caa a22 4500 397555970 CHVBK 20180308164802.0 cr unu---uuuuu 161202e199601 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021205 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021205 Escherichia coli Phosphorylates 1,5-Anhydroglucitol and Releases 1,5-Anhydroglucitol 6-Phosphate When Glucose Is Absent in the Medium [Elektronische Daten] [Yoko Shiga, Shunichi Kametani, Hideaki Mizuno, Hiroshi Akanuma] The cyclic polyol 1,5-anhydro-D-glucitol (AG) is detected in most organisms, but little is known about its metabolism and physiological roles. Our previous study demonstrated thatEscherichia coliC600 synthesizes AG when glucose is exhausted in the medium and that it temporarily releases AG into and then takes it back from the medium, thus forming a sharp peak in AG concentration in the medium a few hours after reaching stationary growth phase. The present study demonstrates that when glucose is absent in the culture medium, E. coli C600 takes up and phosphorylates AG and releases a large portion of it back into the medium in the form of a phosphate ester. [U-13C]AG was added to the medium after the exhaustion of glucose and the resulting [U-13C]AG phosphate was partially purified by several steps of anion exchange chromatography and identified as AG 6-phos-phate by 13C-NMR. The identity of the phosphate ester was also confirmed by GC-MS analysis after further purification. © by the Journal of Biochemistry Regular Papers nationallicence 1,5-anhydro-D-glucitol nationallicence 13C-NMR nationallicence E. coli nationallicence phosphorylation nationallicence sugar metabolism nationallicence Shiga Yoko Department of Life Science (Chemistry), Graduate School of Arts and Sciences, The University of Tokyo, Kornaba, Meguro-ku, Tokyo 153 aut Kametani Shunichi Department of Life Science (Chemistry), Graduate School of Arts and Sciences, The University of Tokyo, Kornaba, Meguro-ku, Tokyo 153 aut Mizuno Hideaki Department of Life Science (Chemistry), Graduate School of Arts and Sciences, The University of Tokyo, Kornaba, Meguro-ku, Tokyo 153 aut Akanuma Hiroshi Department of Life Science (Chemistry), Graduate School of Arts and Sciences, The University of Tokyo, Kornaba, Meguro-ku, Tokyo 153 aut The Journal of Biochemistry Oxford University Press 119/1(1996-01), 173-179 0021-924X 119:1<173 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021205 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021205 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Shiga Yoko Department of Life Science (Chemistry), Graduate School of Arts and Sciences, The University of Tokyo, Kornaba, Meguro-ku, Tokyo 153 aut NATIONALLICENCE 700 1- Kametani Shunichi Department of Life Science (Chemistry), Graduate School of Arts and Sciences, The University of Tokyo, Kornaba, Meguro-ku, Tokyo 153 aut NATIONALLICENCE 700 1- Mizuno Hideaki Department of Life Science (Chemistry), Graduate School of Arts and Sciences, The University of Tokyo, Kornaba, Meguro-ku, Tokyo 153 aut NATIONALLICENCE 700 1- Akanuma Hiroshi Department of Life Science (Chemistry), Graduate School of Arts and Sciences, The University of Tokyo, Kornaba, Meguro-ku, Tokyo 153 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/1(1996-01), 173-179 0021-924X 119:1<173 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford