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Enzyme Nomenclature
Information on EC 4.2.1.84 - nitrile hydratase
for references in articles please use BRENDA:EC4.2.1.84
Word Map on EC 4.2.1.84
- 4.2.1.84
- rhodococcus
- amidase
-
hydration
- acrylamide
- rhodochrous
- erythropolis
-
non-heme
- synthesis
-
fe-type
-
sulfenic
-
low-spin
-
feiii
- benzonitrile
- acetamide
- brevibacterium
-
sulfinate
-
metallochaperone
- testosteroni
-
carboxamido
- chlororaphis
- aldoxime
-
cys-sohs
- pseudonocardia
- propionitrile
- ruber
- propionamide
-
cysteine-sulfinic
- environmental protection
- degradation
- pharmacology
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
4.2.1.84
-
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RECOMMENDED NAME
GeneOntology No.
nitrile hydratase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aliphatic amide = a nitrile + H2O
light
-
-
-
an aliphatic amide = a nitrile + H2O
N-771 and N-774 strains can be inactivated in the dark and reactivated by light
-
an aliphatic amide = a nitrile + H2O
the activity of the enzyme in intact cells increases on light irradiation and gradually decreases in the dark. For purified enzyme no differences are detected when kept in dark or light-irradiated
-
an aliphatic amide = a nitrile + H2O
the iron-type enzyme is photoreactive, it loses the catalytic activity through aerobic incubation in the dark and recovers it by light irradiation
-
an aliphatic amide = a nitrile + H2O
substrate binding occurs via breathing and flip-flop mechanisms
-
an aliphatic amide = a nitrile + H2O
monitoring of binding of substrates and their analogues to the active pocket via the NO bands
-
an aliphatic amide = a nitrile + H2O
possible role of water and active center residues in reaction mechanism is shown
-
an aliphatic amide = a nitrile + H2O
water dynamics and catalytic mechanism, a water molecule bound to the metal ion directly attacks the nitrile carbon, overview. Dynamics of the active site channel, NO diffusion paths, and water molecules positions are key components in the functioning of this important industrial enzyme
-
an aliphatic amide = a nitrile + H2O
reaction mechanism, overview
-
an aliphatic amide = a nitrile + H2O
reaction mechanism, first-shell mechanism of CoIII-NHase involving Tyr68 as catalytic base, deprotonated Tyr68 is proposed to abstract a proton from the nucleophilic water molecule, thus activating it for attack on the metal-bound substrate, modelling, detailed overview
-
an aliphatic amide = a nitrile + H2O
first- and second-shell reaction mechanism, a tyrosine residue acts as catalytic base, modelling, detailed overview
-
an aliphatic amide = a nitrile + H2O
modeling of the catalytic mechanism of nitrile hydratase by semi-empirical quantum mechanical calculation using the enzyme crystal structure, PDB code 1IRE, overview. Active site activation is the first step of NHase catalysis, in which the Co2+ coordinated to a water molecule forms a Co-OH complex mediated by the oxidized alpha-CEA113. Then the oxygen atom in the Co-OH attacks the C atom in the -CN triple bond of acrylonitrile, forming a precursor of acrylamide, proton rearrangement happens transforming the precursor into the final product of acrylamide, under the assistance of the hydrogen atom in the -OH group of alpha-Ser112
an aliphatic amide = a nitrile + H2O
thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview
-
an aliphatic amide = a nitrile + H2O
thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview
an aliphatic amide = a nitrile + H2O
role of residues in the active site and enzymatic reaction mechanism. Cys146 acts as the nucleophile, Glu42 as the general base, Lys113/Glu42 as the general acid, WatA as the hydrolytic water and Nf_Lys113 and N_Phe147 form the oxyanion hole, hydrogen bonding network in the active site of Nit structure, overview
-
an aliphatic amide = a nitrile + H2O
detailed reaction mechanism using large quantum-mechanical active site models, overview. The attack of Cys114-SO- on the coordinated nitrile forms a cyclic intermediate. Cys109-S-S-Cys114 disulfide formation promotes cleavage of the latter to give the amide. Active-site regeneration occurs through attack of water on the disulfide, putative cyclic intermediate structure, overview
-
an aliphatic amide = a nitrile + H2O
