Evidence map›Paper›PMID 19741035›Full record

ArticleDrug metabolism and disposition: the biological fate of chemicals2009

Purification and mechanism of human aldehyde oxidase expressed in Escherichia coli.

Joshua F Alfaro, Carolyn A Joswig-Jones, Wenyun Ouyang, Joseph Nichols, Gregory J Crouch, Jeffrey P Jones

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Drug metabolism and disposition: the biological fate of chemicals, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Enzyme Kinetics, Pharmacokinetics, and Inhibition of Aldehyde Oxidase.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  3. Article
  4. Article
  5. 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 · 2020
    Review
  6. Article
  7. Time Course of Aldehyde Oxidase and Why It Is Nonlinear.Drug metabolism and disposition: the biological fate of chemicals · 2019
    Article
  8. Human Enzymes for Organic Synthesis.Angewandte Chemie (International ed. in English) · 2018
    Review
  9. Article
  10. Article
  11. Article
  12. The mononuclear molybdenum enzymes.Chemical reviews · 2014
    Review
  13. Why do most human liver cytosol preparations lack xanthine oxidase activity?Drug metabolism and disposition: the biological fate of chemicals · 2014
    Article
  14. Article
  15. 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 · 2013
    Article
  16. Article
  17. Article
  18. The impact of single nucleotide polymorphisms on human aldehyde oxidase.Drug metabolism and disposition: the biological fate of chemicals · 2012
    Article
  19. Inhibition of human liver aldehyde oxidase: implications for potential drug-drug interactions.Drug metabolism and disposition: the biological fate of chemicals · 2011
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Joshua F AlfaroDepartment of Chemistry, Washington State University, Pullman, WA 99163, USA.
Carolyn A Joswig-Jones
Wenyun Ouyang
Joseph Nichols
Gregory J Crouch
Jeffrey P Jones
Washington State University · US

Funding

Understanding the Metabolic Impact of Aldehyde Oxidase on New Drug DesignR01GM100874 · NIGMS · WASHINGTON STATE UNIVERSITY · PI JONES, JEFFREY P · 2012 to 2019
$2.6M
Predicting Rates and Regioselectivity in Cytochrome P450 Mediated ReactionsR01GM084546 · NIGMS · WASHINGTON STATE UNIVERSITY · PI JONES, JEFFREY P · 2008 to 2011
$1.4M
NIGMS NIH HHS GM84546NIGMS NIH HHS R01 GM084546NIGMS NIH HHS R01 GM100874
6 · The paper itself

Abstract

Human aldehyde oxidase 1 (AOX1) has been subcloned into a vector suitable for expression in Escherichia coli, and the protein has been expressed. The resulting protein is active, with sulfur being incorporated in the molybdopterin cofactor. Expression levels are modest, but 1 liter of cells supplies enough protein for both biochemical and kinetic characterization. Partial purification is achieved by nickel affinity chromatography through the addition of six histidines to the amino-terminal end of the protein. Kinetic analysis, including kinetic isotope effects and comparison with xanthine oxidase, reveal similar mechanisms, with some subtle differences. This expression system will allow for the interrogation of human aldehyde oxidase structure/function relationships by site-directed mutagenesis and provide protein for characterizing the role of AOX1 in drug metabolism.

Indexed as

Cloning, MolecularAldehyde OxidaseAnimalsCattleChromatography, AffinityEscherichia coliHistidineHumansKineticsMutagenesis, Site-DirectedMutationOligopeptidesRecombinant ProteinsStructure-Activity RelationshipXanthine OxidaseAldehyde OxidaseAOX1 protein, humanHis-His-His-His-His-HisHistidineOligopeptidesRecombinant ProteinsXanthine Oxidase

Identifiers

PMID19741035
PMCPMC2784701
OpenAlexW2135694812

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.