ArticleDrug metabolism and disposition: the biological fate of chemicals2011
Inhibition of human liver aldehyde oxidase: implications for potential drug-drug interactions.
Article in Drug metabolism and disposition: the biological fate of chemicals, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 53 citations in OpenAlex.
- Roles of selected non-P450 human oxidoreductase enzymes in protective and toxic effects of chemicals: review and compilation of reactions.Archives of toxicology · 2022Review
- Enzyme Kinetics, Pharmacokinetics, and Inhibition of Aldehyde Oxidase.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes.The Journal of biological chemistry · 2020Review
- Effects of Phenothiazines on Aldehyde Oxidase Activity Towards Aldehydes and N-Heterocycles: an In Vitro and In Silico Study.European journal of drug metabolism and pharmacokinetics · 2019Article
- ecoAO: A Simple System for the Study of Human Aldehyde Oxidases Role in Drug Metabolism.ACS omega · 2017Article
- Article
- Evaluating the Disposition of a Mixed Aldehyde Oxidase/Cytochrome P450 Substrate in Rats with Attenuated P450 Activity.Drug metabolism and disposition: the biological fate of chemicals · 2016Article
- Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase.Nature chemical biology · 2015Article
- Interspecies differences in the metabolism of methotrexate: An insight into the active site differences between human and rabbit aldehyde oxidase.Biochemical pharmacology · 2015Article
- A novel reaction mediated by human aldehyde oxidase: amide hydrolysis of GDC-0834.Drug metabolism and disposition: the biological fate of chemicals · 2015Article
- Inhibition of human aldehyde oxidase activity by diet-derived constituents: structural influence, enzyme-ligand interactions, and clinical relevance.Drug metabolism and disposition: the biological fate of chemicals · 2015Article
- Potential role of cardiac calsequestrin in the lethal arrhythmic effects of cocaine.Drug and alcohol dependence · 2013Article
- Evaluation of rhesus monkey and guinea pig hepatic cytosol fractions as models for human aldehyde oxidase.Drug metabolism and disposition: the biological fate of chemicals · 2013Article
- Predicting intrinsic clearance for drugs and drug candidates metabolized by aldehyde oxidase.Molecular pharmaceutics · 2013Article
- Evidence for substrate-dependent inhibition profiles for human liver aldehyde oxidase.Drug metabolism and disposition: the biological fate of chemicals · 2013Article
- The first mammalian aldehyde oxidase crystal structure: insights into substrate specificity.The Journal of biological chemistry · 2012Article
- Aldehyde oxidase functions as a superoxide generating NADH oxidase: an important redox regulated pathway of cellular oxygen radical formation.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
During the course of our research efforts to understand the kinetics of human aldehyde oxidase as a xenobiotic-clearing enzyme, we investigated the effect of eight different inhibitors on the oxidation of the probe substrate phthalazine. Saturation kinetic parameters for phthalazine oxidation in human liver cytosol were found to be the following: K(m) = 8.0 ± 0.4 μM and V(max) = 4.3 ± 0.1 nmol · min(-1) · mg protein(-1). Inhibitory potency of the inhibitors tested ranged from 0.1 to 5 μM. Of the eight different inhibitor compounds tested, seven were observed to inhibit through a mixed mode and one through a strictly competitive mode. A ratio of the K(ii) and K(is) values was used to assess the relative competitiveness of each inhibitor. For the mixed inhibitors, the mode of inhibition varied from mostly uncompetitive to predominantly competitive (K(ii)/K(is) values ranging from 0.1 to 15). The implications for potential drug-drug interactions and inhibition mechanism are discussed. We found two inhibitors, clozapine and chlorpromazine, that have a moderate predicted risk of drug-drug interactions based on the K(i) value relative to the inhibitor concentration in human plasma, having a calculated [I]/K(i) value of 0.4 and 0.8, respectively.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.