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
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Metals Ions
Metals Ions on EC 4.2.1.84 - nitrile hydratase
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acetate
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the acetate ion binds close to Mg2+, and it interacts with two coordinating water molecules
Co2+
Co3+
Fe2+
Fe3+
Mg2+
Mn2+
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the enzyme is manganese-dependent, cobalt and nickel ions can substitute for it. One site binding model with Km = 0.8 mM
Ni2+
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the enzyme is manganese-dependent, cobalt and nickel ions can substitute for it
additional information
Co2+
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the enzyme is manganese-dependent, cobalt and nickel ions can substitute for it
Co2+
the enzyme requires non-corrin cobalt for its catalytic activity. Cobalt ions are necessary for the expression and activity of NHaseK in Escherichia coli
Co2+
the enzyme expressed in the presence of 0.25 mM CoCl2 contains about 1.8 equivalents of cobalt per homodimer while the enzyme expressed in the absence of CoCl2 contains 1.6 cobalt ions per homodimer
Co2+
cobalt-containing nitrile hydratase, noncorrin cobalt at the catalytic center, structure, overview. Two cysteine residues (alphaCys111 and alphaCys113) coordinated to the cobalt are posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively
Co2+
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addition at 0.001% results in 68fold enhancement of activity
Co2+
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0.1% w/v, greatly increases the enzyme activity. Different Co2+ compounds increase the enzyme activity
Co2+
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plays a role in the stabilization of the polypeptide structure
Co2+
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incorporation of cobalt into L-NHase depends on the alpha-subunit exchange between cobalt-free, apo-L-NHase and its cobalt-containing mediator, NhlAE, i.e. holo-NhlAE, in a mode of post-translational maturation, i.e. self-subunit swapping. NhlE is recognized as a self-subunit swapping chaperone. Incorporation of cobalt into H-NHase also occurs via self-subunit swapping. Cobalt is inserted into cobalt-free, apo-NhhAG, but not into apo-H-NHase, suggesting that NhhG functions not only as a self-subunit swapping chaperone but also as a metallochaperone. Formation of large-sized complexes during self-subunit swapping in H-NHase. Self-subunit swapping mechanism, detailed overview
Co2+
about 1 mol of cobalt per mol of enzyme
Co2+
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incorporated instead of Fe into the catalytic site with initial weak activity that increases when an oxidizing agent is added
Co2+
cobalt-type nitrile hydratase, and the addition of cobalt to the cell growth broth significantly stimulates nitrile hydratase activity. Supplementing cobalt to phosphate buffer containing purified enzyme has no effect on nitrile hydratase activity
Co2+
the metal cofactor is located in the alpha-subunit at the interfacial active site of the heterodimeric enzyme
Co3+
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CD spectrum suggests low-spin Co3+ in tetragonally-distorted octahedral ligand field
Co3+
a Co-type NHase, Co3+ coordinated to a water molecule forms a Co-OH complex mediated by the oxidized alpha-CEA113
Co3+
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the enzyme belongs to the CoIII-NHase group of enzymes, octahedrally coordinated metal ion with two deprotonated backbone amides as ligands as well as three cysteine residues, two of which are posttranslationally oxidized to cysteine-sulfenic and cysteine-sulfinic acids
Co3+
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the unique active site structure of metalloenzyme nitrile hydratase includes a central metal ion, Co3+ or Fe3+, coordinated octahedrally by two amide nitrogens from the peptide backbone, one cysteine sulfur and two oxidized cysteine sulfurs, Cys-SO and Cys-SO2
Co3+
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the incorporation of cobalt into L-NHase is depend on the alpha-subunit exchange between apo-L-NHase and NhlAE, cobalt is inserted into both the cobaltfree maturation mediator NhlAE (apo-NhlAE) and the cobalt-free alpha-subunit in an NhlE-dependent manner in the presence of cobalt and dithiothreitol in vitro
Co3+
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contains nonheme iron or noncorrin cobalt, the ion is bound buried in the protein core at the interface of two domains alpha and beta
Fe2+
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direct binding of the substrate to the Fe(III)-active site of the enzyme
Fe2+
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non-heme iron enzyme with a typical low-spin Fe(III)-active center
Fe2+
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a protein-bound six-coordinate mononuclear non-heme iron with a mixed sulfur and nitrogen or oxygen coordination sphere. Three of the five cysteines in the enzyme in a tentatively assigned metal binding site
