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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

Reaction

an aliphatic amide
=
A nitrile
 +
H2O

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 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.84 nitrile hydratase

General Stability

General Stability on EC 4.2.1.84 - nitrile hydratase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
active in acrylamide up to 60% w/v
completely stabilized by 22 mM n-butyric acid
-
Escherichia coli chaperones GroEL-ES work well in Rhodococcus and simultaneously possess protein-folding assistance functions and the ability to stabilize and reactivate the native nitrile hydratase
-
immobilization and stabilization of a nitrile hydratase in the form of a cross-linked enzyme aggregate using ammonium sulfate as an aggregation agent followed by cross-linking with glutaraldehyde, method development and evaluation, overview. The stability of aggregated and immobilized enzyme is increased compared to enzyme in cell extract or whole cells
-
KH2PO4-NaOH and Tris-HCl buffer are tested at 28°C and pH 7.5. 20% NHase activity is lost after 18 h and is further decreasing. 73.5 h later, NHase activity in Tris-HCl is unchanged while in KH2PO4-NaOH abrupt decrease is observed.
-
loss of activity caused by storage at 0°C can be restored by irradiation with light of 370 nm
-
nitrile hydratase cross-linked enzyme aggregates are sensitive to water-immiscible organic solvents as well as to aldehydes and hydrogen cyanide, but are remarkably stable and show useful activity in acidic aqueous environments of pH 4-5
-
organic acids stabilize, stable for more than 1 month in 0.1 M HEPES/KOH, pH 7.2, with 44 mM n-butyric acid, n-valeric acid, isovaleric acid, isobutyric acid or n-caproic acid
-
potassium phosphate buffer has a negative effect on stability
-
purified mutant NHases are stored in the dark without n-butyric acid, before use, NHases are activated by light irradiation.
-
residual activity levels after heat shock and acrylamide immersion increase by 2.9fold and 1.1fold, respectively in nitrile hydratase-chaperone GroEL2 chimera compared with the single nitrile hydratase control
-
the enzyme becomes more unstable as it becomes purer. Isovalerate, 30 mM, and caprylate stabilize effectively
-
the partially purified enzyme is stable in the presence of organic acids at higher temperatures
-
unstable when diluted, but completely stabilized with low-molecular organic acids such as n-butyric acid, n-valeric acid, propionic acid and acetic acid
-