N-Acyl-L-aromatic amino acid deacylase in animal tissues.
An enzyme deacylating preferentially N-acyl-L-aromatic amino acids was partially purified from rat kidney. The purification procedure included DEAE-cellulose column chromatography, (NH4)2SO4 fractionation, gel-filtration on a Sephadex G-200 column and further DEAE-cellulose chromatography. The enzyme was thus separated from aminoacylase (N-acylamino-acid amidohydrolase, EC 3.5.1.14) (acylase I). Although the enzyme preparation contained other acylases, the experimental data (effect of p-chloromercuric benzoate, heat stability and inhibition between substrates) suggest that the enzyme acts preferentially on N-acyl derivatives of L-tryptophan, L-tyrosine, L-phenylalanine and L-histidine. This enzyme appears to be present in many animal tissues.
D000581:Amidohydrolases / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids; D000818:Animals; D002729:Chloromercuribenzoates / Q000494:pharmacology; D006168:Guinea Pigs; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008297:Male; D051379:Mice; D051381:Rats; D013045:Species Specificity; D013379:Substrate Specificity; D013552:Swine; D014018:Tissue Distribution
D000596:Amino Acids; D002729:Chloromercuribenzoates; D000581:Amidohydrolases