induction and derepression of arginase and ornithine transaminase in different strains of Saccharomyces cerevisiae.
The syntheses of arginase and ornithine transaminase were studied in two strains of Saccharomyces cerevisiae, viz. strain B and strain alpha-sigma 1278b. Derepression of both enzymes during nitrogen starvation was shown only by strain B, non-specific induction of arginase only by strain alpha-sigma 1278b. This different response of both strains studied reveals substantial differences in the regulation of enzyme synthesis among yeast strains of one and the same species. The specific enzyme activities observed in chemostat cultures with arginine as the nitrogen source and different sugars, at variable carbon to nitrogen ratios, did not indicate the involvement of carbon catabolite repression in the regulation of arginase and ornithine transaminase syntheses. Specific arginase activities observed in the continuous cultures varied widely and did not show a correlation with the intracellular arginine concentration. Extracellular steady-state arginine concentrations higher than about 1.0 mM, in addition to abundant energy supply, were found to be required for high production of arginase. It is suggested that, besides intracellular arginine, extracellular arginine may provide an induction signal necessary for full-scale induction of arginase synthesis. A possible intermediary role of arginine permeases or of other membrane proteins is discussed.
D001119:Arginase / Q000096:biosynthesis*; D002244:Carbon / Q000378:metabolism; D004790:Enzyme Induction; D004794:Enzyme Repression; D009584:Nitrogen / Q000378:metabolism; D009953:Ornithine-Oxo-Acid Transaminase / Q000096:biosynthesis*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013045:Species Specificity; D000637:Transaminases / Q000096:biosynthesis*
D002244:Carbon; D000637:Transaminases; D009953:Ornithine-Oxo-Acid Transaminase; D001119:Arginase; D009584:Nitrogen