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
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sulfenic
- benzonitrile
- pseudonocardia
-
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
-
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
results (
results (Inhibitors
Inhibitors on EC 4.2.1.84 - nitrile hydratase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1-butaneboronic acid
competitive inhibitor, binds directly to the low-spin Co(III) ion in the active site of PtNHase; competitive inhibitor, binds directly to the low-spin Co(III) ion in the active site of PtNHase
2-Nitrophenol
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10 microM, 40-50% residual activity of NilFe, 90% residual activity of NilCo
3-Nitrophenol
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10 microM, 40-50% residual activity of NilFe, fully active NilCo
4-nitrophenol
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10 microM, 40-50% residual activity of NilFe, 80% residual activity of NilCo
acetamide
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10 mM, product inhibition, reduction of acrylonitrile degrading activity from 1.2 micromol/min/mg to 1.0 micromol/min/mg
benzoic acid
competitive inhibitor; competitive inhibitor
CO
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inhibition of NilCo, reversible by photoactivation, no inhibition of NilFe
nicotinamide
0.5 M, sharp decrease in activity, low-molecular weight nitrile hydratase; 1.5 M, 40% decrease of activity, high-molecular weight nitrile hydratase
phenylboronic acid
competitive inhibitor, binds to the enzyme active site; competitive inhibitor, binds to the enzyme active site
propioamide
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10 mM, product inhibition, reduction of acrylonitrile degrading activity from 1.2 micromol/min/mg to 0.91 micromol/min/mg
propionic acid
competitive inhibitor; competitive inhibitor
tert-butylisonitrile
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substrate inhibition, a Dixon plot shows the reciprocal values of the rate of methacrylonitrile hydration as a function of tert-butylisonitrile concentration, overview
tertiary-butyl isonitrile
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NilFe is unaffected by tertiary-butyl isonitrile
3-Cyanopyridine
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the soluble enzyme shows about 15% residual activity at 500 mM 3-cyanopyridine, NHase immobilized to EupergitC and cross-linked with 1-ethyl-3-(dimethylamino-propyl) carbodiimide shows approximately 50% reduction in 3-cyanopyridine inhibition (about 65% residual activity at 500 mM 3-cyanopyridine)
3-Cyanopyridine
1 M, 40% decrease of activity, low-molecular weight nitrile hydratase; high-molecular weight nitrile hydratase show almost no inhibition at 1 M
Acrylamide
mutant enzyme S122C shows higher tolerance under increasing acrylamide levels than recombinant NHase with modified start codon only
Acrylamide
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when the concentration of acrylamide is higher than 150 g/l, the activity of the immersed-NHase in free resting cells is significantly reduced, when the concentration is higher than 250 g/l, the deactivation is more serious and the half-life of the NHase is less than 120 min
CuCl2
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1 mM, strong inhibition of EDTA-dialysed enzyme, 19% remaining activity
KCN
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complete inhibition at 0.1 mM, competitive with acetonitrile as substrate
n-butyric acid
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competitive inhibitor. Complete inhibition beyond 40 mM. IC50 of 4 mM at pH 7.2 in Hepes buffer 100 mM, IC50 of 8 mM at pH 7.2 in sodium phosphate buffer 100 mM, IC50 of 0.8 mM at pH 6.2 in sodium phosphate buffer 100 mM, IC50 of 12 mM at pH 8.2 in sodium phosphate buffer 100 mM
n-butyric acid
competitive inhibitor, the hydroxyl group of enzyme residue betaTyr68 forms hydrogen bonds with both n-butyric acid and residue alphaSer112, which is located in the active center. Butyric acid acts as a stabilizer of Fe-type NHase, Co-type NHase is more stable; competitive inhibitor, the hydroxyl group of enzyme residue betaTyr68 forms hydrogen bonds with both n-butyric acid and residue alphaSer112, which is located in the active center. Butyric acid acts as a stabilizer of Fe-type NHase, Co-type NHase is more stable
NO
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inhibition of NilCo and NilFe, reversible by photoactivation with 150 W white light
NO
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Substantial structural changes upon NO ligand binding to the iron center, indicating that some mechanical signals are sent upon NO photodissociation, determination NO diffusion paths in NHase, overview
additional information
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the enzyme from Alcaligenes faecalis strain CCTCC M 208168 is resistant to inhibition by cyanide
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additional information
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the enzyme from Bacillus subtilis CCTCC M 206038 is resistant to inhibition by cyanide
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additional information
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maleic, succinic, glutaric and pimelic acid do not act as inhibitors
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additional information
Corynebacterium nitrilophilus
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activity is strongly and reversibly inhibited by alpha-amino and alpha-hydroxynitriles
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additional information
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high concentrations of acrylonitrile inhibit the enzyme activity
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additional information
the enzyme shows a high tolerance against acrylamide; the enzyme shows a high tolerance against acrylamide
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additional information
the enzyme shows a high tolerance against acrylamide; the enzyme shows a high tolerance against acrylamide
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additional information
enzyme-boronic acid complexes represent a snapshot of reaction intermediates; enzyme-boronic acid complexes represent a snapshot of reaction intermediates
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additional information
enzyme-boronic acid complexes represent a snapshot of reaction intermediates; enzyme-boronic acid complexes represent a snapshot of reaction intermediates
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additional information
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the enzyme from Rhodococcus boritolerans strain CCTCC M 208108 is resistant to inhibition by cyanide
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additional information
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not inhibited by dithiothreitol, phenylmethylsulfonylfluoride, and beta-mercaptoethanol
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additional information
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the enzyme from Rhodococcus ruber strain CCTCC M 206040 is resistant to inhibition by cyanide
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additional information
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enzyme is inactive in the dark due to an endogenous nitric oxide molecule bound to the iron center, and is activated by photodissociation
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additional information
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the enzyme from Rhodococcus sp. {G20} is resistant to inhibition by cyanide; the enzyme from Rhodococcus sp. strain N595 is resistant to inhibition by cyanide; the enzyme from Rhodococcus sp. strain P4 is resistant to inhibition by cyanide; the enzyme from Rhodococcus sp. strain ZA0707 is resistant to inhibition by cyanide
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additional information
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the enzyme from Serratia marcescens CCTCC M 208231 is resistant to inhibition by cyanide
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