Aldehyde oxidase

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Aldehyde oxidase
Aldehyde oxidase
Belt model according to PDB  4UHW

Available structure data : 4UHW , 4UHX

Properties of human protein
Mass / length primary structure 1338 amino acids
Secondary to quaternary structure Homodimer
Cofactor Molybdopterin , FAD , 2 (2Fe-2S)
Identifier
Gene names AOX1 AO
External IDs
Enzyme classification
EC, category 1.2.3.1 ,  oxidoreductase
Response type Addition of an oxygen atom
Substrate Aldehyde + O 2 + H 2 O
Products Carboxylic acid + H 2 O 2
Occurrence
Homology family AOX / XDH
Parent taxon Euteleostomi
Orthologue (human)
Entrez 316
Ensemble ENSG00000138356
UniProt Q06278
Refseq (mRNA) NM_001159
Refseq (protein) NP_001150
Gene locus Chr 2: 200.59 - 200.68 Mb
PubMed search 316

Aldehyde oxidase (AOX1) is an enzyme in vertebrates that catalyzes the breakdown of aldehydes . It is also known that AOX1 oxidizes nicotine to cotinine . AOX1 is therefore important for the Tryptophan - metabolism and biotransformation . In humans, the enzyme is located in the cytosol of liver cells , but can also be found in the lungs , skeletal muscles , pancreas and fat cells .

AOX1 is homologous to xanthine dehydrogenase , with which it was previously confused. AOX1 deficiency is a factor in the rare molybdenum cofactor deficiency . In humans, only one produces AOX - Gene a functional enzyme, unlike other vertebrates.

In adipocytes , AOX1 is apparently indispensable for adipogenesis and the release of adiponectin , as was concluded from cell studies. In hepatocytes , AOX1 is downregulated by adiponectin. Since it is co-expressed with the ABCA 1 transporter, AOX1 deficiency leads to reduced lipid export from the cells due to ABCA1 deficiency.

Individual evidence

  1. ↑ UniProt Q06278
  2. ↑ Metacyc Enzyme: Aldehyde oxidase
  3. ↑ Terao M, Kurosaki M, Barzago MM, et al. : Avian and canine aldehyde oxidases. Novel insights into the biology and evolution of molybdo-flavoenzymes . In: J. Biol. Chem. . 281, No. 28, July 2006, pp. 19748-61. doi : 10.1074 / jbc.M600850200 . PMID 16672219 .
  4. ↑ Weigert J, Neumeier M, Bauer S, et al. : Small-interference RNA-mediated knock-down of aldehyde oxidase 1 in 3T3-L1 cells impairs adipogenesis and adiponectin release . In: FEBS Lett . . 582, No. 19, August 2008, pp. 2965-72. doi : 10.1016 / j.febslet.2008.07.034 . PMID 18671973 .
  5. ↑ Neumeier M, Weigert J, Schäffler A, et al. : Aldehyde oxidase 1 is highly abundant in hepatic steatosis and is downregulated by adiponectin and fenofibric acid in hepatocytes in vitro . In: Biochem. Biophys. Res. Commun. . 350, No. 3, November 2006, pp. 731-5. doi : 10.1016 / j.bbrc.2006.09.101 . PMID 17022944 .
  6. ↑ Sigruener A, Buechler C, Orsó E, et al. : Human aldehyde oxidase 1 interacts with ATP-binding cassette transporter-1 and modulates its activity in hepatocytes . In: Horm. Metab. Res. . 39, No. 11, November 2007, pp. 781-9. doi : 10.1055 / s-2007-992129 . PMID 17992631 .

Web links

Wikibooks: Biochemistry and Pathobiochemistry: Tryptophan Metabolism  - Learning and Teaching Materials

Biochemistry and molecular biology of molybdenum metabolism in plants and humans