Kinetic Studies on NADPH-Linked Aldehyde Reductase from Human Liver

  • B. Wermuth
  • J.-P. von Wartburg

Abstract

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.

Keywords

Human Liver Product Inhibition Aldehyde Reductase Horse Liver Deuterium Isotope Effect 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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