Formation of different fatty acid anilides, catalyzed by an enzyme pre
sent in rat liver microsomal fraction, is reported. Oleic acid was fou
nd to be a preferred substrate as compared to palmitic, stearic, linol
eic, linolenic and arachidonic acids. No co-factors were required for
this conjugation reaction and the fatty acid anilide forming activity
was completely inhibited at higher concentration of aniline (200 mM).
The identity of fatty acid anilides formed was confirmed by using chro
matographic and mass spectrometric methods. The anilide forming activi
ty was found to be about 4.5 fold higher for the enzyme purified from
rat pancreas than that from the liver. Apparent K(m) for aniline was f
ound to be 0.019 M, while V(max) was approximately 17 nmol/mg/hr for e
nzyme preparation from digitonin solubilized rat liver microsomes.