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Originally published In Press as doi:10.1074/jbc.M211692200 on January 13, 2003

J. Biol. Chem., Vol. 278, Issue 12, 10264-10272, March 21, 2003
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Ser3p (Yer081wp) and Ser33p (Yil074cp) Are Phosphoglycerate Dehydrogenases in Saccharomyces cerevisiae*

Eva AlbersDagger §, Vincent Laizé||, Anders Blomberg, Stefan Hohmann, and Lena GustafssonDagger

From the Dagger  Department of Molecular Biotechnology, Chalmers University of Technology, Box 462, SE-405 30 Göteborg, Sweden and the  Department of Cell and Molecular Biology-Microbiology, Göteborg University, Box 462, SE-405 30 Göteborg, Sweden

Two genes YER081W and YIL074C, renamed SER3 and SER33, respectively, which encode phosphoglycerate dehydrogenases in Saccharomyces cerevisiae were identified. These dehydrogenases catalyze the first reaction of serine and glycine biosynthesis from the glycolytic metabolite 3-phosphoglycerate. Unlike either single mutant, the ser3Delta ser33Delta double mutant lacks detectable phosphoglycerate dehydrogenase activity and is auxotrophic for serine or glycine for growth on glucose media. However, the requirement for the SER-dependent "phosphoglycerate pathway" is conditional since the "glyoxylate" route of serine/glycine biosynthesis is glucose-repressed. Thus, in cells grown on ethanol both expression and activity of all SER-encoded proteins are low, including the remaining enzymes of the phosphoglycerate pathway, Ser1p and Ser2p. Moreover the available nitrogen source regulates the expression of SER genes. However, for only SER33, and not SER3, expression was regulated in relation to the available nitrogen source in a coordinated fashion with SER1 and SER2. Based on these mRNA data together with data on enzyme activities, Ser33p is likely to be the main isoenzyme of the phosphoglycerate pathway during growth on glucose. Moreover, since phosphoglycerate dehydrogenase activity requires NAD+ as cofactor, deletion of SER3 and SER33 markedly affected redox metabolism as shown by substrate and product analysis.

* This work was financially supported by the Swedish National Energy Administration (Energimyndigheten).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed. Tel.: 46-31-773-2598; Fax: 46-31-773-2599; E-mail: Eva.Albers@molbiotech.chalmers.se.

|| Present address: Universidade do Algarve, Centro de Ciências do Mar, Campus de Gambelas, P-8000-117 Faro, Portugal.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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