4uhw
From Proteopedia
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| - | ''' | + | ==Human aldehyde oxidase== |
| - | + | <StructureSection load='4uhw' size='340' side='right' caption='[[4uhw]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4uhw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UHW FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MOS:DIOXOTHIOMOLYBDENUM(VI)+ION'>MOS</scene>, <scene name='pdbligand=MTE:PHOSPHONIC+ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER'>MTE</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uhx|4uhx]]</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uhw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uhw RCSB], [http://www.ebi.ac.uk/pdbsum/4uhw PDBsum]</span></td></tr> | |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/AOXA_HUMAN AOXA_HUMAN]] Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N-methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis.<ref>PMID:20444863</ref> <ref>PMID:22031625</ref> <ref>PMID:22279051</ref> <ref>PMID:22522748</ref> <ref>PMID:22996261</ref> <ref>PMID:23857892</ref> <ref>PMID:7786031</ref> <ref>PMID:9224775</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Coelho, C]] | [[Category: Coelho, C]] | ||
| - | [[Category: Romao, M | + | [[Category: Romao, M J]] |
| + | [[Category: Santos-Silva, T]] | ||
| + | [[Category: Drug metabolism]] | ||
| + | [[Category: Molybdenum enzyme]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Xanthine oxidase enzyme]] | ||
Revision as of 12:29, 2 September 2015
Human aldehyde oxidase
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