Phenylethylaminoalanine (PEAA), derived from biogenic phenylethylamine and dehydroalanine, inhibited the enzymatic activity of the metalloenzyme, carboxypeptidase A (CPA). The inhibition was maximal at pH 7.0 in the pH range 7-8.5. The extent of inhibition increased with time of treatment and PEAA concentration. N-AcetylPEAA did not inhibit the enzyme, suggesting that the free alpha-NH2 group is required for inhibition. PEAA also inactivated the copper enzyme, polyphenol oxidase (tyrosinase). Comparative studies with three other inhibitors, lysinoalanine, ethylenediaminetetraacetic acid and sodium phytate, suggest that the potency of PEAA as an inhibitor of CPA is similar to that of sodium phytate. Of these four inhibitors and three thiol compounds also tested, PEAA was the least and cysteine the most effective against tyrosinase. The pattern of observations in these studies suggests differences in the mechanisms of action of the inhibitors studied. The formation of PEAA, lysinoalanine and sodium phytate in foods is of possible nutritional and toxicological significance.