Involvement of pyruvate dehydrogenase in product formation in pyruvate-limited anaerobic chemostat cultures of Enterococcus faecalis NCTC 775 |
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| Authors: | Jacky L Snoep M Joost Teixeira de Mattos Pieter W Postma Oense M Neijssel |
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| Institution: | (1) Department of Microbiology, Biotechnology Centre, University of Amsterdam, P. O. Box 20245, 1000 HE Amsterdam, The Netherlands;(2) E. C. Slater Institute for Biochemical Research, Biotechnology Centre, University of Amsterdam, Amsterdam, The Netherlands |
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| Abstract: | Enterococcus faecalis NCTC 775 was grown anaerobically in chemostat culture with pyruvate as the energy source. At low culture pH values, high in vivo and in vitro activities were found for both pyruvate dehydrogenase and lactate dehydrogenase. At high culture pH values the carbon flux was shifted towards pyruvate formate lyase. Some mechanisms possibly involved in this metabolic switch are discussed. In particular attention is paid to the NADH/NAD ratio (redox potential) and the fructose-1,6-bisphosphate-dependent lactate dehydrogenase activity as possible regulatory factors.Abbreviations PDH
pyruvate dehydrogenase complex (EC 1.2.2.2)
- PFL
pyruvate formate lyase (EC 2.3.1.54)
- LDH
lactate dehydrogenase (EC 1.1.1.27)
- FBP
fructose-1,6-bisphosphate
- MTT
3-(4,5-dimethyl-thiazoyl-2)-2,5-diphenyltetrazolium bromide
- TPP
thiamine pyrophosphate |
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| Keywords: | Enterococcus faecalis Chemostat culture Pyruvate dehydrogenase NADH/NAD Redox potential Fructose-1 6-bisphosphate Carbon metabolism |
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