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CHARACTERIZATION OF ENZYMES HYDROLYZING ACYL NAPHTHYLAMIDES III. ROLE OF KYNURENINE FORMAMIDASE

V. K. HOPSU 1, R. SANTTI 1, and G. G. GLENNER 1

1 Department of Anatomy, University of Turku, Turku, Finland, and Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland

An enzyme fraction in guinea pig liver catalyzing the hydrolysis of chloroacetyl agr-naphthylamide was separated by gel filtration and demonstrated to hydrolyze N-formyl-l-kynurenine. On the basis of relative substrate hydrolysis rates, the enzymes in this peak were shown to have the characteristics of kynurenine formamidase, an enzyme catalyzing the transformation of N-formyl-l-kynurenine to l-kynurenine and formic acid. The histochemical localization in fixed tissue of the hydrolysis of chloroacetyl agr-naphthylamide can be almost totally ascribed to this enzyme and, thereby, indicates tissue sites of tryptophan catabolism.

Submitted on February 28, 1966


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