Amino acid oxidase

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{{STRUCTURE_2jb1| PDB=2jb1 | SIZE=400| SCENE= |right|CAPTION=Viper L-amino acid oxidase dimer containing FAD complex with L-alanine, [[2jb1]] }}
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<StructureSection load='2jb1' size='400' side='right' scene='48/486454/Cv/1' caption='L-amino acid oxidase dimer containing FAD complex with alanine, [[2jb1]]'>
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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. DAOs oxidize neutral and basic D-amino acids. Some DAOs are used in cancer therapy as inducers of oxidative stress and apoptosis. DAO and LAO use FAD as a cofactor.
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==3D structures of amino acid oxidase==
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== Function ==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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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>
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*'''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>.
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'''D-amino acid oxidase'''
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== Relevance ==
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[[1kif]] – pDAO – pig<br />
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Some DAOs are used in cancer therapy as inducers of oxidative stress and apoptosis. DAO and LAO use FAD as a cofactor.
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[[1c0l]] – RtDAO – ''Rhodosporidium toruloides''<br />
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[[1dao]] – pDAO + methyl-oxo-valeric acid<br />
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[[1ddo]] – pDAO + imino-tryptophan<br />
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[[1an9]] – pDAO + aminobenzoate<br />
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[[1ve9]] - pDAO + benzoate<br />
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[[1evi]] – pDAO + dihydro-pyrrolium-carboxylate<br />
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[[1c0k]] – RtDAO + L-lactate<br />
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[[1c0p]] – RtDAO + peroxide<br />
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[[1c0i]] - RtDAO + aminobenzoate<br />
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'''L-amino acid oxidase'''
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== Structural highlights ==
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LAO structure contains 3 domains: <scene name='48/486454/Cv/5'>FAD-binding, substrate-binding and helical</scene> domains. <scene name='48/486454/Cv/6'>Active site</scene> of L-amino acid oxidase ([[2jb1]]).<ref>PMID:17234209</ref> Water molecules are shown as red spheres.
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==3D structures of amino acid oxidase==
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[[Amino acid oxidase 3D structures]]
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[[2jae]] – RoLAO – ''Rhodococcus opacus''<br />
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</StructureSection>
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[[1f8r]] – CrLAO + citrate – ''Calloselasma rhodostoma''<br />
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[[1f8s]] - CrLAO + aminobenzoate<br />
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[[1tdk]] – HvLAO + L-vinylglycine – Halys viper<br />
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[[1tdn]] - HvLAO + L-leucine<br />
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[[1tdo]] - HvLAO + L-phenylalanine<br />
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[[2jb1]] - RoLAO + L-alanine<br />
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[[2jb2]] - RoLAO + L-phenylalanine<br />
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[[2jb3]] - RoLAO + aminobenzoate<br />
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[[3kve]] – LAO + Zn – Vipera ammodytes
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

L-amino acid oxidase dimer containing FAD complex with alanine, 2jb1

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References

  1. ↑ Du XY, Clemetson KJ. Snake venom L-amino acid oxidases. Toxicon. 2002 Jun;40(6):659-65. PMID:12175601
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

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Michal Harel, Alexander Berchansky

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