Enzymic degradation of uridine diphosphoacetylglucosamine

Pattabiraman, T. N. ; Sekhara Varma, T. N. ; Bachhawat, B. K. (1964) Enzymic degradation of uridine diphosphoacetylglucosamine Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides, 83 (1). pp. 74-83. ISSN 0926-6526

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/092665...

Related URL: http://dx.doi.org/10.1016/0926-6526(64)90053-9


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-acetylglucosamine I-phosphate and UMP. The enzyme responsible for this degradation has a wide distribution in the tissues of the rat. ATP, UTP, ADP and N-acetylglucosamine I-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.

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