Subcellular compartmentation in control of converging pathways for proline and arginine metabolism in Saccharomyces cerevisiae

J Bacteriol. 1981 Mar;145(3):1359-64. doi: 10.1128/jb.145.3.1359-1364.1981.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 1-Pyrroline-5-Carboxylate Dehydrogenase
  • Arginine / metabolism
  • Cell Compartmentation*
  • Cytoplasm / enzymology
  • Mitochondria / enzymology
  • Oxidoreductases Acting on CH-NH Group Donors / metabolism*
  • Proline / metabolism*
  • Pyrroline Carboxylate Reductases / metabolism*
  • Saccharomyces cerevisiae / enzymology*

Substances

  • Arginine
  • Proline
  • 1-Pyrroline-5-Carboxylate Dehydrogenase
  • Oxidoreductases Acting on CH-NH Group Donors
  • Pyrroline Carboxylate Reductases