Abstract
Phosphoribosylpyrophosphate (PRPP) synthetase (E.C. 2.7.6.1) catalyzes the formation of PRPP from ribose-5-phosphate and ATP in the presence of Mg++ and inorganic phosphate. The product, PRPP, is a substrate of the first rate limiting step of the de novo synthesis of purine nucleotides and its availability has been shown to regulate this pathway in human tissue (1). A superactive mutant erythrocyte PRPP synthetase with decreased sensitivity to feedback inhibition has recently been found by us in a gouty family (2,3).
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© 1974 Springer Science+Business Media New York
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Boer, P., Sperling, O., de Vries, A. (1974). Electrophoretic Separation of Normal and Mutant Phosphoribosylpyrophosphate Synthetase. In: Sperling, O., De Vries, A., Wyngaarden, J.B. (eds) Purine Metabolism in Man. Advances in Experimental Medicine and Biology, vol 41. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-1433-3_59
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DOI: https://doi.org/10.1007/978-1-4757-1433-3_59
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