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
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feiii
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low-spin
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fe-type
-
non-heme
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sulfenic
- benzonitrile
- pseudonocardia
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sulfinate
- propionamide
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cysteine-sulfinic
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neonicotinoid
- ruber
- propionitrile
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cgmcc
- thiacloprid
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carboxamido
- aldoxime
- indole-3-acetonitrile
- chlororaphis
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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
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Application
Application on EC 4.2.1.84 - nitrile hydratase
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analysis
Bacillus sp. APB-6
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the enzyme is used in production of acrylamide from acrylonitrile. For maximum production of Co2+ containing nitrile hydratase, is cultured in the medium containing lactose (18.0 g/l), peptone (1.0 g/l), yeast extract (2.0 g/l), MgSO4 (0.5 g/l), K2HPO4 (0.6 g/l), urea (9.0 g/l), and CoCl2 (0.01 g/l), pH 7.0, and incubated at 35°C for 24 h in an incubator shaker (160 rpm). Nitrile hydratase exhibits relatively high specificity for aliphatic nitriles. Free cells are immobilized using 2% (w/v) agar solution to enhance enzyme stability and reusability in repetitive cycles of acrylamide production. Under optimized conditions, nearly complete bioconversion of acrylonitrile is achieved with a fair recovery of 85% using free and immobilized cells equivalent to 500 mg/dry cell weight/l
degradation
environmental protection
industry
pharmacology
synthesis
additional information
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treatment of acetonitrile-containing wastes on-site, Brevundimonas diminuta containing enzyme degrades acetonitrile at concentrations up to 6 M
degradation
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treatment of acetonitrile-containing wastes on-site, Rhodococcus pyridinivorans S85-2 containing enzyme degrades acetonitrile at concentrations up to 6 M
degradation
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treatment of acetonitrile-containing wastes on-site, Brevundimonas diminuta containing enzyme degrades acetonitrile at concentrations up to 6 M
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degradation
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treatment of acetonitrile-containing wastes on-site, Rhodococcus pyridinivorans S85-2 containing enzyme degrades acetonitrile at concentrations up to 6 M
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environmental protection
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NHase is used in two-step degradation (including amidase, EC 3.5.1.4) of acetonitrile-containing waste
environmental protection
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NHase is used in two-step degradation (including amidase, EC 3.5.1.4) of acetonitrile-containing waste
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biotransformation of nitrile. Nitrile hydratase from Rhodococcus rhodochrous J1 is used for industrial production of acrylamide and nicotinamide. Production of enzyme by recombinant Escherichia coli is superior to that in R. rhodochrous J1. Genetically engineered Escherichia coli can be used for industrial applications instead of Rhodococcus rhodochrous J1. High-molecular weight nitrile hydratase may be more suitable for industrial application than low-molecular weight nitrile hydratase because of its higher product tolerance, which would lead to a high product concentration
industry
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biotransformation of nitrile. Nitrile hydratase from Rhodococcus rhodochrous J1 is used for industrial production of acrylamide and nicotinamide. Production of enzyme by recombinant Escherichia coli is superior to that in R. rhodochrous J1. Genetically engineered Escherichia coli can be used for industrial applications instead of Rhodococcus rhodochrous J1. High-molecular weight nitrile hydratase may be more suitable for industrial application than low-molecular weight nitrile hydratase because of its higher product tolerance, which would lead to a high product concentration
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synthesis, biotransformation and biocatalysis of unsaturated/saturated aliphatic, aromatic and heterocyclic nitriles
pharmacology
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synthesis, biotransformation and biocatalysis of unsaturated/saturated aliphatic, aromatic and heterocyclic nitriles
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synthesis
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useful for modification of polyacrylonitrile fibers and granulates
synthesis
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H-NHase is used in the industrial production of acrylamide and nicotinamide
synthesis
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production of nicotinamide (=vitamin B3) for vitamin supplement for food and animal feed
synthesis
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production of 2-naphthylacetamide by one-pot chemo-enzymatic conversion
synthesis
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production of D-tert-leucine-nitrile from racemic tert-leucine-nitrile by use of enzyme plus D-selective amidase from Variovorax paradoxus
synthesis
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production of propionamide by use of enzyme in ultrafiltration-membrane reactor with maximum volumetric production of 0.5 g propionamide per litre and h
synthesis
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industrial production of (S)-2,2-dimethylcyclopropanecarboxylic acid
synthesis
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enzyme can be used in conjunction with a stereoselective amidase to synthesize ethyl (S)-4-chloro-3-hydroxybutyrate, an intermediate for a hypercholesterolemia drug, Atorvastatin
synthesis
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nitrile hydratase is an enzyme used in the industrial biotechnological production of acrylamide
synthesis
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nitrile hydratase is used for large scale industrial production of important commodities such as acrylamide and nicotinamide
synthesis
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the enzyme is useful in synthesis of compounds by hydrating biotransformations, optimization of strain cultivation and enzyme production and activity, overview
synthesis
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bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, carried out in continuously stirred tank UF-membrane bioreactors arranged in series, the reactor configuration enables both enzymes, involved in the cascade reaction, to work with optimized kinetics, without any purification, exploiting their differing temperature dependences, method optimization, overview
synthesis
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bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, operated in either batch or continuous mode, method optimization, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
