Catabolite repression during single and multiple induction in Escherichia coli.
Intracellular concentration of cAMP regulates the synthesis of enzymes sensitive to catabolite repression. The relationship between the single and multiple induction of beta-galactosidase (EC 3.2.1.23), L-tryptophanase (EC 4.1.99.1), D-serine deaminase (EC 4.2.1.14), L-asparaginase (EC 3.5.1.1) and L-malate dehydrogenase (EC 1.1.1.37) was studied and the effect of cAMP level on the induction in Escherichia coli Crookes (ATCC 8739) was investigated. A varying degree of catabolite repression was observed during induction of individual enzymes induced separately on different energy sources. The synthesis of l-tryptophanase was most sensitive, whereas l-asparaginase was not influenced at all. Exogenous cAMP was found to overcome partially the catabolite repression of beta-galactosidase and D-serine deaminase, both during single induction. The synthesis of l-malate dehydrogenase was negatively influenced by the multiple induction even in the presence of cAMP; on the other hand, the synthesis of l-tryptophanase was stimulated, independently of the level of the exogenous cAMP. Similarly, the activity of L-asparaginase slightly but significantly increased during the multiple induction of all five enzymes; here too the activity increase did not depend on exogenous cAMP.
D001215:Asparaginase / Q000096:biosynthesis; D000242:Cyclic AMP / Q000494:pharmacology*; D004790:Enzyme Induction / Q000187:drug effects; D004794:Enzyme Repression / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology*; D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase; D012695:L-Serine Dehydratase / Q000096:biosynthesis; D008291:Malate Dehydrogenase / Q000096:biosynthesis; D014368:Tryptophanase / Q000096:biosynthesis; D001616:beta-Galactosidase / Q000096:biosynthesis
D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase; D000242:Cyclic AMP; D008291:Malate Dehydrogenase; D001616:beta-Galactosidase; D001215:Asparaginase; D014368:Tryptophanase; D012695:L-Serine Dehydratase