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Control of carbon flux through enzymes of central and intermediary metabolism during growth of Escherichia coli on acetate.
Curr Opin Microbiol. 2006 Apr; 9(2):173-9.CO

Abstract

During aerobic growth of Escherichia coli on acetate, the component parts of the 'acetate switch' are turned-on as a consequence of direct competition, on the one hand, between phosphotransacetylase (PTA) and alpha-ketoglutarate dehydrogenase (alpha-KGDH) for their common co-factor free-CoA (HS-CoA) and, on the other hand, between isocitrate lyase (ICL) and isocitrate dehydrogenase (ICDH) for their common substrate isocitrate. Flux analysis revealed that competitions at both junctions in central metabolism are resolved in a precise way, so that the fraction of HS-CoA flux processed through PTA for biosynthesis relative to that processed through alpha-KGDH for energy generation, matches that observed for isocitrate flux through ICL relative to ICDH at the junction of isocitrate. Whereas the mechanism involved in the partition of carbon flux at the level of HS-CoA in central metabolism remains to be unravelled, the competition at the junction of isocitrate is resolved by the reversible phosphorylation/inactivation of ICDH and the operation of the glyoxylate bypass, the expression of which is subject to regulation at the transcriptional and translational levels as well as being dependent on growth rate.

Authors+Show Affiliations

School of Life Sciences, Faculty of Health and Life Sciences, Napier University, Edinburgh, EH10 5DT, Scotland, UK. m.el-mansi@napier.ac.ukNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

16530464

Citation

El-Mansi, Mansi, et al. "Control of Carbon Flux Through Enzymes of Central and Intermediary Metabolism During Growth of Escherichia Coli On Acetate." Current Opinion in Microbiology, vol. 9, no. 2, 2006, pp. 173-9.
El-Mansi M, Cozzone AJ, Shiloach J, et al. Control of carbon flux through enzymes of central and intermediary metabolism during growth of Escherichia coli on acetate. Curr Opin Microbiol. 2006;9(2):173-9.
El-Mansi, M., Cozzone, A. J., Shiloach, J., & Eikmanns, B. J. (2006). Control of carbon flux through enzymes of central and intermediary metabolism during growth of Escherichia coli on acetate. Current Opinion in Microbiology, 9(2), 173-9.
El-Mansi M, et al. Control of Carbon Flux Through Enzymes of Central and Intermediary Metabolism During Growth of Escherichia Coli On Acetate. Curr Opin Microbiol. 2006;9(2):173-9. PubMed PMID: 16530464.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Control of carbon flux through enzymes of central and intermediary metabolism during growth of Escherichia coli on acetate. AU - El-Mansi,Mansi, AU - Cozzone,Alain J, AU - Shiloach,Joseph, AU - Eikmanns,Bernhard J, Y1 - 2006/03/10/ PY - 2005/12/05/received PY - 2006/02/21/accepted PY - 2006/3/15/pubmed PY - 2006/6/9/medline PY - 2006/3/15/entrez SP - 173 EP - 9 JF - Current opinion in microbiology JO - Curr Opin Microbiol VL - 9 IS - 2 N2 - During aerobic growth of Escherichia coli on acetate, the component parts of the 'acetate switch' are turned-on as a consequence of direct competition, on the one hand, between phosphotransacetylase (PTA) and alpha-ketoglutarate dehydrogenase (alpha-KGDH) for their common co-factor free-CoA (HS-CoA) and, on the other hand, between isocitrate lyase (ICL) and isocitrate dehydrogenase (ICDH) for their common substrate isocitrate. Flux analysis revealed that competitions at both junctions in central metabolism are resolved in a precise way, so that the fraction of HS-CoA flux processed through PTA for biosynthesis relative to that processed through alpha-KGDH for energy generation, matches that observed for isocitrate flux through ICL relative to ICDH at the junction of isocitrate. Whereas the mechanism involved in the partition of carbon flux at the level of HS-CoA in central metabolism remains to be unravelled, the competition at the junction of isocitrate is resolved by the reversible phosphorylation/inactivation of ICDH and the operation of the glyoxylate bypass, the expression of which is subject to regulation at the transcriptional and translational levels as well as being dependent on growth rate. SN - 1369-5274 UR - https://www.unboundmedicine.com/medline/citation/16530464/Control_of_carbon_flux_through_enzymes_of_central_and_intermediary_metabolism_during_growth_of_Escherichia_coli_on_acetate_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1369-5274(06)00022-1 DB - PRIME DP - Unbound Medicine ER -