@article{mbs:/content/journal/micro/10.1099/00221287-93-1-69, author = "Higa, Azucena I. and de Forchetti, Silvia R. Milrad and Cazzulo, J. J.", title = "CO2-fixing Enzymes in Pseudomonas fluorescens", journal= "Microbiology", year = "1976", volume = "93", number = "1", pages = "69-74", doi = "https://doi.org/10.1099/00221287-93-1-69", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-93-1-69", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Summary: Pseudomonas fluorescens grown on glucose or glutamate at 1 or 20 °, or on acetate at 20 °, as sole carbon sources, contained both pyruvate carboxylase and phosphoenolpyruvate carboxylase. Pyruvate carboxylase was insensitive to acetylcoenzyme A and l-aspartate, and its level in cell-free extracts was markedly dependent on the carbon source for growth, the highest specific activity being attained in glucose-grown cells. Phosphoenolpyruvate carboxylase, on the other hand, although less dependent on the nature of the carbon source, showed its highest level in acetate-grown cells; the enzyme activity required acetyl-coenzyme A and was strongly inhibited by l-aspartate. The micro-organism had, in addition, a phosphoenolpyruvate carboxykinase, which showed its highest specific activity in cells grown on acetate, and a NADP-linked malate enzyme, apparently repressed by acetate and showing its highest specific activity in glutamate-grown cells.", }