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 == | ||
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</StructureSection> | </StructureSection> | ||
| - | ==3D structures of amino acid oxidase== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *D-amino acid oxidase | ||
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| - | **[[1kif]] – pDAO + FAD – pig<br /> | ||
| - | **[[3wgt]], [[4yjd]], [[4yjf]], [[4yjg]], [[4yjh]] – pDAO (mutant) + FAD<br /> | ||
| - | **[[1c0l]] – RtDAO – ''Rhodosporidium toruloides''<br /> | ||
| - | **[[2e48]] - hDAO – human<br /> | ||
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| - | *D-amino acid oxidase complex | ||
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| - | **[[1dao]] – pDAO + methyl-oxo-valeric acid<br /> | ||
| - | **[[1ddo]] – pDAO + imino-tryptophan<br /> | ||
| - | **[[1an9]] – pDAO + aminobenzoate<br /> | ||
| - | **[[1ve9]] - pDAO + benzoate<br /> | ||
| - | **[[1evi]] – pDAO + dihydro-pyrrolium-carboxylate<br /> | ||
| - | **[[5wwv]], [[5wx2]] - pDAO (mutant) + chlorobenzhydrylamine<br /> | ||
| - | **[[1c0k]] – RtDAO + L-lactate<br /> | ||
| - | **[[1c0p]] – RtDAO + peroxide<br /> | ||
| - | **[[1c0i]] - RtDAO + aminobenzoate<br /> | ||
| - | **[[2du8]] - hDAO + benzoate <br /> | ||
| - | **[[2e4a]] - hDAO + aminobenzoate <br /> | ||
| - | **[[2e49]] - hDAO + iminoserine <br /> | ||
| - | **[[2e82]] - hDAO + imino-DOPA <br /> | ||
| - | **[[3cuk]], [[3w4i]], [[3w4j]], [[3w4k]], [[3znn]], [[3zno]], [[3znp]], [[3znq]], [[4qfc]], [[4qfd]], [[5zj9]], [[5zja]] - hDAO + inhibitor <br /> | ||
| - | **[[3g3e]] - hDAO + hydroxyquinoline<br /> | ||
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| - | *L-amino acid oxidase | ||
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| - | **[[2jae]] – RoLAO – ''Rhodococcus opacus''<br /> | ||
| - | **[[4e0v]] – LAO – ''Bothrops jararacussu''<br /> | ||
| - | **[[1reo]] – HvLAO - Halys viper <br /> | ||
| - | **[[3kve]] – LAO + Zn – ''Vipera ammodytes''<br /> | ||
| - | **[[4cnj]], [[4cnk]] – LAO + FAD – ''Streptococcus oligofermentans''<br /> | ||
| - | **[[5hxv]], [[5i39]] – LAO + FAD - ''Proteus vulgaris'' <br /> | ||
| - | **[[5z2g]] – LAO + FAD – ''Naja atra''<br /> | ||
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| - | *L-amino acid oxidase complex | ||
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| - | **[[1f8r]] – PvLAO + citrate – pit viper<br /> | ||
| - | **[[1f8s]] - PvLAO + aminobenzoate<br /> | ||
| - | **[[1tdk]] – HvLAO + L-vinylglycine <br /> | ||
| - | **[[1tdn]] - HvLAO + L-leucine<br /> | ||
| - | **[[1tdo]] - HvLAO + L-phenylalanine<br /> | ||
| - | **[[2jb1]] - RoLAO + L-alanine<br /> | ||
| - | **[[2jb2]] - RoLAO + L-phenylalanine<br /> | ||
| - | **[[2jb3]] - RoLAO + aminobenzoate<br /> | ||
| - | **[[2iid]] - LAO + L-phenylalanine – ''Calloselasma rhodostoma''<br /> | ||
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| - | *L-amino acid oxidase/monooxigenase | ||
| - | **[[3we0]] - PsLAO + FAD – ''Pseudomonas''<br /> | ||
| - | **[[5yb6]] - PsLAO + FAD + L-lysine<br /> | ||
| - | **[[5yb7]] - PsLAO + FAD + L-ornithine<br /> | ||
| - | **[[5yb8]] - PsLAO + FAD + L-arginine<br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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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
