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CO2-fixing enzymes in Pseudomonas fluorescens

A I Higa, S R Milrad de Forchetti, J J Cazzulo

    Journal of General Microbiology
    |March 1, 1976
    PubMed
    Summary

    Pseudomonas fluorescens utilizes different carbon sources, influencing key carboxylase enzymes. Enzyme levels varied with growth conditions, impacting metabolic pathways.

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    Area of Science:

    • Microbiology
    • Enzymology
    • Metabolic Biochemistry

    Background:

    • Pseudomonas fluorescens is a versatile bacterium known for its metabolic flexibility.
    • Carboxylase enzymes play crucial roles in carbon assimilation and anaplerosis.
    • Understanding enzyme regulation is key to comprehending bacterial metabolism.

    Purpose of the Study:

    • To investigate the presence and regulation of key carboxylase enzymes in Pseudomonas fluorescens.
    • To determine the influence of different carbon sources and growth temperatures on enzyme activity.
    • To elucidate the specific roles of pyruvate carboxylase, phosphoenolpyruvate carboxylase, phosphoenolpyruvate carboxykinase, and malate enzyme in Pseudomonas fluorescens.

    Main Methods:

    • Growth of Pseudomonas fluorescens on sole carbon sources: glucose, glutamate, and acetate at varying temperatures (1°C and 20°C).
    • Assay of cell-free extracts for pyruvate carboxylase, phosphoenolpyruvate carboxylase, phosphoenolpyruvate carboxykinase, and NADP-linked malate enzyme activities.
    • Determination of enzyme sensitivity to effectors like acetyl-coenzyme A and L-aspartate.

    Main Results:

    • Both pyruvate carboxylase and phosphoenolpyruvate carboxylase were detected across tested conditions.
    • Pyruvate carboxylase activity was highest in glucose-grown cells and insensitive to acetyl-CoA and L-aspartate.
    • Phosphoenolpyruvate carboxylase activity was highest in acetate-grown cells, requiring acetyl-CoA and inhibited by L-aspartate.
    • Phosphoenolpyruvate carboxykinase activity was highest in acetate-grown cells.
    • NADP-linked malate enzyme activity was highest in glutamate-grown cells and repressed by acetate.

    Conclusions:

    • Pseudomonas fluorescens possesses multiple carboxylase systems, suggesting metabolic adaptability.
    • The regulation of these enzymes is significantly influenced by the carbon source used for growth.
    • Differential expression and regulation of these enzymes allow Pseudomonas fluorescens to optimize carbon metabolism under diverse environmental conditions.

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