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Catabolite inactivation of isocitrate lyase fromSaccharomyces cerevisiae

✍ Scribed by Y. S. López-Boado; P. Herrero; S. Gascón; F. Moreno

Publisher
Springer
Year
1987
Tongue
English
Weight
417 KB
Volume
147
Category
Article
ISSN
0302-8933

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✦ Synopsis

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 increase is involved in the catabolite inactivation mechanism of both enzymes. From results obtained by addition of glucose to yeast cultures at pH 7.5 it was concluded that others factors than cAMP can play a role in the catabolite inactivation mechanism of both enzymes.

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