THE enzyme 5-carboxymethylhydantoinase, which reversibly cyclized carbamylaspartate to 5-carboxymethylhydantoin, was demonstrated in Zymobacterium oroticum by Lieberman and Kornberg1. No enzymatic activity was found in rat liver or in two corynebacterium strains2. In recent studies on pyrimidine metabolism in man this enzyme was found to be absent in erythrocytes and normal or leukæmic leukocytes3,4. The absence of this enzyme in mammalian cells and its presence in bacteria suggested the possibility that chemotherapeutic agents might be developed as competitive inhibitors of 5-carboxy-methylhydahtoinase. Inhibition of the growth of Lactobacillus casei by thiohydantoin-5-acetic acid has been reported5. A survey of the distribution of the enzyme in micro-organisms was therefore undertaken.