Amino acid oxidase

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{{STRUCTURE_2jb1| PDB=1f8s | SIZE=400| SCENE= |right|CAPTION=Pit viper L-amino acid oxidase dimer containing FAD complex with aminobenzoate, [[1f8s]] }}
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{{STRUCTURE_2jb1| PDB=2jb1 | SIZE=400| SCENE= |right|CAPTION=Pit viper L-amino acid oxidase dimer containing FAD complex with aminobenzoate, [[2jb1]] }}
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Revision as of 07:12, 1 November 2015

Template:STRUCTURE 2jb1

Contents

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.

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 residues include E209 and R90.

3D structures of amino acid oxidase

Updated on 01-November-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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