Abstract
1. 1. A rapid reproducible method for the isolation of substantially pure urocanase from cat liver has been developed. 2. 2. The enzyme has a molecular weight of 127 000 and is isoclectric at pH 5.4. The K m for the urocanase-urocanate complex was 7.1 μM. No evidence could be found for a requirement for pyridoxal phosphate. The enzyme was inhibited by NH 2OH but complete activity was restored after dialysis or gel-permeation chromatography. 3. 3. Only trans-urocanic acid was a substrate for the enzyme. Imidazolylpropionic acid was an effective inhibitor of urocanase; of other analogues tested only imidazolyl-lactic acid and α-chloroimidazolylpropionic acid inhibited the enzyme, and these were much less effective. 4. 4. Possible reaction mechanisms for urocanase are considered, and a tentative picture of the urocanic acid binding site on the enzyme is developed. The contributions to the overall binding of different kinds of forces of interactions at various regions of the urocanic acid molecules are examined.
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