• Citer

Arginine metabolism in Saccharomyces cerevisiae: Subcellular localization of the enzymes

par Jauniaux, Jean Claude ;Urrestarazu, Luis ;Wiame, Jean-Marie
Référence Journal of bacteriology, 133, 3, page (1096-1107)
Publication Publié, 1978

Article révisé par les pairs

• Détails
• Contenu

Résumé :

Subcellular localization of enzymes of arginine metabolism in S. cerevisiae was studied by partial fractionation and stepwise homogenization of spheroplast lysates. These enzymes could clearly be divided into two groups. The first group comprised the five enzymes of the acetylated compound cycle, i.e., acetylglutamate synthase, acetylglutamate kinase, acetylglutamyl-phosphate reductase, acetylornithine aminotransferase, and acetylornithine-glutamate acetyltransferase. These enzymes are exclusively particulate. Comparison with citrate synthase and cytochrome oxidase. and results from isopycnic gradient analysis, suggested that these enzymes were associated with the mitochondria. By contrast, enzymatic activities going from ornithine to arginine, i.e. arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the 'soluble' fraction of the cell.