Amino acid oxidase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:13, 23 May 2024) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_2jb1| PDB=1f8s | SIZE=400| SCENE= |right|CAPTION=Pit viper L-amino acid oxidase dimer containing FAD complex with aminobenzoate, [[1f8s]] }}
+
<StructureSection load='2jb1' size='400' side='right' scene='48/486454/Cv/1' caption='L-amino acid oxidase dimer containing FAD complex with alanine, [[2jb1]]'>
-
<!--
+
__TOC__
-
Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
+
-
Or use the four-green-boxes-button to insert scrollable text adjacent
+
-
to a Jmol applet. Check out the other buttons as well!
+
-
-->
+
== Function ==
== 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. DAOs oxidize neutral and basic D-amino acids.
+
'''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 ==
Line 16: Line 13:
== Structural highlights ==
== Structural highlights ==
-
LAO structure contains 3 domains: FAD-binding, substrate-binding and helical domains. Active site residues include E209 and R90.
+
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.
==3D structures of amino acid oxidase==
==3D structures of amino acid oxidase==
 +
[[Amino acid oxidase 3D structures]]
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
</StructureSection>
-
{{#tree:id=OrganizedByTopic|openlevels=0|
+
-
*D-amino acid oxidase
+
== References ==
-
 
+
<references/>
-
**[[1kif]] – pDAO – pig<br />
+
-
**[[3wgt]] – pDAO (mutant)<br />
+
-
**[[1c0l]] – RtDAO – ''Rhodosporidium toruloides''<br />
+
-
**[[2e48]] - hDAO – human<br />
+
-
 
+
-
*D-amino acid oxidase complex
+
-
 
+
-
**[[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 />
+
-
**[[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]] - hDAO + inhibitor <br />
+
-
**[[3g3e]] - hDAO + hydroxyquinoline<br />
+
-
 
+
-
*L-amino acid oxidase
+
-
 
+
-
**[[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 />
+
-
 
+
-
*L-amino acid oxidase complex
+
-
 
+
-
**[[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 />
+
-
}}
+
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Amino_acid_oxidase"
Personal tools