An extensive literature exists concerning the role of tyrosine and tyrosinase in the formation of melano-pigments. This interest reflects the widespread distribution of the enzyme and the conspicuousness of such pigments in man, animals, and plants. Several comprehensive reviews exist on these pigments and the various factors which influence their formation (Raper, 1928; Lerner and Fitzpatrick, 1950; Dawson and Tarpley, 1951). Much of the emphasis has been directed to the metabolism of tyrosine, an amino acid which plays an important role in melanopigmentation. The formation of these darkly colored products from their precursors is a complex phenomenon, and detailed information concerning their identity and the sequence of chemical reactions which transform tyrosine to pigmented products is also incomplete. Bacterium salmonicida, a pathogen of salmonoid fishes, produces a dark amber to brown-black pigment especially when grown on a tryptic digest of casein-yeast extract medium (Gutsell and Snieszko, 1949). Griffin (1952) reported that only a light brown color was produced in nutrient agar and that the addition of L-phenylalanine or L-tyrosine resulted in the formation of a deep amber pigment. The present report deals largely with the effect of compounds structurally related to tyrosine and phenylalanine on pigment formation. These studies suggest that B. salmonicida may be a convenient tool for investigating the nature and formation of pigments derived from phenylalanine and tyrosine.