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Literature summary for 4.2.1.84 extracted from

  • Song, L.; Wang, M.; Shi, J.; Xue, Z.; Wang, M.X.; Qian, S.
    High resolution X-ray molecular structure of the nitrile hydratase from Rhodococcus erythropolis AJ270 reveals posttranslational oxidation of two cysteines into sulfinic acids and a novel biocatalytic nitrile hydration mechanism (2007), Biochem. Biophys. Res. Commun., 362, 319-324.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method, X-ray diffraction, resolution: 1.3 A, ferric ion coordinating residues Rhodococcus erythropolis

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis
-
-
-
Rhodococcus erythropolis AJ270
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification alphaCys112 and alphaCys114 are modified to cysteine sulfinic acids and isobutyronitrile is included in active site, evidence from crystallographic data Rhodococcus erythropolis

Purification (Commentary)

Purification (Comment) Organism
sonication, (NH4)2SO4 fractionation, DEAE-Sephacel/phenyl Sepharose/Sephacryl S200 column chromatography Rhodococcus erythropolis

Subunits

Subunits Comment Organism
heterodimer alphabeta Rhodococcus erythropolis

Synonyms

Synonyms Comment Organism
NHase
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Rhodococcus erythropolis
nitrile hydratase
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Rhodococcus erythropolis