Fe2+
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contains approximately 3 g-atoms iron/mol enzyme, tightly bound to the protein
Fe2+
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non-heme iron enzyme with a typical low-spin Fe(III)-active center
Fe2+
with cobalt substitution for iron, the enzyme activity becomes weak
Fe2+
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an FeIII-NHase with a non-heme iron center. Structure of NHase active site showing the FeIII coordination sphere and some conserved residues, overview
Fe2+
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non-heme iron enzyme with a typical low-spin Fe(III)-active center
Fe-type nitrile hydratase. Iron content of wild-type enzyme is 1.4 equivalents of iron per (alphabeta)2 heterotetramer. Mutating the active site alphaH80, alphaHs81, and alphaR157 residues have little or no effect on the incorporation of iron into the active site. In the alpha-subunit mutant enzyme (H80W/H81W, H80A/H81A and R157A), hydrogen-bonding interactions crucial for the catalytic function of the alphaCys104-SOH ligand are disrupted. Disruption of these hydrogen bonding interactions likely alters the nucleophilicity of the sulfenic acid oxygen and the Lewis acidity of the active site Fe(III) ion
Fe3+
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the unique active site structure of metalloenzyme nitrile hydratase includes a central metal ion, Co3+ or Fe3+, coordinated octahedrally by two amide nitrogens from the peptide backbone, one cysteine sulfur and two oxidized cysteine sulfurs, Cys-SO and Cys-SO2
Fe3+
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the enzyme contains an Fe(III) ion coordinated in a characteristic claw setting by an axial cysteine thiolate, two equatorial peptide nitrogens, the sulfur atoms of equatorial cysteine-sulfenic and cysteine-sulfinic acids, and an axial water/hydroxyl moiety. The cysteine-sulfenic acid is susceptible to oxidation, and the enzyme is traditionally prepared using butyric acid as an oxidative protectant. The as-prepared enzyme exhibits a complex electron paramagnetic resonance spectrum due to multiple low-spin (S = 1/2) Fe(III) species
Fe3+
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NHase N'4 is a Fe-type enzyme with a Cys109-Ser110-Leu111-Cys112-Ser113-Cys114 sequence
Fe3+
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the enzyme belongs to the FeIII-NHase group of enzymes, octahedrally coordinated metal ion with two deprotonated backbone amides as ligands as well as three cysteine residues, two of which are posttranslationally oxidized to cysteine-sulfenic and cysteine-sulfinic acids
Fe3+
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contains nonheme iron or noncorrin cobalt, the ion is bound buried in the protein core at the interface of two domains alpha and beta, photosensitivity of the Fe-type NHase
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Mg2+ bound in chain B interacts with five water molecules and Asn49B
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the Agrobacterium tunefaciens enzyme does not contain Be, B, Mg, Al, Si, P, S, Ca, Ti, V, Cr, Mn, Ni, Cu, Zn, Se, Sr, Zr, Mo, Pd, Ag, Cd, Sn, Sb, Ba, Ta, W, Pt, Au, Hg, Pb, La, or Ce
additional information
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redox potentials and structures of metal ion-enzyme complexes, overview
additional information
structure comparison with the Fe-type NHase, overview. In cobalt-containing nitrile hydratase, a tryptophan residue betaTrp72, which may be involved in substrate binding, replaces the tyrosine residue of iron-containing nitrile hydratase
additional information
structure comparison with the Fe-type NHase, overview. In cobalt-containing nitrile hydratase, a tryptophan residue betaTrp72, which may be involved in substrate binding, replaces the tyrosine residue of iron-containing nitrile hydratase
additional information
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the apoenzyme shows no detectable activity, a disulfide bond between highly conserved Co-binding residues alphaCys108 and alphaCys113 is formed in the apoenzyme structure
additional information
the apoenzyme shows no detectable activity, a disulfide bond between highly conserved Co-binding residues alphaCys108 and alphaCys113 is formed in the apoenzyme structure
additional information
the apoenzyme shows no detectable activity, a disulfide bond between highly conserved Co-binding residues alphaCys108 and alphaCys113 is formed in the apoenzyme structure
additional information
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specific binding of the carboxylate group, as well as a more general electrostatic preference for negatively charged ligands revealed by binding of the Br- ions, overview
additional information
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CuSO4, CaCl2, ZnSO4, MnCl2, NaMnO4, FeCl3, FeSO4, AlCl3, BaCl2, SrCl2, NaWO4, SnCl2, BeSO4, NiCl2, PbCl2, LiCl and CoCl2 at 0.1% w/v neither inhibit nor enhance the enzyme activity