1973
DOI: 10.1016/0003-9861(73)90321-4
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Rates of glycogen synthesis and the cellular levels of ATP and FDP during exponential growth and the nitrogen-limited stationary phase of Escherichia coli W4597 (K)

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Cited by 49 publications
(29 citation statements)
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“…ADP-pyrophosphorylase is activated by fructose 1,6-bisphosphate Figure 9. Ef (Preiss et al, 1975), whose intracellular from Takahas level is high under glucose-excess and nitrogen source-limiting conditions (Dietzler et al, 1973). On the other hand, the ADP-glucose pyrophosphorylase is inhibited by ADP, AMP, and/or Pi (Preiss and Romeo, 1989), whose levels are expected to be high under glucose-limiting conditions.…”
Section: (Viic) Phmentioning
confidence: 99%
“…ADP-pyrophosphorylase is activated by fructose 1,6-bisphosphate Figure 9. Ef (Preiss et al, 1975), whose intracellular from Takahas level is high under glucose-excess and nitrogen source-limiting conditions (Dietzler et al, 1973). On the other hand, the ADP-glucose pyrophosphorylase is inhibited by ADP, AMP, and/or Pi (Preiss and Romeo, 1989), whose levels are expected to be high under glucose-limiting conditions.…”
Section: (Viic) Phmentioning
confidence: 99%
“…The physiological energy charge range in various E. coli strains is found to be 0.74-0.9 (69,73). The physiological concentrations of fructose-P2 ranges between 0.71 and 3 m M (68,69). Under these conditions the C L l l 3 6 enzyme shows maximal activity and is not sensitive either to change in energy charge or to fluctuations of fructose-P2.…”
Section: Table Xi1mentioning
confidence: 99%
“…Dietzler et al (68,69) have shown that when the growth of E. coli W4597(K) ceased because of NH,+ depletion, the rate of glycogen accumulation increased about 3.3-to 4.2-fold. Concomitant with this, a decrease of fructose-P2 of about 76% (from 3.1 to 0.71 mM) and an increase in the energy charge from 0.74 in exponential phase to 0.87 in stationary phase occurred (68,69).…”
Section: B Kelationships Of Fructose-pz Concentrations and Energy Chmentioning
confidence: 99%
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