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Inhibition of Aldehyde Reductase by Carboxylic Acids

  • Bendicht Wermuth
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 284)

Abstract

Aldehyde reductase (EC 1.1.1.2) and aldose reductase (EC 1.1.1.21) are structurally related, monomeric oxidoreductases that catalyze the NADPH-dependent reduction of a variety of aliphatic, aromatic and sugar aldehydes. For most substrates Km values of aldose reductase are one to two orders of magnitude lower than those of aldehyde reductase. Exceptions are anionic aldehydes, e.g. succinic semialdehyde, 4-carboxybenzaldehyde and glucuronate, which are metabolized much more efficiently by aldehyde than aldose reductase. The partiality of aldehyde reductase for negatively charged substrates has been attributed to the presence of an anion binding site, most probably an arginine residue, in the substrate binding domain of the active site (Davidson and Flynn, 1979; Branlant et al., 1981; Bohren et al., 1987).

Keywords

Valproic Acid Aldose Reductase Arginine Residue Aldose Reductase Inhibitor Succinic Semialdehyde 
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

© Plenum Press, New York 1990

Authors and Affiliations

  • Bendicht Wermuth
    • 1
  1. 1.Chemisches ZentrallaborInselspitalBernSwitzerland

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