1987
DOI: 10.1007/bf00463480
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Catabolite inactivation of isocitrate lyase from Saccharomyces cerevisiae

Abstract: A reversible carbon catabolite inactivation step is described for isocitrate lyase from Saccharomyces cerevisiae. This reversible inactivation step of isocitrate lyase is similar to that described for fructose 1,6-bisphosphatase. Addition of 2,4-dinitrophenol, nystatin or glucose to cultures, grown in ethanol as carbon source, caused a rapid loss of the isocitrate lyase and fructose 1,6-bisphosphatase activities at pH 5.5 but not at pH 7.5. These results suggest that intracellular acidification and thus a cAMP… Show more

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Cited by 51 publications
(38 citation statements)
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“…This degradation process is called catabolite inactivation (3). A similar process was described for cytosolic malate dehydrogenase (cMDH) (4), isocitrate lyase (ICL) (5), and phosphoenolpyruvate carboxykinase (PEPCK) (6). In the case of FBPase, a rapid reversible phosphorylation is involved in the loss of enzymatic activity and followed by a proteolytic breakdown of the enzyme (1,7,8).…”
mentioning
confidence: 86%
“…This degradation process is called catabolite inactivation (3). A similar process was described for cytosolic malate dehydrogenase (cMDH) (4), isocitrate lyase (ICL) (5), and phosphoenolpyruvate carboxykinase (PEPCK) (6). In the case of FBPase, a rapid reversible phosphorylation is involved in the loss of enzymatic activity and followed by a proteolytic breakdown of the enzyme (1,7,8).…”
mentioning
confidence: 86%
“…Most yeast peroxisomal enzymes that function in the glyoxylate pathway, including malate synthase (11) and isocitrate lyase (12), are subject to rapid glucose-induced inactivation and degradation. We therefore investigated this phenomenon for MDH3.…”
Section: Peroxisomal Localization and Expression Of Mdh3-previ-mentioning
confidence: 99%
“…Understanding the mechanisms that induce these enzymes may provide clues about their physiological functions. For example, the activities of isocitrate lyase and malate synthase genes in bacteria and fungi are regulated by metabolite levels; expression of these genes is repressed by carbohydrates or their derivatives and/or activated by acetate or related metabolites (Kornberg, 1966;Lopez-Boado et al, 1987;Chin et al, 1989;Rua et al, 1989;Sanderman and Hynes, 1989; Tolstorukov et al, 1989). Studies have also shown that isocitrate lyase and malate synthase are similarly regulated by metabolite levels in cultured plant cells and protoplasts (Kudielka et al, 1981; Kudielka and Theimer, 1983a, 198313;Graham et al, 1994b).…”
mentioning
confidence: 99%