Monoamine oxidase
From Proteopedia
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<StructureSection load='' size='350' side='right' caption='Human MAO-B complex with safinamide and FAD (PDB entry [[2v5z]])' scene='45/458397/Cv/1'> | <StructureSection load='' size='350' side='right' caption='Human MAO-B complex with safinamide and FAD (PDB entry [[2v5z]])' scene='45/458397/Cv/1'> | ||
== Function == | == Function == | ||
| - | '''Monoamine | + | '''Monoamine oxidase''' or '''amine oxidase (Flavin-containing)''' (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 /> | ||
* '''MAO-B''' or '''amine oxidase [flavin-containing] B''' is a human enzyme which oxidizes benzylamine and phenylethylamine. For details on MAO-B see [[Monoamine oxidase b]].<br /> | * '''MAO-B''' or '''amine oxidase [flavin-containing] B''' is a human enzyme which oxidizes benzylamine and phenylethylamine. For details on MAO-B see [[Monoamine oxidase b]].<br /> | ||
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**[[1gos]] – hMAO-B<br /> | **[[1gos]] – hMAO-B<br /> | ||
| - | **[[3po7]], [[2xcg]], [[2xfn]], [[2xfp]], [[2xfq]], [[2xfu]], [[2vz2]], [[2vrl]], [[2vrm]], [[2v5z]], [[2v60]], [[2v61]], [[2c64]], [[2c65]], [[2c66]], [[2c67]], [[2byb]], [[2bk3]], [[1s2q]], [[1s2y]], [[1s3b]], [[1s3e]], [[1oj9]], [[1oja]], [[1ojc]], [[1ojd]], [[4a79]], [[4a7a]], [[4crt]], [[5mrl]], [[6fvz]], [[6gw0]], [[6fwc]], [[6fw0]], [[6rkb]], [[6rkp]], [[6rle]], [[6yt2]] – hMAO-B + inhibitor + FAD<br /> | + | **[[3po7]], [[2xcg]], [[2xfn]], [[2xfp]], [[2xfq]], [[2xfu]], [[2vz2]], [[2vrl]], [[2vrm]], [[2v5z]], [[2v60]], [[2v61]], [[2c64]], [[2c65]], [[2c66]], [[2c67]], [[2byb]], [[2bk3]], [[1s2q]], [[1s2y]], [[1s3b]], [[1s3e]], [[1oj9]], [[1oja]], [[1ojc]], [[1ojd]], [[4a79]], [[4a7a]], [[4crt]], [[5mrl]], [[6fvz]], [[6gw0]], [[6fwc]], [[6fw0]], [[6rkb]], [[6rkp]], [[6rle]], [[6yt2]], [[7b0v]], [[7b0z]] – hMAO-B + inhibitor + FAD<br /> |
**[[2xfo]], [[2bk4]], [[2bk5]] - hMAO-B (mutant) + inhibitor + FAD<br /> | **[[2xfo]], [[2bk4]], [[2bk5]] - hMAO-B (mutant) + inhibitor + FAD<br /> | ||
**[[2c72]], [[2c73]], [[2c75]], [[2c76]] - hMAO-B (mutant) + FAD<br /> | **[[2c72]], [[2c73]], [[2c75]], [[2c76]] - hMAO-B (mutant) + FAD<br /> | ||
Revision as of 09:22, 4 November 2021
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3D structures of monoamine oxidase
Updated on 04-November-2021
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
