Function
Amino acid oxidase catalyzes the oxidation of amino acids to the keto acid producing ammonia and hydrogen peroxide. These enzymes oxidize D-amino acids (DAO) and L-amino acids (LAO). The LAO oxidation products are 2-oxo acid, ammonia and hydrogen peroxide. LAO is widely found in snake venom.[1] DAOs oxidize neutral and basic D-amino acids.[2]
- L-amino acid oxidase/monooxigenase catalyzes both the oxidative deamination and oxidative decarboxylation of the alpha group of L-Lys producing keto acid and amide[3].
Relevance
Some DAOs are used in cancer therapy as inducers of oxidative stress and apoptosis. DAO and LAO use FAD as a cofactor.
Structural highlights
LAO structure contains 3 domains: FAD-binding, substrate-binding and helical domains. Active site of L-amino acid oxidase (2jb1).[4] Water molecules are shown as red spheres.
3D structures of amino acid oxidase
Amino acid oxidase 3D structures
- ↑ Du XY, Clemetson KJ. Snake venom L-amino acid oxidases. Toxicon. 2002 Jun;40(6):659-65. PMID:12175601
- ↑ Pollegioni L, Piubelli L, Sacchi S, Pilone MS, Molla G. Physiological functions of D-amino acid oxidases: from yeast to humans. Cell Mol Life Sci. 2007 Jun;64(11):1373-94. PMID:17396222 doi:https://dx.doi.org/10.1007/s00018-007-6558-4
- ↑ Im D, Matsui D, Arakawa T, Isobe K, Asano Y, Fushinobu S. Ligand complex structures of l-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 and its conformational change. FEBS Open Bio. 2018 Feb 8;8(3):314-324. doi: 10.1002/2211-5463.12387. eCollection, 2018 Mar. PMID:29511608 doi:https://dx.doi.org/10.1002/2211-5463.12387
- ↑ Faust A, Niefind K, Hummel W, Schomburg D. The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation. J Mol Biol. 2007 Mar 16;367(1):234-48. Epub 2006 Dec 1. PMID:17234209 doi:https://dx.doi.org/10.1016/j.jmb.2006.11.071
