Amino acid oxidase
From Proteopedia
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'''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.<ref>PMID:12175601</ref> DAOs oxidize neutral and basic D-amino acids.<ref>PMID:17396222</ref> | '''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.<ref>PMID:12175601</ref> DAOs oxidize neutral and basic D-amino acids.<ref>PMID:17396222</ref> | ||
| + | *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<ref>PMID:29511608</ref>. | ||
== Relevance == | == Relevance == | ||
Revision as of 09:11, 23 May 2024
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References
- ↑ 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:http://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:http://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:http://dx.doi.org/10.1016/j.jmb.2006.11.071
