期刊
FEBS LETTERS
卷 586, 期 23, 页码 4114-4118出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.09.042
关键词
Yeast; Phosphoribomutase; Purine nucleotide metabolism
资金
- ANR Blanc [05-2-42128]
The phosphoglucomutases (PGM) Pgm1, Pgm2, and Pgm3 of the yeast Saccharomyces cerevisiae were tested for their ability to interconvert ribose-1-phosphate and ribose-5-phosphate. The purified proteins were studied in vitro with regard to their kinetic properties on glucose-1-phosphate and ribose-1-phosphate. All tested enzymes were active on both substrates with Pgm1 exhibiting only residual activity on ribose-1-phosphate. The Pgm2 and Pgm3 proteins had almost equal kinetic properties on ribose-1-phosphate, but Pgm2 had a 2000 times higher preference for glucose-1-phosphate when compared to Pgm3. The in vivo function of the PGMs was characterized by monitoring ribose-1-phosphate kinetics following a perturbation of the purine nucleotide balance. Only mutants with a deletion of PGM3 hyper-accumulated ribose-1-phosphate. We conclude that Pgm3 functions as the major phosphoribomutase in vivo. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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