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Glutamate as an inhibitor of phosphoenolpyruvate carboxylase activity in Corynebacterium glutamicum

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Journal of Industrial Microbiology and Biotechnology

Abstract

The glutamate-producing bacterium, Corynebacterium glutamicum is known to possess two anaplerotic enzymes: pyruvate carboxylase (Pc) and phosphoenolpyruvate carboxylase (PEPc). In vitro, this latter enzyme appeared to be inhibited by different glutamic acid salts, whereas ammonium-glutamate had no influence on Pc activity. To investigate the in vivo relevance of PEPc activity inhibition, the intracellular concentration of glutamate was determined throughout the glutamate-producing process. The intracellular concentration was then shown to be sufficient to induce a dramatic inhibition of PEPc activity during the process. As a consequence, intracellular accumulation of glutamate could be at least partially responsible for the weak participation of PEPc within the anaplerosis activity in amino-acid-producing strains of C. glutamicum.

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Acknowledgements

This work was supported by the CNRS (GdR 1157 and 1597 and Programme Interdisciplinaire de Recherche en Génie des Procédés).

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Correspondence to Stéphane Delaunay.

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Delaunay, S., Daran-Lapujade, P., Engasser, JM. et al. Glutamate as an inhibitor of phosphoenolpyruvate carboxylase activity in Corynebacterium glutamicum . J IND MICROBIOL BIOTECHNOL 31, 183–188 (2004). https://doi.org/10.1007/s10295-004-0137-6

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  • DOI: https://doi.org/10.1007/s10295-004-0137-6

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