mechanism of action for the hydration of nitriles by NHase, overview. The cysteine-sulfenic acid ligand acts as the catalytic nucleophile. The first step in catalysis involves the direct ligation of the nitrile to the active site lowspin, trivalent metal ion. One proton transfer occurs between the alphaCys113-OH ligand and the nitrile N-atom, while the second transfer occurs between the water molecule that reforms alphaCys113-OH and the newly forming imidate N-atom; mechanism of action for the hydration of nitriles by NHase, overview. The cysteine-sulfenic acid ligand acts as the catalytic nucleophile. The first step in catalysis involves the direct ligation of the nitrile to the active site lowspin, trivalent metal ion. One proton transfer occurs between the alphaCys113-OH ligand and the nitrile N-atom, while the second transfer occurs between the water molecule that reforms alphaCys113-OH and the newly forming imidate N-atom
-
an aliphatic amide = a nitrile + H2O
thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview
Bacillus sp. (in: Bacteria) SC-105-1
-
-
an aliphatic amide = a nitrile + H2O
mechanism of action for the hydration of nitriles by NHase, overview. The cysteine-sulfenic acid ligand acts as the catalytic nucleophile. The first step in catalysis involves the direct ligation of the nitrile to the active site lowspin, trivalent metal ion. One proton transfer occurs between the alphaCys113-OH ligand and the nitrile N-atom, while the second transfer occurs between the water molecule that reforms alphaCys113-OH and the newly forming imidate N-atom; mechanism of action for the hydration of nitriles by NHase, overview. The cysteine-sulfenic acid ligand acts as the catalytic nucleophile. The first step in catalysis involves the direct ligation of the nitrile to the active site lowspin, trivalent metal ion. One proton transfer occurs between the alphaCys113-OH ligand and the nitrile N-atom, while the second transfer occurs between the water molecule that reforms alphaCys113-OH and the newly forming imidate N-atom; modeling of the catalytic mechanism of nitrile hydratase by semi-empirical quantum mechanical calculation using the enzyme crystal structure, PDB code 1IRE, overview. Active site activation is the first step of NHase catalysis, in which the Co2+ coordinated to a water molecule forms a Co-OH complex mediated by the oxidized alpha-CEA113. Then the oxygen atom in the Co-OH attacks the C atom in the -CN triple bond of acrylonitrile, forming a precursor of acrylamide, proton rearrangement happens transforming the precursor into the final product of acrylamide, under the assistance of the hydrogen atom in the -OH group of alpha-Ser112; possible role of water and active center residues in reaction mechanism is shown; reaction mechanism, first-shell mechanism of CoIII-NHase involving Tyr68 as catalytic base, deprotonated Tyr68 is proposed to abstract a proton from the nucleophilic water molecule, thus activating it for attack on the metal-bound substrate, modelling, detailed overview; reaction mechanism, overview; thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview
-
-
an aliphatic amide = a nitrile + H2O
first- and second-shell reaction mechanism, a tyrosine residue acts as catalytic base, modelling, detailed overview
-
-
an aliphatic amide = a nitrile + H2O
N-771 and N-774 strains can be inactivated in the dark and reactivated by light; the activity of the enzyme in intact cells increases on light irradiation and gradually decreases in the dark. For purified enzyme no differences are detected when kept in dark or light-irradiated
Rhodococcus sp. N-774
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-O bond cleavage by elimination of water
additional information
C-O bond cleavage by elimination of water
-
-
-
-
additional information
-
a new biocatalytic mechanism is proposed, that is based on crystallographic data of the active center
additional information
-
a new biocatalytic mechanism is proposed, that is based on crystallographic data of the active center
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
degradation of aromatic, nitrogen containing compounds
-
-
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SYSTEMATIC NAME
IUBMB Comments
aliphatic-amide hydro-lyase (nitrile-forming)
Acts on short-chain aliphatic nitriles, converting them into the corresponding amides. Does not act on these amides or on aromatic nitriles. cf. EC 3.5.5.1 nitrilase.
