Summary
The enzyme lactate dehydrogenase (LDH) in Clostridium thermohydrosulfuricum is controlled by the type and the concentration of the substrate. In batch fermentations an increase of the initial concentration of glucose leads to an increase in the activity of LDH. This increase in activity is related to the accumulation of fructose 1,6-diphosphate (F 1,6-DP), an intermediate of the Embden-Meyerhof-Parnas (EMP) pathway, which stimulates the enzyme by increasing its affinity for pyruvate and NADH. The K mvalues of LDH for pyruvate and NADH, which are 2.5×10-3 M and 9.1×10-5 M respectively in absence of F 1,6-DP, fall considerably in the presence of this substrate. In presence of 0.2 mM of F 1,6-DP we observed a K mof 3.3×10-4 M for pyruvate and 4.1×10-5 M for NADH.
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Germain, P., Toukourou, F. & Donaduzzi, L. Ethanol production by anaerobic thermophilic bacteria: regulation of lactate dehydrogenase activity in Clostridium thermohydrosulfuricum . Appl Microbiol Biotechnol 24, 300–305 (1986). https://doi.org/10.1007/BF00257053
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DOI: https://doi.org/10.1007/BF00257053