Monoamine oxidase

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{{STRUCTURE_1gos| PDB=1gos | SIZE=400| SCENE= |right| CAPTION=Human MAO-B dimer complex with FAD and phenyl-propenylidine derivative, [[1gos]] }}
{{STRUCTURE_1gos| PDB=1gos | SIZE=400| SCENE= |right| CAPTION=Human MAO-B dimer complex with FAD and phenyl-propenylidine derivative, [[1gos]] }}
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== Function ==
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'''Monoamine oxidas'''e (MAO) are enzymes which catalyze the oxidation of monoamines. MAO contains FAD as co-factor.<br />
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'''Monoamine oxidas'''e (MAO) are enzymes which catalyze the oxidation of monoamines<ref>PMID:15279561</ref>. MAO contains FAD as co-factor.<br />
* '''MAO-A''' and '''MAO-C''' are human enzymes which oxidize adrenaline, noradrenaline, serotonin and dopamine.<br />
* '''MAO-A''' and '''MAO-C''' are human enzymes which oxidize adrenaline, noradrenaline, serotonin and dopamine.<br />
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* '''MAO-B''' is a human enzyme which oxidizes benzylamine and phenylethylamine. For details on MAO-B see [[Monoamine oxidase b]].
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* '''MAO-B''' is a human enzyme which oxidizes benzylamine and phenylethylamine. For details on MAO-B see [[Monoamine oxidase b]].<br />
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* '''MAO-N''' is a ''Aspergillus niger'' enzyme which oxidizes primary amines<ref>PMID:18951902</ref>.
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== Relevance ==
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Elevated levels of MAO-A in the brain are measured during depression<ref>PMID:17088501</ref>. MAO inhibitors were the first anti-depression drugs developed.
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== Structural highlights ==
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MAO-B active site is composed of 2 cavities: the substrate cavity in front of the FAD and the entrance cavity. Safinamide - a drug tested for Parkinson's disease<ref>PMID:17030736</ref> - occupies both cavities<ref>PMID:17915852</ref>.
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</StructureSection>
==3D structures of monoamine oxidase ==
==3D structures of monoamine oxidase ==
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**[[2vvl]], [[2vvm]], [[3zdn]] – MAO-N (mutant) + FAD – ''Aspergillus niger''
**[[2vvl]], [[2vvm]], [[3zdn]] – MAO-N (mutant) + FAD – ''Aspergillus niger''
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 08:08, 1 May 2016

PDB ID 1gos

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Human MAO-B dimer complex with FAD and phenyl-propenylidine derivative, 1gos
Ligands: ,
Activity: Monoamine oxidase, with EC number 1.4.3.4
Related: 1h8r
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

Function

Monoamine oxidase (MAO) are enzymes which catalyze the oxidation of monoamines[1]. MAO contains FAD as co-factor.

  • MAO-A and MAO-C are human enzymes which oxidize adrenaline, noradrenaline, serotonin and dopamine.
  • MAO-B is a human enzyme which oxidizes benzylamine and phenylethylamine. For details on MAO-B see Monoamine oxidase b.
  • MAO-N is a Aspergillus niger enzyme which oxidizes primary amines[2].

Relevance

Elevated levels of MAO-A in the brain are measured during depression[3]. MAO inhibitors were the first anti-depression drugs developed.

Structural highlights

MAO-B active site is composed of 2 cavities: the substrate cavity in front of the FAD and the entrance cavity. Safinamide - a drug tested for Parkinson's disease[4] - occupies both cavities[5].

</StructureSection>

3D structures of monoamine oxidase

Updated on 01-May-2016

References

  1. ↑ Tipton KF, Boyce S, O'Sullivan J, Davey GP, Healy J. Monoamine oxidases: certainties and uncertainties. Curr Med Chem. 2004 Aug;11(15):1965-82. PMID:15279561
  2. ↑ Atkin KE, Reiss R, Koehler V, Bailey KR, Hart S, Turkenburg JP, Turner NJ, Brzozowski AM, Grogan G. The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution. J Mol Biol. 2008 Dec 31;384(5):1218-31. Epub 2008 Oct 14. PMID:18951902 doi:10.1016/j.jmb.2008.09.090
  3. ↑ Meyer JH, Ginovart N, Boovariwala A, Sagrati S, Hussey D, Garcia A, Young T, Praschak-Rieder N, Wilson AA, Houle S. Elevated monoamine oxidase a levels in the brain: an explanation for the monoamine imbalance of major depression. Arch Gen Psychiatry. 2006 Nov;63(11):1209-16. PMID:17088501 doi:http://dx.doi.org/10.1001/archpsyc.63.11.1209
  4. ↑ Caccia C, Maj R, Calabresi M, Maestroni S, Faravelli L, Curatolo L, Salvati P, Fariello RG. Safinamide: from molecular targets to a new anti-Parkinson drug. Neurology. 2006 Oct 10;67(7 Suppl 2):S18-23. PMID:17030736
  5. ↑ Binda C, Wang J, Pisani L, Caccia C, Carotti A, Salvati P, Edmondson DE, Mattevi A. Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs. J Med Chem. 2007 Nov 15;50(23):5848-52. Epub 2007 Oct 4. PMID:17915852 doi:http://dx.doi.org/10.1021/jm070677y

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