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Literature summary extracted from

  • Kubiak, K.; Nowak, W.
    Molecular dynamics simulations of the photoactive protein nitrile hydratase (2008), Biophys. J., 94, 3824-3838.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.84 additional information the enzyme is activated by absorption of photons of wavelength of about 630 nm Rhodococcus sp.

Application

EC Number Application Comment Organism
4.2.1.84 synthesis nitrile hydratase is an enzyme used in the industrial biotechnological production of acrylamide Rhodococcus sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.84 analysis of the crystal structure of inactive NHase, overview Rhodococcus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.84 NO 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 Rhodococcus sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.84 Co3+ contains nonheme iron or noncorrin cobalt, the ion is bound buried in the protein core at the interface of two domains alpha and beta Rhodococcus sp.
4.2.1.84 Fe3+ 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 Rhodococcus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.84 acrylonitrile + H2O Rhodococcus sp.
-
 acrylamide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.84 Rhodococcus sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.84 an aliphatic amide = a nitrile + H2O water dynamics and catalytic mechanism, a water molecule bound to the metal ion directly attacks the nitrile carbon, overview. Dynamics of the active site channel, NO diffusion paths, and water molecules positions are key components in the functioning of this important industrial enzyme Rhodococcus sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.84 acrylonitrile + H2O
-
 Rhodococcus sp. acrylamide
-
 ?
4.2.1.84 additional information hydrogen bonds between betaArg56 and alphaCys114 sulfenic acid are important to maintain the enzymatic activity, molecular dynamics simulations determining the differences in the dynamics of lightactive and dark-inactive forms of NHase, overview Rhodococcus sp. ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.84 NHase
-
 Rhodococcus sp.