Amino acid oxidase
From Proteopedia
(Difference between revisions)
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| - | {{STRUCTURE_2jb1| PDB= | + | {{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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| - | '''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. | + | |
| + | == 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== | ==3D structures of amino acid oxidase== | ||
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*L-amino acid oxidase complex | *L-amino acid oxidase complex | ||
| - | **[[1f8r]] – | + | **[[1f8r]] – PvLAO + citrate – pit viper<br /> |
| - | **[[1f8s]] - | + | **[[1f8s]] - PvLAO + aminobenzoate<br /> |
| - | **[[1tdk]] – HvLAO + L-vinylglycine | + | **[[1tdk]] – HvLAO + L-vinylglycine <br /> |
**[[1tdn]] - HvLAO + L-leucine<br /> | **[[1tdn]] - HvLAO + L-leucine<br /> | ||
**[[1tdo]] - HvLAO + L-phenylalanine<br /> | **[[1tdo]] - HvLAO + L-phenylalanine<br /> | ||
Revision as of 07:09, 1 November 2015
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
