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Prostaglandin 15-hydroxy dehydrogenase from human placenta.

W Schlegel, R O Greep

    European Journal of Biochemistry
    |August 1, 1975
    PubMed
    Summary

    Human placenta prostaglandin 15-hydroxy dehydrogenase, crucial for inactivating prostaglandins, was purified. Kinetic analysis revealed a sequential ordered mechanism for rapid prostaglandin degradation and prevention of accumulation.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Human Physiology

    Background:

    • Prostaglandins are biologically active lipids involved in numerous physiological processes.
    • Prostaglandin 15-hydroxy dehydrogenase (PGDH) enzyme plays a critical role in prostaglandin metabolism by catalyzing their inactivation.
    • Understanding PGDH's kinetics is essential for elucidating prostaglandin homeostasis and potential therapeutic interventions.

    Purpose of the Study:

    • To purify and characterize human placental prostaglandin 15-hydroxy dehydrogenase (PGDH).
    • To investigate the enzyme kinetics, including substrate interactions and inhibition patterns.
    • To elucidate the catalytic mechanism of PGDH.

    Main Methods:

    • Purification of prostaglandin 15-hydroxy dehydrogenase from human placenta (1270-fold).
    • Kinetic studies using prostaglandin E2 and NAD+ as substrates.
    • Determination of kinetic constants (Km, Ki, Vmax) and equilibrium constant.
    • Analysis of inhibition by 15-ketoprostaglandin E2 and 13,14-dihydro-15-ketoprostaglandin E2.
    • Isoelectric focusing to determine the enzyme's isoelectric point.

    Main Results:

    • Purified PGDH exhibits Michaelis constants (Km) of 1 μM for prostaglandin E2 and 44 μM for NAD+.
    • The enzyme is non-competitively inhibited by 15-ketoprostaglandin E2 and 13,14-dihydro-15-ketoprostaglandin E2.
    • Kinetic data support a sequential ordered catalytic mechanism, excluding random, ping-pong, and Theorell-Chance mechanisms.
    • The isoelectric point of PGDH was determined to be pH 5.35.

    Conclusions:

    • Human placental PGDH is efficiently purified and characterized.
    • The enzyme operates via a sequential ordered mechanism, contributing to controlled prostaglandin degradation.
    • These findings provide insights into the regulation of prostaglandin levels in vivo.

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