The Pasteur Effect in Escherichia Coli K-12 Mutants Lacking the Allosteric Form of Phosphofructokinase

Doelle, Horst W.; McIvor, S.

doi:10.1111/j.1574-6941.1980.tb01617.x

Cited by 5 publications

(1 citation statement)

References 19 publications

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“…Accepting that the two enzymes are endowed with regulatory controls which have roughly the same efficiency in vivo [10,30] one can more easily understand why, among different Enterobacteriaceae (or even among different E. coli strains), the distribution of these two enzymes has been found to be so variable.…”

Section: Oligomeric Structure and Regulatory Propertiesmentioning

confidence: 99%

Regulatory Properties of Phosphofructokinase 2 from Escherichia coli

Kotlarz

Buc

1981

European Journal of Biochemistry

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Escherichia coli K12 contains two phosphofructokinases: phosphofructokinase 1, the most studied one, appears to behave as an allosteric enzyme, while phosphofructokinase 2 presents the features of a Michaelian enzyme.We show in the present paper that, in fact, phosphofructokinase 2 also presents some regulatory properties in vitro: at high concentrations, ATP is an inhibitor of phosphofructokinase 2 and it provokes the tetramerization of the dimeric native enzyme.The binding of the two substrates to phosphofructokinase 2 is sequential and ordered as for phosphofructokinase 1, but in the former case fructose 6-phosphate is the first substrate to be bound and ADP the first product to be released. Each dimer of phosphofructokinase 2 binds two molecules of fructose 6-phosphate but only one molecule of the product fructose 1,6-bisphosphate.Although both phosphofructokinases of E. coli K12 present regulatory properties in vitro, the mechanism of regulation of the activity of the two enzymes is strikingly different, It can be asked whether or not these mechanisms operate in vivo.

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Section: Oligomeric Structure and Regulatory Propertiesmentioning

confidence: 99%