Xanthine Dehydrogenase and Pteridine Metabolism in Colias Butterflies
Ward B. Watt 1
From the
1 From the Department of Biological Sciences, Stanford University, Stanford, California 94305
It is shown that an enzyme from Colias butterflies, oxidizing the yellow pteridine xanthopterin to the colorless pteridine leucopterin, is in fact xanthine dehydrogenase. Methods for the partial purification of the enzyme are given. The enzyme oxidizes a number of purines and pteridines effectively, with NAD+ as cosubstrate. It is inhibited competitively by its products of reaction, leucopterin and uric acid, and by the precursor of xanthopterin, 7,8-dihydroxanthopterin. A model is constructed for the regulation of portions of the Colias pteridine pathway during ontogeny, incorporating both product and "feed forward" inhibition of xanthine dehydrogenase as shown here.
Submitted on October 6, 1971