Substrate properties of a number of potentially fluorogenic
aromatic aldehydes of naphthalenes, phenanthrenes and anthracenes and of
some coumarin aldehydes towards various forms of the human and rat aldehyde
oxidase and dehydrogenase were examined using absorption and emission
spectroscopy. It was demonstrated that recombinant human class 1 aldehyde
dehydrogenase (ALDH-1) readily oxidizes naphthalene (except for those
ortho-substituted), phenanthrene and coumarin aldehydes, whereas
the class 3 enzyme (ALDH-3) from human saliva is active only towards
2-naphthaldehyde derivatives. The observed reaction rates in both cases are
comparable to those of the best known substrates, and the
Km values are typically in the sub-micromolar range.
Aldehyde oxidases (AlOx), which are present in mammalian liver, reveal much
broader substrate specificity, oxidizing nearly all the compounds examined,
including those of the anthracene series, with maximum activity in the
micromolar range of substrate concentration. In rat liver, nearly all AlOx
activity was located in the cytosolic fraction.
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