Abstract
Phosphoribosylpyrophosphate (PRPP) synthetase catalyzes the synthesis of PRPP, a critical substrate common to the de novo and salvage pathways of purine nucleotide synthesis. The PRPP synthetase reaction involves the transfer of the terminal pyrophosphate group of ATP (as a MgATP complex) to the C-1 carbon of ribose-5-P and is dependent on inorganic phosphate (Pi) and Mg2+ which serve as enzyme activators as well as cofactors. Activity of PRPP synthetase is inhibited by a number of phosphorylated compounds including the reaction products (PRPP) and AMP), purine, pyrimidine, and pyridine nucleotides and 2,3-DPG.1 Human PRPP synthetase is composed of a single polypeptide subunit2 the structural gene for which maps to the long arm of the X-chromasome.3 Under appropriate conditions of enzyme and effector concentration in vitro PRPP synthetase subunits are capable of reversible self-association to aggregates containing 2,4,8,16 and 32 subunits, with only the largest two of these containing significant enzyme activity.4
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© 1984 Plenum Press, New York
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Becker, M.A. (1984). Phosphoribosylpyrophosphate Synthetase Superactivity: Detection, Characterization of Underlying Defects, and Treatment. In: De Bruyn, C.H.M.M., Simmonds, H.A., Müller, M.M. (eds) Purine Metabolism in Man-IV. Advances in Experimental Medicine and Biology, vol 165. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4553-4_16
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DOI: https://doi.org/10.1007/978-1-4684-4553-4_16
Publisher Name: Springer, Boston, MA
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