| Value |
2.6
mM
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Albe KR, Butler MH, Wright BE. Cellular concentrations of enzymes and their substrates. J Theor Biol. 1990 Mar 22143(2):163-95.PubMed ID2200929
|
| Primary Source |
Lowry OH, Carter J, Ward JB, Glaser L. The effect of carbon and nitrogen sources on the level of metabolic intermediates in Escherichia coli. J Biol Chem. 1971 Nov246(21):6511-21.PubMed ID4257200
|
| Method |
Primary source: Analyses were conducted with 1 ml of reagent in fluorometer tubes (8 X 100 mm) plus neutralized HClO4 extract equivalent to the weight of bacteria indicated. Readings were
made before and after addition of the last enzyme listed. The incubation time refers to this interval. For ATP measurement: Buffer Imidazole-acetate, 200 mM, pH 7.0. Enzyme Glucose-6-P dehydrogenase, 0.25 µg/ml plus hexokinase, 2 µg/ml. Other components TPN+, 30 µM glucose, 100 µM MgCl2,5 mM EDTA, 200 µM. Bacterial equivalent, 100 µg dry weight. Incubation
time 3 min. |
| Comments |
Table 5 in primary source gives values of 4.1 and 4.35 µmoles ATP/g dry weight of E. coli strains K1.1.2.5c and Hfr 139, respectively. For ATP conc. of 9.6mM in glucose-fed, exponentially growing E. coli see BNID 104673 |
| Entered by |
Sudhakaran Prabakaran, Ruchi Chauhan |
| ID |
101181 |