Abstract
Enzymes of proline biosynthesis and proline degradation which act on the same compound, delta 1-pyrroline-5-carboxylate, are physically separated in yeast cells. The enzyme responsible for the final step in proline biosynthesis, pyrroline-5-carboxylate reductase, converts pyrroline-5-carboxylate to proline and is located in the cytoplasm. The last enzyme in the proline degradative pathway, pyrroline-5-carboxylate dehydrogenase, converts pyrroline-5-carboxylate to glutamate and is found in the particulate fraction of the cell, presumably in the mitochondrion. By subcellular compartmentation, yeast cells avoid futile cycling between proline and pyrroline-5-carboxylate.
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Selected References
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- Brandriss M. C. Isolation and preliminary characterization of Saccharomyces cerevisiae proline auxotrophs. J Bacteriol. 1979 Jun;138(3):816–822. doi: 10.1128/jb.138.3.816-822.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brandriss M. C., Magasanik B. Genetics and physiology of proline utilization in Saccharomyces cerevisiae: enzyme induction by proline. J Bacteriol. 1979 Nov;140(2):498–503. doi: 10.1128/jb.140.2.498-503.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brandriss M. C., Magasanik B. Proline: an essential intermediate in arginine degradation in Saccharomyces cerevisiae. J Bacteriol. 1980 Sep;143(3):1403–1410. doi: 10.1128/jb.143.3.1403-1410.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Clifton D., Weinstock S. B., Fraenkel D. G. Glycolysis mutants in Saccharomyces cerevisiae. Genetics. 1978 Jan;88(1):1–11. doi: 10.1093/genetics/88.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Davis R. H. Compartmentation and regulation of fungal metabolism: genetic approaches. Annu Rev Genet. 1975;9:39–65. doi: 10.1146/annurev.ge.09.120175.000351. [DOI] [PubMed] [Google Scholar]
- JOHNSON A. B., STRECKER H. J. The interconversion of glutamic acid and proline. IV. The oxidation of proline by rat liver mitochondria. J Biol Chem. 1962 Jun;237:1876–1882. [PubMed] [Google Scholar]
- Jauniaux J. C., Urrestarazu L. A., Wiame J. M. Arginine metabolism in Saccharomyces cerevisiae: subcellular localization of the enzymes. J Bacteriol. 1978 Mar;133(3):1096–1107. doi: 10.1128/jb.133.3.1096-1107.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MIDDELHOVEN W. J. THE PATHWAY OF ARGININE BREAKDOWN IN SACCHAROMYCES CEREVISIAE. Biochim Biophys Acta. 1964 Dec 9;93:650–652. doi: 10.1016/0304-4165(64)90349-6. [DOI] [PubMed] [Google Scholar]
- Ryan E. D., Kohlhaw G. B. Subcellular localization of isoleucine-valine biosynthetic enzymes in yeast. J Bacteriol. 1974 Nov;120(2):631–637. doi: 10.1128/jb.120.2.631-637.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ryan E. D., Tracy J. W., Kohlhaw G. B. Subcellular localization of the leucine biosynthetic enzymes in yeast. J Bacteriol. 1973 Oct;116(1):222–225. doi: 10.1128/jb.116.1.222-225.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Scarpulla R. C., Soffer R. L. Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization. J Biol Chem. 1978 Sep 10;253(17):5997–6001. [PubMed] [Google Scholar]