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- W1981129465 abstract "Acetate-grown Bacillus megaterium KM possessed high isocitrate lyase and malate synthase activity as compared to glucose-grown cells. Chloramphenicol prevented the increase in isocitrate lyase activity when cells were transferred from glucose to acetate media, indicating that such an increase in activity was probably due to de novo protein synthesis.The affinity of the substrate, isocitrate, was greater for isocitrate dehydrogenase than for isocitrate lyase. Phosphoenolpyruvate was found to inhibit isocitrate lyase non-competitively. The concerted action of glyoxylate and oxaloacetate was capable of inhibiting isocitrate dehydrogenase. The role such factors play in the balancing of the tricarboxylic acid cycle and the glyoxylate pathway in the microorganism is considered." @default.
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- W1981129465 date "1970-12-01" @default.
- W1981129465 modified "2023-09-26" @default.
- W1981129465 title "Metabolic activity of acetate-grown Bacillus megaterium KM" @default.
- W1981129465 doi "https://doi.org/10.1139/m70-202" @default.
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