriles under very mild conditions, in mixtures of pH 7 buffer and a range of organic solvents, often with excellent chemoselectivity. Major determinant of hydration occurring is the degree of steric hindrance around the nitrile moiety and/or size of the substrates
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-
?
additional information
?
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-
the nitrile hydratase can hydrate aliphatic, aromatic and heterocyclic nitriles under very mild conditions, in mixtures of pH 7 buffer and a range of organic solvents, often with excellent chemoselectivity. Major determinant of hydration occurring is the degree of steric hindrance around the nitrile moiety and/or size of the substrates
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-
?
