Characterization of a nitrilase from Nocardia sp. (Rhodochrous group) N.C.I.B. 11215, using p-hydroxybenzonitrile as sole carbon source.
The purification and properties of an enzyme from Nocardia sp. which catalyses the conversion of p-hydroxybenzonitrile to p-hydroxybenzoic acid and ammonia without intermediate formation of the amide is described. The enzyme displayed a broad pH optimum between 7.0 and 9.5 and exhibited Michaelis-Menten kinetics with Km of 1.27 mM for p-hydroxybenzonitrile. The 12-unit multimeric enzyme possessed a mol. wt of 560,000 and was sensitive to thiol-specific reagents. Although aliphatic nitriles were not substrates for the enzyme a broad range of substituted aromatic nitriles were attacked with a general preference being shown for those with meta substitution.
D000619:Aminohydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009615:Nocardia / Q000201:enzymology* / Q000254:growth & development; D010101:Oxygen Consumption; D010636:Phenols / Q000378:metabolism*; D013379:Substrate Specificity
D046911:Macromolecular Substances; D010636:Phenols; C007178:4-cyanophenol; D000619:Aminohydrolases; C021867:nitrilase