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CAS REGISTRY NUMBER
COMMENTARY
82391-37-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
contain at least two NHases, it is currently not known whether the aeroplysinin-1-hydrating enzyme is of sponge origin or produced by its symbiotic microorganisms
-
-
Bacillus sp. (in: Bacteria) SC-105-1
strain F28, isolated from a wastewater treatment system in a polyacrylonitrile fibre factory
-
-
strain F28, isolated from a wastewater treatment system in a polyacrylonitrile fibre factory
-
-
activity is induced by acetonitrile, acetamide, propionamide, urea
-
-
Fe-dependent, wild-type nitrile hydratase is compared with artificial, Co-dependent nitrile hydratase
-
-
beta-subunit; expression in Escherichia coli
Q5XPL4
Swissprot
gene Pput_2728 encoding subunit alpha; gene Pput_2729 encoding subunit alpha
UniProt
alpha-subunit
SwissProt
cobalt-containing subunit alpha; strain JCM3095
SwissProt
-
-
-
alpha-subunit, gene nha1; genes nha1 and nha2 encoding the alpha and beta subunits of nitrile hydratase
T1VWN1
UniProt
beta-subunit, gene nha2; genes nha1 and nha2 encoding the alpha and beta subunits of nitrile hydratase
T1VX74
UniProt
gene nha1, alpha-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase
UniProt
gene nha1, beta-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase; gene nha2, beta-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase
UniProt
origin of genes encoding NHase (nha1 and nha2) and P44k protein (nha3)
-
-
gene nha1, alpha-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase
UniProt
gene nha1, beta-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase; gene nha2, beta-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase
UniProt
origin of genes encoding NHase (nha1 and nha2) and P44k protein (nha3)
-
-
alpha-subunit, gene nha1; genes nha1 and nha2 encoding the alpha and beta subunits of nitrile hydratase
T1VWN1
UniProt
beta-subunit, gene nha2; genes nha1 and nha2 encoding the alpha and beta subunits of nitrile hydratase
T1VX74
UniProt
activity is induced by acetonitrile, acetamide, propionamide, urea
-
-
2 kinds of enzyme, a high molecular mass: H-NHase, and a low molecular mass enzyme: L-NHase
-
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2 kinds of enzyme, a high molecular mass: H-NHase, and a low molecular mass enzyme: L-NHase
-
-
-
648425, 648428, 648430, 648434, 648436, 648441, 648442, 648444, 648446, 648449, 648454, 665421, 672689, 672727, 673098, 676087, 696768, 698138, 699044, 703230, 715804
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gene toyJ; genes toyJ, toyK, and toyL encoding the three subunits of the enzyme
UniProt
gene toyK; genes toyJ, toyK, and toyL encoding the three subunits of the enzyme
UniProt
gene toyL; genes toyJ, toyK, and toyL encoding the three subunits of the enzyme
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
toyocamycin nitrile hydratase is a unique three-subunit member of the nitrile hydratase family; toyocamycin nitrile hydratase is a unique three-subunit member of the nitrile hydratase family; toyocamycin nitrile hydratase is a unique three-subunit member of the nitrile hydratase family
evolution
because of the absence of sequence similarity between the Co- and Fe-type NHase activators, the two types of NHases might be assembled and maturated by different molecular mechanisms
evolution
-
mass spectrometry of the primary structure of the studied NHases does not reveal any homology to known NHases
metabolism
-
hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation
metabolism
hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation
metabolism
the enzyme is important in the indole-3-acetic acid biosynthesis pathway together with the nitrilase, EC 3.5.5.1, which produces indole-3-amide, but also indole-3-acetic acid , overview; the enzyme is important in the indole-3-acetic acid biosynthesis pathway together with the nitrilase, EC 3.5.5.1, which produces indole-3-amide, but also indole-3-acetic acid , overview
metabolism
-
the enzyme is important in the indole-3-acetic acid biosynthesis pathway together with the nitrilase, EC 3.5.5.1, which produces indole-3-amide, but also indole-3-acetic acid , overview; the enzyme is important in the indole-3-acetic acid biosynthesis pathway together with the nitrilase, EC 3.5.5.1, which produces indole-3-amide, but also indole-3-acetic acid , overview
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metabolism
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hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation
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metabolism
-
hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation
-
physiological function