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transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is a cellfree extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
synthesis
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transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
synthesis
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transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
synthesis
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NHases are important for large scale production of acrylamide and nicotinamide
synthesis
industrial production of highly purified acrylamide and nicotinamide. The thermostability and catalytic efficiency of the subunit-fused nitrile hydratase is improved by semi-rational engineering
synthesis
A0A2Z6FCE3; A0A2Z6FCD3
the enzyme from Rhodococcus aetherivorans JB1208 shows high regioselectivity and strong substrate tolerance for alicyclic dinitrile and affords a potentially industrial route to gabapentin (a precursor of gamma-aminobutyric acid, which has been approved for treatment of a variety of central nervous system disorders, partial seizures, and restless legs syndrome)
synthesis
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use of recombinant Corynebacterium cells for the production of acrylamide from acrylonitrile results in a conversion yield of 93% and a final acrylamide concentration of 42.5% within 6 h when the total amount of fed acrylonitrile is 456 g
synthesis
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transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
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synthesis
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transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is a cellfree extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
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synthesis
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the enzyme is useful in synthesis of compounds by hydrating biotransformations, optimization of strain cultivation and enzyme production and activity, overview
-
synthesis
-
transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
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synthesis
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production of 2-naphthylacetamide by one-pot chemo-enzymatic conversion
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synthesis
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
production of D-tert-leucine-nitrile from racemic tert-leucine-nitrile by use of enzyme plus D-selective amidase from Variovorax paradoxus
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
enzyme can be used in conjunction with a stereoselective amidase to synthesize ethyl (S)-4-chloro-3-hydroxybutyrate, an intermediate for a hypercholesterolemia drug, Atorvastatin
-
synthesis
-
use of recombinant Corynebacterium cells for the production of acrylamide from acrylonitrile results in a conversion yield of 93% and a final acrylamide concentration of 42.5% within 6 h when the total amount of fed acrylonitrile is 456 g
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
industrial production of highly purified acrylamide and nicotinamide. The thermostability and catalytic efficiency of the subunit-fused nitrile hydratase is improved by semi-rational engineering
-
synthesis
-
nitrile hydratase is used for large scale industrial production of important commodities such as acrylamide and nicotinamide
-
synthesis
-
useful for modification of polyacrylonitrile fibers and granulates
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, operated in either batch or continuous mode, method optimization, overview
-
synthesis
-
bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, carried out in continuously stirred tank UF-membrane bioreactors arranged in series, the reactor configuration enables both enzymes, involved in the cascade reaction, to work with optimized kinetics, without any purification, exploiting their differing temperature dependences, method optimization, overview
-
synthesis
-
production of propionamide by use of enzyme in ultrafiltration-membrane reactor with maximum volumetric production of 0.5 g propionamide per litre and h
-
synthesis
Rhodococcus aetherivorans JB1208
-
the enzyme from Rhodococcus aetherivorans JB1208 shows high regioselectivity and strong substrate tolerance for alicyclic dinitrile and affords a potentially industrial route to gabapentin (a precursor of gamma-aminobutyric acid, which has been approved for treatment of a variety of central nervous system disorders, partial seizures, and restless legs syndrome)
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
Rhodococcus sp. N595
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nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
production of nicotinamide (=vitamin B3) for vitamin supplement for food and animal feed
-
synthesis
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H-NHase is used in the industrial production of acrylamide and nicotinamide
-
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Rhodococcus erythropolis A4 converts benzonitrile herbicides into amides, the strain is able to hydrolyze 2,6-dichlorobenzamide into 2,6-dichlorobenzoic acid, and produces also the carboxylic acids from the other herbicides. Transformation of nitriles into amides decreases acute toxicities for chloroxynil and dichlobenil, but increases them for bromoxynil and ioxynil. The amides inhibit root growth in Lactuca sativa less than the nitriles but more than the acids. The conversion of the nitrile group may be the first step in the mineralization of benzonitrile herbicides but cannot be itself considered to be a detoxification
additional information
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Rhodococcus rhodochrous PA-34 converts benzonitrile herbicides into amides, but the strain does not hydrolyze 2,6-dichlorobenzamide into 2,6-dichlorobenzoic acid. Transformation of nitriles into amides decreases acute toxicities for chloroxynil and dichlobenil, but increases them for bromoxynil and ioxynil. The amides inhibit root growth in Lactuca sativa less than the nitriles but more than the acids. The conversion of the nitrile group may be the first step in the mineralization of benzonitrile herbicides but cannot be itself considered to be a detoxification
additional information
-
Rhodococcus erythropolis A4 converts benzonitrile herbicides into amides, the strain is able to hydrolyze 2,6-dichlorobenzamide into 2,6-dichlorobenzoic acid, and produces also the carboxylic acids from the other herbicides. Transformation of nitriles into amides decreases acute toxicities for chloroxynil and dichlobenil, but increases them for bromoxynil and ioxynil. The amides inhibit root growth in Lactuca sativa less than the nitriles but more than the acids. The conversion of the nitrile group may be the first step in the mineralization of benzonitrile herbicides but cannot be itself considered to be a detoxification
-
additional information
-
Rhodococcus rhodochrous PA-34 converts benzonitrile herbicides into amides, but the strain does not hydrolyze 2,6-dichlorobenzamide into 2,6-dichlorobenzoic acid. Transformation of nitriles into amides decreases acute toxicities for chloroxynil and dichlobenil, but increases them for bromoxynil and ioxynil. The amides inhibit root growth in Lactuca sativa less than the nitriles but more than the acids. The conversion of the nitrile group may be the first step in the mineralization of benzonitrile herbicides but cannot be itself considered to be a detoxification
-