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Related Experiment Videos

Lactate dehydrogenases in cyanobacteria.

J J Sanchez, N J Palleroni, M Doudoroff

    Archives of Microbiology
    |June 20, 1975
    PubMed
    Summary

    This study investigates NAD-linked D-lactate dehydrogenase in cyanobacteria. The enzyme is crucial for D-lactate metabolism, with its activity varying with culture age.

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    Area of Science:

    • Biochemistry
    • Microbiology
    • Photosynthesis

    Background:

    • Unicellular cyanobacteria possess NAD-linked lactate dehydrogenases for D- and L-lactate.
    • Understanding these enzymes is key to cyanobacterial metabolic pathways.

    Purpose of the Study:

    • To partially purify and characterize NAD-linked D-lactate dehydrogenase from Synechococcus 6716.
    • To investigate the physiological roles of D-lactate dehydrogenase in cyanobacterial metabolism.

    Main Methods:

    • Partial purification of D-lactate dehydrogenase.
    • Enzyme property analysis (molecular weight, specificity, inhibition).
    • Metabolic studies using radiolabeled D-lactate and glucose, and analysis of end products.

    Main Results:

    • The D-lactate dehydrogenase (ca. 115-120 kDa) is specific, autooxidizable, and inhibited by iodoacetamide, oxamate, and ATP.
    • D-lactate carbon incorporated into cell material during photosynthesis; lactate not a sole carbon source.
    • Aerobic oxidation of D-lactate and pyruvate in the dark, with acetate excretion. D-lactate detected in endogenous metabolism.
    • Enzymes for lactate production from glucose/glycogen present, but activity declines in older cultures.

    Conclusions:

    • D-lactate dehydrogenase plays a role in cyanobacterial carbon metabolism, particularly during active growth.
    • Enzyme activity is regulated by culture age, suggesting metabolic shifts in cyanobacteria.

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