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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Subunits
Subunits on EC 4.2.1.84 - nitrile hydratase
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dimer
heterodimer
heterotetramer
heterotrimer
homotetramer
monomer
the two usually separated NHase subunits fused in one protein of the choanoflagellate Monosiga brevicollis
oligomer
tetramer
trimer
additional information
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x * 23000, alpha-subunit, + x * 24000, beta-subunit, calculated
?
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x * 23000, alpha-subunit, + x * 24000, beta-subunit, calculated
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dimer
1 * 22000 (alpha-subunit) + 1 * 24000 (beta-subunit), SDS-PAGE
dimer
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1 * 22000 (alpha-subunit) + 1 * 24000 (beta-subunit), SDS-PAGE
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heterodimer
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1 * 23000, about, alpha-subunit + 1 x 23000, about, beta-subunit, Co-type NHases are bacterial heterodimers, consisting of nonhomologous alpha- and beta-subunits
heterodimer
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1 * 23000, about, alpha-subunit + 1 x 23000, about, beta-subunit, Co-type NHases are bacterial heterodimers, consisting of nonhomologous alpha- and beta-subunits
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heterodimer
alphabeta, nitrile hydratase alpha (NthA), and beta (NthB) subunits
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alpha,beta2, 1 * 55746 + 2 * 63001, 32% amino acid sequence identity of subunits, MALDI-TOF MS and HPLC
heterotrimer
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alpha,beta2, 1 * 55746 + 2 * 63001, 32% amino acid sequence identity of subunits, MALDI-TOF MS and HPLC
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heterotrimer
comparisons of the steady state kinetic parameters of the single subunit variant to the heterotrimeric protein show that the additional subunits impart substrate specificity and catalytic efficiency. 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
alpha10beta10, 10 * 22800 (alpha) + 10 * 26300 (beta), calculated from sequence
oligomer
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alpha10beta10, 10 * 22800 (alpha) + 10 * 26300 (beta), calculated from sequence
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tetramer
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2 * 25400, alpha-subunit, + 2 * 26700, beta-subunit, calculated
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tetramer
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2 * 22982, alpha + 2 * 24108, beta, amino acid sequence, gel filtration
tetramer
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2 * 22982, alpha + 2 * 24108, beta, amino acid sequence, gel filtration
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tetramer
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2 * 27000, alpha-subunit, + 2 * 29000, beta-subunit, alpha2beta2 structure, SDS-PAGE, 2 * 22953, alpha-subunit, + 2 * 23486, beta-subunit, alpha2beta2 structure, sequence calculation
tetramer
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2 * 27000, alpha-subunit, + 2 * 29000, beta-subunit, alpha2beta2 structure, SDS-PAGE, 2 * 22953, alpha-subunit, + 2 * 23486, beta-subunit, alpha2beta2 structure, sequence calculation
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tetramer
alpha2beta2, 2 * 22800 (alpha) + 2 * 25200 (beta), calculated from sequence
tetramer
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alpha2beta2, 2 * 22800 (alpha) + 2 * 25200 (beta), calculated from sequence
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additional information
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structure analysis and salt-bridge interactions involving main chain atoms in region A1 of 1V29, overview
additional information
Bacillus sp. (in: Bacteria) SC-105-1
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structure analysis and salt-bridge interactions involving main chain atoms in region A1 of 1V29, overview
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additional information
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enzyme is comprised of a alpha-subunit with cobalt-binding site and a beta subunit, deduced from sequence
additional information
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enzyme is comprised of a alpha-subunit with cobalt-binding site and a beta subunit, deduced from sequence
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additional information
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NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobaltcontaining alpha-subunit of L-NHase and NhlE. Formation of large-sized complexes during self-subunit swapping in H-NHase. Self-subunit swapping mechanisms, detailed overview
additional information
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NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobaltcontaining alpha-subunit of L-NHase and NhlE. Formation of large-sized complexes during self-subunit swapping in H-NHase. Self-subunit swapping mechanisms, detailed overview
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additional information
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formation of an heterodimer is indispensable for stabilizing the structure of the two subunits, alpha and beta
additional information
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sequence similarity and size of subunits is unusual for NHases
additional information
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sequence similarity and size of subunits is unusual for NHases
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