Molecular cloning studies have revealed the existence of two additional genes that encode phosphoribosyl pyrophosphate synthetase-like proteins, one widely expressed (phosphoribosyl pyrophosphate synthetase 2) and one whose expression appears to be confined to the testis (phosphoribosyl pyrophosphate synthetase 1-like 1) (Taira et al. 1989; 1991). Neither of these proteins has been purified and characterized enzymatically, nor have variations in the abundance or sequence of either protein been associated with alterations in human nucleotide metabolism (Roessler et al. 1993; Becker et al. 1996), so their dimerization and ability to catalyze the synthesis of PRPP from D-ribose 5-phosphate are inferred here on the basis of their predicted amino acid sequence similarity to phosphoribosyl pyrophosphate synthetase 1.
Tatibana, M, Yamada, K, Shimada, H, Taira, M, Iizasa, T
Fox, IH, Kelley, WN
Deuel, TF, Roth, DG, Shelton, E
Ahmed, M, Taylor, W, Smith, PR, Becker, MA
Kim, M, Becker, MA
Kudoh, J, Tatibana, M, Shimizu, N, Shimada, H, Taira, M, Iizasa, T
Smith, PR, Switzer, RL, Heidler, SA, Becker, MA, Palella, TD, Roessler, BJ, Nosal, JM
Simms, ES, Kornberg, A, Lieberman, I
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