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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Posttranslational Modification
Posttranslational Modification on EC 4.2.1.84 - nitrile hydratase
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side-chain modification
additional information
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alphaCys112 and alphaCys114 are modified to cysteine sulfinic acids and isobutyronitrile is included in active site, evidence from crystallographic data
side-chain modification
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alphaCys112 and alphaCys114 are modified to cysteine sulfinic acids and isobutyronitrile is included in active site, evidence from crystallographic data
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alphaCys112 is modified to a cysteine-sulfinic acid in both recombinant and native enzymes
additional information
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two cysteine ligands, alphaCys112 and alphaCys114, are oxidized to a cysteine sulfinic acid and a cysteine sulfenic acid, respectively. Cysteine sulfinic acid in 112 is responsible for the catalytic activity. First metalloprotein having posttranslationally modified cysteine ligands