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Contribution of cyclic adenosine 3':5'-monophosphate to the regulation of bacterial glycogen synthesis in vivo. Effect of carbon source and cyclic adenosine 3':5'-monophosphate on the quantitative relationship between the rate of glycogen synthesis and the cellular concentrations of glucose 6-phosphate and fructose 1,6-diphosphate in Escherichia coli.
J Biol Chem. 1979 Sep 10; 254(17):8308-17.JB

Abstract

When either fructose, glycerol, or succinate served as a sole source of carbon and energy in nitrogen-starved cultures of Escherichia coli W4597(K) the values of the kinetic constants of the equation that expresses the relationship between glycogen synthesis and hexose phosphates were different from the values observed when glucose was the sole source of carbon and energy. Addition of glucose during either exponential growth or nitrogen starvation to a culture using one of the other carbon sources slowed the rate of glycogen synthesis and shifted the values of the constants toward the values observed in cultures using glucose alone. Addition of cyclic AMP (cyclic adenosine 3':5'-monophosphate) during exponential growth of a culture using glucose caused the values of the constants to be shifted toward the values observed in cultures using a carbon source other than glucose. In all of the metabolic conditions studied in this report the adenylate energy charge ((ATP + 1/2 ADP)/(ATP + ADP + AMP)) and the level of the rate-limiting enzyme of glycogen synthesis, ADP-glucose synthetase (glucose 1-phosphate adenylyltransferase, EC 2.7.7.27), were the same. The data presented here indicate that the difference we observed in the quantitative relationship for glycogen synthesis is the result of the different cellular levels of cyclic AMP in the cells using glucose and the cells using one of the other carbon sources. Since cyclic AMP does not affect the velocity of ADP-glucose synthetase in vitro, apparently a change in the cellular level of cyclic AMP causes a shift in the cellular level of a presently unknown (and previously undetected) effector of this enzyme. The shift in the level of this effector evidently alters the response of the enzyme in vivo to the substrate glucose 1-phosphate and the activator fructose 1,6-diphosphate.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

224050

Citation

Dietzler, D N., et al. "Contribution of Cyclic Adenosine 3':5'-monophosphate to the Regulation of Bacterial Glycogen Synthesis in Vivo. Effect of Carbon Source and Cyclic Adenosine 3':5'-monophosphate On the Quantitative Relationship Between the Rate of Glycogen Synthesis and the Cellular Concentrations of Glucose 6-phosphate and Fructose 1,6-diphosphate in Escherichia Coli." The Journal of Biological Chemistry, vol. 254, no. 17, 1979, pp. 8308-17.
Dietzler DN, Leckie MP, Magnani JL, et al. Contribution of cyclic adenosine 3':5'-monophosphate to the regulation of bacterial glycogen synthesis in vivo. Effect of carbon source and cyclic adenosine 3':5'-monophosphate on the quantitative relationship between the rate of glycogen synthesis and the cellular concentrations of glucose 6-phosphate and fructose 1,6-diphosphate in Escherichia coli. J Biol Chem. 1979;254(17):8308-17.
Dietzler, D. N., Leckie, M. P., Magnani, J. L., Sughrue, M. J., Bergstein, P. E., & Sternheim, W. L. (1979). Contribution of cyclic adenosine 3':5'-monophosphate to the regulation of bacterial glycogen synthesis in vivo. Effect of carbon source and cyclic adenosine 3':5'-monophosphate on the quantitative relationship between the rate of glycogen synthesis and the cellular concentrations of glucose 6-phosphate and fructose 1,6-diphosphate in Escherichia coli. The Journal of Biological Chemistry, 254(17), 8308-17.
Dietzler DN, et al. Contribution of Cyclic Adenosine 3':5'-monophosphate to the Regulation of Bacterial Glycogen Synthesis in Vivo. Effect of Carbon Source and Cyclic Adenosine 3':5'-monophosphate On the Quantitative Relationship Between the Rate of Glycogen Synthesis and the Cellular Concentrations of Glucose 6-phosphate and Fructose 1,6-diphosphate in Escherichia Coli. J Biol Chem. 1979 Sep 10;254(17):8308-17. PubMed PMID: 224050.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Contribution of cyclic adenosine 3':5'-monophosphate to the regulation of bacterial glycogen synthesis in vivo. Effect of carbon source and cyclic adenosine 3':5'-monophosphate on the quantitative relationship between the rate of glycogen synthesis and the cellular concentrations of glucose 6-phosphate and fructose 1,6-diphosphate in Escherichia coli. AU - Dietzler,D N, AU - Leckie,M P, AU - Magnani,J L, AU - Sughrue,M J, AU - Bergstein,P E, AU - Sternheim,W L, PY - 1979/9/10/pubmed PY - 1979/9/10/medline PY - 1979/9/10/entrez SP - 8308 EP - 17 JF - The Journal of biological chemistry JO - J Biol Chem VL - 254 IS - 17 N2 - When either fructose, glycerol, or succinate served as a sole source of carbon and energy in nitrogen-starved cultures of Escherichia coli W4597(K) the values of the kinetic constants of the equation that expresses the relationship between glycogen synthesis and hexose phosphates were different from the values observed when glucose was the sole source of carbon and energy. Addition of glucose during either exponential growth or nitrogen starvation to a culture using one of the other carbon sources slowed the rate of glycogen synthesis and shifted the values of the constants toward the values observed in cultures using glucose alone. Addition of cyclic AMP (cyclic adenosine 3':5'-monophosphate) during exponential growth of a culture using glucose caused the values of the constants to be shifted toward the values observed in cultures using a carbon source other than glucose. In all of the metabolic conditions studied in this report the adenylate energy charge ((ATP + 1/2 ADP)/(ATP + ADP + AMP)) and the level of the rate-limiting enzyme of glycogen synthesis, ADP-glucose synthetase (glucose 1-phosphate adenylyltransferase, EC 2.7.7.27), were the same. The data presented here indicate that the difference we observed in the quantitative relationship for glycogen synthesis is the result of the different cellular levels of cyclic AMP in the cells using glucose and the cells using one of the other carbon sources. Since cyclic AMP does not affect the velocity of ADP-glucose synthetase in vitro, apparently a change in the cellular level of cyclic AMP causes a shift in the cellular level of a presently unknown (and previously undetected) effector of this enzyme. The shift in the level of this effector evidently alters the response of the enzyme in vivo to the substrate glucose 1-phosphate and the activator fructose 1,6-diphosphate. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/224050/Contribution_of_cyclic_adenosine_3':5'_monophosphate_to_the_regulation_of_bacterial_glycogen_synthesis_in_vivo__Effect_of_carbon_source_and_cyclic_adenosine_3':5'_monophosphate_on_the_quantitative_relationship_between_the_rate_of_glycogen_synthesis_and_the_cellular_concentrations_of_glucose_6_phosphate_and_fructose_16_diphosphate_in_Escherichia_coli_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(19)86890-4 DB - PRIME DP - Unbound Medicine ER -