Regulation of the amount and of the activity of phosphofructokinases and pyruvate kinases in Escherichia coli.
Two isozymes of fructose-6-phosphate kinase and two isozymes of pyruvate kinase have been detected in Escherichia coli under a wide variety of growth conditions. Their kinetic behavior has been characteriized with respect to different effectors and substrates. The conclusions reached on one hand by Malcovati and Kornberg (Biochim. Biophys. Acta (1969) 178, 420-423), on the other hand by Fraenkel, Kotlarz and Buc (J. Biol. Chem. (1973) 248, 4865-4866) have been found to be true in aerobiosis as well as in anaerobiosis. The biosynthesis of the four proteins is sensitive to the nature of the carbon sources as well as to the shift from aerobic to anaerobic conditions. Kinetics of depression after a shift to anaerobiosis have been followed and found to be of the order of the doubling time.
D000332:Aerobiosis; D000494:Allosteric Regulation; D000693:Anaerobiosis; D004794:Enzyme Repression; D004926:Escherichia coli / Q000201:enzymology* / Q000254:growth & development; D007527:Isoenzymes / Q000096:biosynthesis / Q000378:metabolism*; D007700:Kinetics; D010732:Phosphofructokinase-1 / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D011770:Pyruvate Kinase / Q000096:biosynthesis / Q000378:metabolism*
D007527:Isoenzymes; D010732:Phosphofructokinase-1; D011770:Pyruvate Kinase