toyocamycin nitrile hydratase is involved in the biosynthesis of pyrrolopyrimidine antibiotics; toyocamycin nitrile hydratase is involved in the biosynthesis of pyrrolopyrimidine antibiotics; toyocamycin nitrile hydratase is involved in the biosynthesis of pyrrolopyrimidine antibiotics
physiological function
-
formation of aeroplysinin-1 and of the corresponding dienone amide is part of the chemical defence system of the mediterrenean sponge Aplysina cavernicola
additional information
-
in Co-type NHase, the side-chain of alphaThr109, located iin the cysteine cluster region, undergoes a hydrophobic interaction with the side-chain of alphaVal136. The hydroxyl group of residue alphaTyr114, located near the cysteine cluster region, forms hydrogen bonds with the main-chain oxygen atoms of alphaLeu119 and alphaLeu121, via a water molecule; in Co-type NHase, the side-chain of alphaThr109, located iin the cysteine cluster region, undergoes a hydrophobic interaction with the side-chain of alphaVal136. The hydroxyl group of residue alphaTyr114, located near the cysteine cluster region, forms hydrogen bonds with the main-chain oxygen atoms of alphaLeu119 and alphaLeu121, via a water molecule
additional information
-
incorporation of cobalt into L-NHase in a mode of post-translational maturation, i.e. self-subunit swapping. NhlE is recognized as a self-subunit swapping chaperone, mechanism, detailed overview
additional information
-
the recombinant enzyme shows almost the same specific activity and other properties as the native enzyme. Structure of the active center of the recombinant enzyme, overview; the recombinant enzyme shows almost the same specific activity and other properties as the native enzyme. Structure of the active center of the recombinant enzyme, overview
additional information
the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts; the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts; the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts
additional information
the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts; the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts; the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts
additional information
the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts; the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts; the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts
additional information
-
the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts; the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts; the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts
additional information
-
structural modeling, overview; structural modeling, overview
additional information
-
in Co-type NHase, the side-chain of alphaThr109, located iin the cysteine cluster region, undergoes a hydrophobic interaction with the side-chain of alphaVal136. The hydroxyl group of residue alphaTyr114, located near the cysteine cluster region, forms hydrogen bonds with the main-chain oxygen atoms of alphaLeu119 and alphaLeu121, via a water molecule; in Co-type NHase, the side-chain of alphaThr109, located iin the cysteine cluster region, undergoes a hydrophobic interaction with the side-chain of alphaVal136. The hydroxyl group of residue alphaTyr114, located near the cysteine cluster region, forms hydrogen bonds with the main-chain oxygen atoms of alphaLeu119 and alphaLeu121, via a water molecule; structural modeling, overview; structural modeling, overview; the recombinant enzyme shows almost the same specific activity and other properties as the native enzyme. Structure of the active center of the recombinant enzyme, overview; the recombinant enzyme shows almost the same specific activity and other properties as the native enzyme. Structure of the active center of the recombinant enzyme, overview
-
additional information
-
incorporation of cobalt into L-NHase in a mode of post-translational maturation, i.e. self-subunit swapping. NhlE is recognized as a self-subunit swapping chaperone, mechanism, detailed overview
-
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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
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbamide
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbonitrile + H2O
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbamide
(2R)-2-hydroxy-3-methylbutanenitrile + H2O
(2R)-2-hydroxy-3-methylbutanamide
-
-
-
-
?
(2R)-2-hydroxybut-3-enenitrile + H2O
(2R)-2-hydroxybut-3-enamide
-
-
-
-
?
(2R)-2-hydroxybutanenitrile + H2O
(2R)-2-hydroxybutanamide
-
-
-
-
?
(2R)-2-hydroxyhexanenitrile + H2O
(2R)-2-hydroxyhexanamide
-
-
-
-
?
(2R)-2-hydroxypentanenitrile + H2O
(2R)-2-hydroxypentanamide
-
-
-
-
?
