Biochemical and Biophysical Research Communications
Regular ArticleTwo Different Enzymes Are Primarily Responsible for Retinoic Acid Synthesis in Rabbit Liver Cytosol
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Critical overview on the structure and metabolism of human aldehyde oxidase and its role in pharmacokinetics
2018, Coordination Chemistry ReviewsCitation Excerpt :Similarly, tamoxifen (not in Table 3) is bio-transformed into an aldehyde intermediate by a monoamine oxidase, which is subsequently recognized and further metabolized by rat liver AOX enzymatic activity. Several potentially physiological relevant aldehydes that are substrates of AOX (reviewed in [4]) are 5-hydroxyindoleacetaldehyde, a serotonin oxidation metabolite, retinaldehyde [89–91] and pyridoxal, the dephosphorylated form of the active vitamin B6 metabolite [92,93]. Pyridoxal is an established substrate of aldehyde oxidases being of particular relevance in insects.
Xanthine Oxidoreductase and Aldehyde Oxidases
2018, Comprehensive Toxicology: Third EditionPharmacological inhibition of ALDH1A in mice decreases all-trans retinoic acid concentrations in a tissue specific manner
2015, Biochemical PharmacologyCitation Excerpt :In support of an enzyme other than an ALDH1A, WIN 18,446 only inhibited approximately 50% of the atRA formation by liver S10 protein. Previous work has demonstrated that AOX forms atRA from at-retinal [53] and contributes to approximately 50% of the atRA formation from at-retinal in the rabbit liver cytosol [54]. In agreement with this, the AOX inhibitor hydralazine inhibited approximately 50% of the mouse liver atRA formation suggesting a much greater importance of AOX in atRA formation in mice than previously suggested [30].
In vitro oxidation of aldehyde oxidase from rabbit liver: Specificity toward endogenous substrates
2014, Journal of King Saud University - ScienceCitation Excerpt :Pyridoxal is currently the sole example of a substrate that shows a certain degree of selectivity for a specific aldehyde oxidase protein as it is not recognized by purified mouse (Terao et al., 2009). These findings are consistent with Huang and Ichikawa (1994) and Tsujita et al. (1994) who first observed the role of AO in the oxidation of all-trans-retinaldehyde to retinoic acid without NAD+ in rabbit by liver AO cytosol (Huang and Ichikawa, 1994; Tsujita et al., 1994). Km and Vmax values for the formation of 4-pyridoxic acid and retinoic acid metabolites, also determined spectrophotometrically as described in Methods, by rabbit enzyme fractions are tabulated in Table 3 and Figs. 3 and 4.
Effect of tea beverages on aldehyde oxidase activity
2011, Drug Metabolism and Pharmacokinetics