Abstract
PRPP is a substrate in the synthesis of virtually all nucleotides1 and is also an important regulator of the de novo pathways of purine2 and pyrimidine3 nucleotide synthesis. Formation of PRPP is catalyzed in eukaryotes by a family of PRPP synthetase (PRS; EC2.7.6.1) isoforms.4–6 The substrates in the reaction are MgATP and Rib-5-P, and Mg2+ and P1 are essential activators. Inhibitors of PRS activity include: purine, pyrimidine, and pyridine nucleotides; reaction products; and 2,3-diphosphoglycerate.4,5,7 Human erythrocyte PRS is composed of a polypeptide subunit of 34.5 kD which undergoes concentration-dependent and effector-mediated reversible aggregation in vitro to active forms of 16 and 32 subunits.4,8 The primary structure and kinetic and physical properties of purified human erythrocyte PRS are those of the purified recombinant PRS 1 isoform.
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Becker, M.A., Taylor, W., Smith, P.R., Ahmed, M. (1998). Regulation of Human PRS Isoform Expression. In: Griesmacher, A., Müller, M.M., Chiba, P. (eds) Purine and Pyrimidine Metabolism in Man IX. Advances in Experimental Medicine and Biology, vol 431. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5381-6_42
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DOI: https://doi.org/10.1007/978-1-4615-5381-6_42
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