(R)-2-chloromandelonitrile + H2O
(R)-2-chloromandelamide
at 100% the rate of 2-hydroxy-4-phenylbutyronitrile
-
-
?
(S)-3-benzoyloxypentanedinitrile + H2O
3-amino-1-(2-amino-2-oxoethyl)-3-oxopropyl benzoate
-
substrate conversion: 38.5%, enantiomeric excess: 68.2
-
-
r
1-(4-bromo-phenyl)-aziridine-2-carbonitrile + H2O
1-(4-bromophenyl)aziridine-2-carboxamide
-
-
-
-
r
1-(4-methoxy-phenyl)-aziridine-2-carbonitrile + H2O
1-(4-methoxyphenyl)aziridine-2-carboxamide
-
-
-
-
r
17alpha-cyanomethyl-17beta-hydroxy-estra-4,9-dien-3-one + H2O
17alpha-acetamido-estra-1,3,5(10),9(11)-tetraene-3,17beta-diol
-
the steroidal group is metabolized very slowly
-
?
2(R)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(R)-(4-chloro-phenyl)-3-methyl-butyramide
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
2,3,4,5,6-pentafluorobenzonitrile + H2O
2,3,4,5,6-pentafluorobenzamide
-
-
-
-
?
2,3-dihydro-benzo(1,4)dioxine-2-carbonitrile + H2O
2,3-dihydro-1,4-benzodioxine-2-carboxamide
-
substrate conversion: 45.1%, enantiomeric excess: 0
-
-
r
2-aminopropionitrile + H2O
2-aminopropionic acid amide
-
90% of the activity with propionitrile
-
-
?
2-chlorobenzaldehyde + HCN + H2O
(R)-2-chloromandelonitrile
-
-
90% conversion to alpha-hydroxy nitrile
-
?
2-fluorobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
2-hydroxy-4-phenylbutyronitrile + H2O
2-hydroxy-4-phenylbutyramide
-
-
-
?
2-hydroxymethyl-3-phenyl-propionitrile + H2O
2-benzyl-3-hydroxypropanamide
-
-
-
-
r
2-methoxymethyl-3-phenyl-propionitrile + H2O
2-benzyl-3-methoxypropanamide
-
-
-
-
r
2-nitrobenzaldehyde + HCN + H2O
? + H2O
-
-
20% conversion to alpha-hydroxy nitrile
-
?
2-phenylbutyronitrile + H2O
2-phenylbutyramide
-
used as well as phenylacetonitrile
-
-
?
2-phenylglycinonitrile + H2O
aminoacetamide
-
used as well as phenylacetonitrile
-
-
?
3-(trifluoromethyl)benzonitrile + H2O
3-(trifluoromethyl)benzamide
-
5% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-(trifluoromethyl)pyridine-4-carbonitrile + H2O
3-(trifluoromethyl)pyridine-4-carboxamide
-
-
-
-
ir
3-allyloxy-4-phenyl-butyronitrile + H2O
4-phenyl-3-(prop-2-en-1-yloxy)butanamide
-
-
-
-
r
3-aminopropionitrile + H2O
3-aminopropionic acid amide
-
2.7% of the activity with propionitrile
-
-
?
3-benzyloxy-3-vinyl-propionitrile + H2O
3-(benzyloxy)pent-4-enamide
-
-
-
-
r
3-bromobenzonitrile + H2O
3-bromobenzamide
-
5% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-chlorobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
3-fluorobenzonitrile + H2O
3-fluorobenzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-hydroxy-3-phenylpropionitrile + H2O
3-hydroxy-3-phenylpropionamide
-
-
-
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropanamide
-
35% of the activity with propionitrile
-
-
?
3-methoxybenzonitrile + H2O
3-methoxybenzamide
-
3% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-phenoxymandelonitrile + H2O
3-phenoxymandelamine
at 10% the rate of 2-hydroxy-4-phenylbutyronitrile
-
-
?
3-phenylpropionitrile + H2O
3-phenylpropionamide
-
used as well as phenylacetonitrile
-
-
?
