ArticlePloS one2009
Site directed mutagenesis of amino acid residues at the active site of mouse aldehyde oxidase AOX1.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Review
- Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes.The Journal of biological chemistry · 2020Review
- Molybdenum-Containing Enzymes.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities.PloS one · 2018Article
- ecoAO: A Simple System for the Study of Human Aldehyde Oxidases Role in Drug Metabolism.ACS omega · 2017Article
- Interspecies differences in the metabolism of methotrexate: An insight into the active site differences between human and rabbit aldehyde oxidase.Biochemical pharmacology · 2015Article
- The four aldehyde oxidases of Drosophila melanogaster have different gene expression patterns and enzyme substrate specificities.The Journal of experimental biology · 2014Article
- The mononuclear molybdenum enzymes.Chemical reviews · 2014Review
- 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
- Identification of crucial amino acids in mouse aldehyde oxidase 3 that determine substrate specificity.PloS one · 2013Article
- The first mammalian aldehyde oxidase crystal structure: insights into substrate specificity.The Journal of biological chemistry · 2012Article
- The impact of single nucleotide polymorphisms on human aldehyde oxidase.Drug metabolism and disposition: the biological fate of chemicals · 2012Article
- Genetic association mapping identifies single nucleotide polymorphisms in genes that affect abscisic acid levels in maize floral tissues during drought.Journal of experimental botany · 2011Article
- The mammalian aldehyde oxidase gene family.Human genomics · 2009Article
- Purification and mechanism of human aldehyde oxidase expressed in Escherichia coli.Drug metabolism and disposition: the biological fate of chemicals · 2009Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mouse aldehyde oxidase (mAOX1) forms a homodimer and belongs to the xanthine oxidase family of molybdoenzymes which are characterized by an essential equatorial sulfur ligand coordinated to the molybdenum atom. In general, mammalian AOs are characterized by broad substrate specificity and an yet obscure physiological function. To define the physiological substrates and the enzymatic characteristics of mAOX1, we established a system for the heterologous expression of the enzyme in Escherichia coli. The recombinant protein showed spectral features and a range of substrate specificity similar to the native protein purified from mouse liver. The EPR data of recombinant mAOX1 were similar to those of AO from rabbit liver, but differed from the homologous xanthine oxidoreductase enzymes. Site-directed mutagenesis of amino acids Val806, Met884 and Glu1265 at the active site resulted in a drastic decrease in the oxidation of aldehydes with no increase in the oxidation of purine substrates. The double mutant V806E/M884R and the single mutant E1265Q were catalytically inactive enzymes regardless of the aldehyde or purine substrates tested. Our results show that only Glu1265 is essential for the catalytic activity by initiating the base-catalyzed mechanism of substrate oxidation. In addition, it is concluded that the substrate specificity of molybdo-flavoenzymes is more complex and not only defined by the three characterized amino acids in the active site.
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