Involvement of the glucose enzymes II of the sugar phosphotransferase system in the regulation of adenylate cyclase by glucose in escherichia coli

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dc.contributor.authorHarwood, J.P.
dc.contributor.authorGazdar, C.
dc.contributor.authorPrasad, Chandan
dc.contributor.authorPeterkofsky, A.
dc.contributor.authorCurtis, S.J.
dc.contributor.authorEpstein, W.
dc.creator.orcidhttps://orcid.org/0000-0001-9870-7626
dc.date.accessioned2023-04-12T19:01:22Z
dc.date.available2023-04-12T19:01:22Z
dc.date.issued1976
dc.descriptionArticle originally published in Journal of Biological Chemistry, 251(8), 2462–2468. English. Published Online 2021. https://doi.org/10.1016/s0021-9258(17)33610-4
dc.description.abstractThe nature of the interaction of glucose with toluene-treated cells of Escherichia coli leading to inhibition of adenylate cyclase was examined by the use of analogues. Those analogues with variations of the substituents about carbon atoms 1 or 2 (e.g. alpha-methylglucoside or 2-deoxyglucose) are inhibitory, and they are also substrates of the phosphoenolpyruvate-dependent sugar phosphotransferase system. Analogues with changes in other parts of the molecule (e.g. 3-O-methylglucose or galactose), L-glucose and several disaccharides and pentoses, do not inhibit adenylate cyclase and are not substrates of the phosphotransferase system. This correlation suggests some functional relationship between the adenylate cyclase and phosphotransferase systems. Further studies were done with mutants defective in glucose enzymes II of the phosphotransferase system (designated GPT and MPT); these two activities are measured by phosphorylation of alpha-methyl-glucoside and 2-deoxyglucose, respectively. The wild-type parent phosphorylates both analogues, and both inhibit adenylate cyclase. In the GPT- mutant, alpha-methylglucoside does not inhibit adenylate cyclase and is not phosphorylated, while 2-deoxyglucose is inhibitory and phosphorylated. In the GPT- MPT- double mutant, adenylate cyclase activity is present, but neither alpha-methylglucoside nor 2-deoxyglucose inhibits adenylate cyclase, and neither sugar is phosphorylated. These studies demonstrate that glucose inhibition of adenylate cyclase in toluene-treated cells requires an interaction of this sugar with either the GPT or mpt enzyme II of the phosphotransferase system.en_US
dc.identifier.citationThis is the published version of an article that is available at https://doi.org/10.1016/s0021-9258(17)33610-4. Recommended citation: Harwood, J. P., Gazdar, C., Prasad, C., Peterkofsky, A., Curtis, S. J., & Epstein, W. (1976). Involvement of the glucose enzymes II of the sugar phosphotransferase system in the regulation of adenylate cyclase by glucose in escherichia coli. Journal of Biological Chemistry, 251(8), 2462–2468. This item has been deposited in accordance with publisher copyright and licensing terms and with the author’s permission.en_US
dc.identifier.urihttps://hdl.handle.net/11274/14818
dc.identifier.urihttps://doi.org/10.1016/s0021-9258(17)33610-4
dc.language.isoen_USen_US
dc.publisherElsevieren_US
dc.rights.licenseCC BY-NC-ND
dc.subjectInduction of enzyme synthesisen_US
dc.subjectCatabolite repressionen_US
dc.subjectAdenylate cyclase activityen_US
dc.titleInvolvement of the glucose enzymes II of the sugar phosphotransferase system in the regulation of adenylate cyclase by glucose in escherichia colien_US
dc.typeArticleen_US

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