4-bromobenzonitrile + H2O
4-bromobenzonitrile
-
above 99% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-chloro-3-hydroxybutyronitrile + H2O
4-chloro-3-hydroxybutyramide
-
the following reaction by an amidase leads to the correspondend carboxylic acid
-
-
?
4-chlorobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
4-cyanobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
4-fluorobenzonitrile + H2O
4-fluorobenzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-hydroxybenzaldehyde + HCN + H2O
? + H2O
-
-
55% conversion to alpha-hydroxy nitrile
-
?
4-methylbenzaldehyde + HCN + H2O
? + H2O
-
-
51% conversion to alpha-hydroxy nitrile
-
?
4-methylmandelonitrile + H2O
4-methylmandelamine
at 60% the rate of 2-hydroxy-4-phenylbutyronitrile
-
-
?
4-nitrobenzaldehyde + HCN + H2O
? + H2O
-
-
100% conversion to alpha-hydroxy nitrile
-
?
5-cyanovaleric acid + H2O
6-amino-6-oxohexanoic acid
-
NilFe and NilCo
-
-
r
aeroplysinin-1 + H2O
verongiaquinol
-
high substrate specificity towards the physiological substrate aeroplysinin-1
-
-
?
benzaldehyde + HCN
? + H2O
-
-
95% conversion to alpha-hydroxy nitrile
-
?
ethyl 3-cyanobenzoate + H2O
ethyl 3-carbamoylbenzoate
-
no conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
thiophene-2-carbonitrile + H2O
thiophene-2-carboxamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
toyocamycin + H2O
toyocamycin acid amide
-
-
-
?
trans-4-cyanocyclohexane-1-carboxylic acid + H2O
4-(aminocarbonyl)cyclohexanecarboxylic acid
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbamide
-
substrate conversion: 11.6%, enantiomeric excess: 83.8, 88.9 (methanol), 81.0 (n-hexane)
-
-
r
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbamide
-
substrate conversion: 11.6%, enantiomeric excess: 83.8, 88.9 (methanol), 81.0 (n-hexane)
-
-
r
(1R,3R)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-3-phenylcyclopropanecarbamide
-
substrate conversion: 49.1%, enantiomeric excess: 22.7, 31.1 (methanol), 21.6 (n-hexane)
-
-
r
(1R,3R)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-3-phenylcyclopropanecarbamide
-
substrate conversion: 49.1%, enantiomeric excess: 22.7, 31.1 (methanol), 21.6 (n-hexane)
-
-
r
(1R,3S)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3S)-3-phenylcyclopropanecarbamide
-
substrate conversion: 25.8%, enantiomeric excess: 95.4, 95.4 (methanol), 95.5 (n-hexane)
-
-
r
(1R,3S)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3S)-3-phenylcyclopropanecarbamide
-
substrate conversion: 25.8%, enantiomeric excess: 95.4, 95.4 (methanol), 95.5 (n-hexane)
-
-
r
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbonitrile + H2O
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbamide
-
substrate conversion: 40.3%, enantiomeric excess: 84.7
-
-
r
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbonitrile + H2O
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbamide
-
substrate conversion: 7.9%, enantiomeric excess: 3.2, 5.9 (methanol), 0.7 (n-hexane)
-
-
r
1,1,3,3,-tetramethylbutylisonitrile + H2O
1,1,3,3,-tetramethylisobutylamide
-
-
-
-
?
1,1,3,3,-tetramethylbutylisonitrile + H2O
1,1,3,3,-tetramethylisobutylamide
-
-
-
-
?
2(R)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(R)-(4-chloro-phenyl)-3-methyl-butyramide
-
enantioselective hydration
-
?
2(R)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(R)-(4-chloro-phenyl)-3-methyl-butyramide
-
enantioselective hydration
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
-
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
-
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
enantioselective hydration
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
-
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
-
enantioselective hydration
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarbamide
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarbamide
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
Comamonas oleophilus
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
Rhodococcus sp. N595
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
-
-
-
-
?
2-hydroxypropionitrile + H2O
2-hydroxypropionic acid amide
-
i.e. DL-lactonitrile
-
-
?
