Enzymic degradation of uridine diphosphoacetylglucosamine

Abstract

Uridine diphosphoacetylglucosamine is shown to undergo a hydrolytic cleavage by an enzyme present in sheep brain. The products of the reaction are identified as N-acetylglucosaminei-phosphate and UMP. The enzyme responsible for this degradation has a wide distribution in the tissues of the rat. ATP, UTP, ADP and N-acetylglucosaminei-phosphate act as powerful inhibitors of this enzyme. The enzyme requires Co²⁺ for its maximal activity. It shows a broad optimal range of pH from 8–9. The enzyme preparation cleaves uridine diphosphoglucose and uridine diphosphoglucuronic acid to lesser extents than uridine diphosphoacetylglucosamine.