ABSTRACT
The nitrile hydratase from Rhodococcus equi A4 consisted of two kinds of subunits which slightly differed in molecular weight (both approximately 25 kDa) and showed a significant similarity in the N-terminal amino acid sequences to those of the nitrile hydratase from Rhodococcus sp. N-774. The enzyme preferentially hydrated the S-isomers of racemic 2-(2-, 4-methoxyphenyl)propionitrile, 2-(4-chlorophenyl)propionitrile and 2-(6-methoxynaphthyl)propionitrile (naproxennitrile) with E-values of 5-15. The enzyme functioned in the presence of 5-98% (v/v) of different hydrocarbons, alcohols or diisopropyl ether. The addition of 5% (v/v) of n-hexane, n-heptane, isooctane, n-hexadecane, pristane and methanol increased the E-value for the enzymatic hydration of 2-(6-methoxynaphthyl)propionitrile.
Subject(s)
Hydro-Lyases/isolation & purification , Hydro-Lyases/metabolism , Nitriles/metabolism , Rhodococcus equi/enzymology , Amino Acid Sequence , Hydro-Lyases/chemistry , Hydrocarbons/pharmacology , Hydrogen-Ion Concentration , Isoelectric Point , Methanol/pharmacology , Molecular Weight , Protein Subunits , Solvents/pharmacology , Stereoisomerism , Substrate Specificity , TemperatureABSTRACT
From a mixture of lysergamide and its epimer isolysergamide, Rhodococcus equi A4 containing amidase preferentially hydrolyzed lysergamide into lysergic acid.
