Kinetic Studies on NADPH-Linked Aldehyde Reductase from Human Liver

  • B. Wermuth
  • J.-P. von Wartburg


The mechanism of D-glucuronate reduction by human liver NADPH-dependent aldehyde reductase was investigated. At pH 7.4 the Km values for NADPH, NADP+, D-glucuronate and L-gulonate were 2.2 μM, 6 μM, 3.2 mM and 6 mM, respectively. Product inhibition studies in the forward direction (reduction of glucuronate) gave a competitive pattern for the inhibition of NADPH oxidation by NADP+ and non-competitive patterns for the other three inhibitions. In the backward direction all patterns appeared to be competitive. Deuterium isotope effects were dependent on the concentration of D-glucuronate and decreased to unity at infinite concentrations of D-glucuronate. Our findings suggest for aldehyde reductase a kinetic mechanism with sequential ordered binding of NADPH and D-glucuronate and random dissociation of NADP+ and L-gulonate.


Human Liver Product Inhibition Aldehyde Reductase Horse Liver Deuterium Isotope Effect 
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Copyright information

© Springer Science+Business Media New York 1980

Authors and Affiliations

  • B. Wermuth
    • 1
  • J.-P. von Wartburg
    • 1
  1. 1.University of BernSwitzerland

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