2-hydroxypropionitrile + H2O
2-hydroxypropionic acid amide
-
116% of the activity with propionitrile
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
used as well as phenylacetonitrile
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is not enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is not enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is highly enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is highly enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
-
the enzyme is highly enantioselective with the compound
-
-
?
3,4,5-trimethoxybenzonitrile + H2O
3,4,5-trimethoxybenzamide
-
conversion rate: 21.71%
-
-
?
3,4,5-trimethoxybenzonitrile + H2O
3,4,5-trimethoxybenzamide
-
conversion rate: 21.71%
-
-
?
3,4-dimethoxybenzonitrile + H2O
3,4-dimethoxybenzaldehyde
Rhodococcus sp. Novo SP361
-
-
-
-
?
3,4-dimethoxybenzonitrile + H2O
3,4-dimethoxybenzaldehyde + HCN
Rhodococcus sp. Novo SP361
-
-
-
-
?
3-(1-cyanoethyl)benzoic acid + H2O
?
-
the enzyme is enantioselective with the compound
-
-
?
3-(1-cyanoethyl)benzoic acid + H2O
?
-
the enzyme is enantioselective with the compound
-
-
?
3-(1-cyanoethyl)benzoic acid + H2O
?
-
the enzyme is enantioselective with the compound
-
-
?
3-benzoyloxyglutaronitrile + H2O
(S)-3-benzoyloxy-4-cyanobutyramide
-
enantiomeric excess: 95%, 5 h
-
-
?
3-benzoyloxyglutaronitrile + H2O
(S)-3-benzoyloxy-4-cyanobutyramide
-
enantiomeric excess: 95%, 5 h
-
-
?
3-benzyloxyglutaronitrile + H2O
3-benzyloxy-4-cyanobutyramide
-
enantiomeric excess: 69%, 30 min
-
-
?
3-benzyloxyglutaronitrile + H2O
3-benzyloxy-4-cyanobutyramide
-
enantiomeric excess: 69%, 30 min
-
-
?
3-chlorobenzonitrile + H2O
3-chlorobenzamide
-
95% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
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
-
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
-
NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
3-cyanopyridine + H2O
nicotinamide
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
3-cyanopyridine + H2O
nicotinamide
-
a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
-
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
a niacin precursor
-
-
?
3-hydroxybutryronitrile + H2O
3-hydroxybutyramide
Q5XPL4;
-
yield 99%
-
?
3-hydroxybutryronitrile + H2O
3-hydroxybutyramide
Q5XPL4;
-
yield 99%
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropionamide
Q5XPL4;
-
yield 100%
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropionamide
Q5XPL4;
-
yield 100%
-
?
3-hydroxyvaleronitrile + H2O
3-hydroxyvaleramide
Q5XPL4;
-
yield 99%
-
?
3-hydroxyvaleronitrile + H2O
3-hydroxyvaleramide
Q5XPL4;
-
yield 99%
-
?
3-methylbenzonitrile + H2O
3-methylbenzamide
-
17% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
3-phenylpropanenitrile + H2O
3-phenylpropanamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-(trifluoromethyl)benzonitrile + H2O
4-(trifluoromethyl)benzamide
-
-
-
-
ir
4-(trifluoromethyl)benzonitrile + H2O
4-(trifluoromethyl)benzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-acetylbenzonitrile + H2O
4-acetylbenzamide
-
above 99% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-chlorobenzonitrile + H2O
4-chlorobenzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-cyanopyridine + H2O
isonicotinamide
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
4-cyanopyridine + H2O
isonicotinamide
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid amide
-
-
-
-
?
4-methoxybenzonitrile + H2O
4-methoxybenzamide
-
above 99% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
4-methylbenzonitrile + H2O
4-methylbenzamide
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
5-hydroxymethyl-2-furonitrile + H2O
5-hydroxymethyl-2-furamide
-
-
-
-
?
