title: Energy-dependent inactivation of citrate lyase in Enterobacter aerogenes.
abstract: Enterobacter aerogenes was grown in continous culture with ammonia as the growth-limiting substrate, and changes in citrate lyase and citrate synthase activities were monitored after growth shifts from anaerobic growth on citrate to aerobic growth on citrate, aerobic growth on glucose, anaerobic growth on glucose, and anaerobic growth on glucose plus nitrate. Citrate lyase was inactivated during aerobic growth on glucose and during anaerobic growth with glucose plus nitrate. Inactivation did not occur during anaerobic growth on glucose, and as a result of the simultaneous presence of citrate lyase and citrate synthase, growth difficulties were observed. Citrate lyase inactivation consisted of deacetylation of the enzyme. The corresponding deacetylase could not be demonstrated in cell extracts, and it is concluded that, as in a number of other inactivations, electron transport to oxygen or nitrate was required for inactivation.
mesh_terms: D000332:Aerobiosis; D000693:Anaerobiosis; D001149:Arsenates / Q000494:pharmacology; D002701:Chloramphenicol / Q000494:pharmacology; D002951:Citrates / Q000378:metabolism; D004579:Electron Transport; D004754:Enterobacter / Q000201:enzymology*; D004755:Enterobacteriaceae / Q000201:enzymology*; D005947:Glucose / Q000378:metabolism; D009566:Nitrates / Q000378:metabolism; D007652:Oxo-Acid-Lyases / Q000378:metabolism*; D014475:Uncoupling Agents / Q000494:pharmacology
chemical_list: D001149:Arsenates; D002951:Citrates; D009566:Nitrates; D014475:Uncoupling Agents; D002701:Chloramphenicol; D007652:Oxo-Acid-Lyases; D005947:Glucose