5-hydroxymethyl-2-furonitrile + H2O
5-hydroxymethyl-2-furamide
-
-
-
-
?
acetonitrile + H2O
acetamide
-
10% of the activity with propionitrile
-
-
?
acetonitrile + H2O
acetamide
-
10% of the activity with propionitrile
-
-
?
acetonitrile + H2O
acetamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acetonitrile + H2O
acetamide
-
79% of the activity with acrylonitrile
-
-
?
acetonitrile + H2O
acetamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
r
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
78% of the activity with propionitrile
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylamide
-
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
acrylamide
analysis of the structure model of the enzyme-substrate complex and catalytic mechanism, overview
-
-
?
acrylonitrile + H2O
acrylamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
acrylonitrile + H2O
acrylamide
-
stereoselective reaction
-
-
?
acrylonitrile + H2O
acrylamide
analysis of the structure model of the enzyme-substrate complex and catalytic mechanism, overview
-
-
?
acrylonitrile + H2O
acrylamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
acrylonitrile + H2O
acrylamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acrylonitrile + H2O
acrylamide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
adiponitrile + H2O
adipic acid amide
-
108% of the activity with propionitrile
-
-
?
an aliphatic amide
a nitrile + H2O
-
ligand exchange reactions, overview
-
-
?
an aliphatic amide
a nitrile + H2O
-
ligand exchange reactions, overview
-
-
?
an aliphatic amide
a nitrile + H2O
-
ligand exchange reactions, overview
-
-
?
an aliphatic amide
a nitrile + H2O
-
ligand exchange reactions, overview
-
-
?
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
-
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
substrate of recombinant wild-type and mutant enzymes
-
-
?
benzonitrile + H2O
benzamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
benzonitrile + H2O
benzamide
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
-
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
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
benzonitrile + H2O
benzamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
benzonitrile + H2O
benzoic acid amide
-
1.3% of the activity with propionitrile
-
-
?
benzonitrile + H2O
benzoic acid amide
-
15% of the activity with acrylonitrile
-
-
?
benzonitrile + H2O
benzoic acid amide
-
19.4% of the activity with acrylonitrile
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
-
-
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
-
-
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
butyronitrile + H2O
butyramide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
butyronitrile + H2O
butyramide
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
chloroacetonitrile + H2O
chloroacetamide
-
42% of the activity with propionitrile
-
-
?
chloroacetonitrile + H2O
chloroacetamide
-
42% of the activity with propionitrile
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
-
19% of the activity with propionitrile
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
-
19% of the activity with propionitrile
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
-
19% of the activity with propionitrile
-
-
?
ethyl 4-cyanobenzoate + H2O
ethyl 4-carbamoylbenzoate
-
95% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
furan-2-carbonitrile + H2O
furan-2-carboxamide
-
99.9% conversion, in phosphate buffer pH 7.0, at 30°C
-
-
?
hydroxyacetonitrile + H2O
hydroxyacetamide
-
50% of the activity with propionitrile
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
-
-
-
-
?
indole-3-acetonitrile + H2O
indole-3-acetamide
-
conversion rate: 34.44%
-
-
?
indole-3-nitrile + H2O
indole-3-acetamide
-
the nitrile hydratase produces only indole-3-acetamide, no indole-3-acetic acid
-
?
indole-3-nitrile + H2O
indole-3-acetamide
-
the nitrile hydratase produces only indole-3-acetamide, no indole-3-acetic acid
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
113% of the activity with propionitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
113% of the activity with propionitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
71% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
71% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
62.5% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
-
62.5% of the activity with acrylonitrile
-
-
?
isovaleronitrile + H2O
isovaleric acid amide
-
more active than trans-4-cyanocyclohexane-1-carboxylic acid as substrate
-
-
?
isovaleronitrile + H2O
isovaleric acid amide
-
-
product identification by liquid chromatography tandem mass spectrometry
-
?
isovaleronitrile + H2O
isovaleric acid amide
-
-
product identification by liquid chromatography tandem mass spectrometry
-
?
methacrylamide + H2O
?
-
causes the greatest induction of activity
-
-
?
methacrylamide + H2O
?
-
causes the greatest induction of activity
-
-
?
methacrylonitrile + H2O
methacrylamide
substrate of recombinant wild-type and mutant enzymes
-
-
?
methacrylonitrile + H2O
methacrylamide
substrate of recombinant wild-type and mutant enzymes
-
-
?