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==Crystal structure of human aldehyde dehydrogenase ALDH3A1 in complex with octanal== | |||
<StructureSection load='8bb8' size='340' side='right'caption='[[8bb8]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8bb8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BB8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OYA:OCTANAL'>OYA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bb8 OCA], [https://pdbe.org/8bb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bb8 RCSB], [https://www.ebi.ac.uk/pdbsum/8bb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bb8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AL3A1_HUMAN AL3A1_HUMAN] ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Oxidoreductases are major enzymes of xenobiotic metabolism. Consequently, they are essential in the chemoprotection of the human body. Many xenobiotic metabolism enzymes have been shown to be involved in chemosensory tissue protection. Among them, some were additionally shown to be involved in chemosensory perception, acting in signal termination as well as in the generation of metabolites that change the activation pattern of chemosensory receptors. Oxidoreductases, especially aldehyde dehydrogenases and aldo-keto reductases, are the first barrier against aldehyde compounds, which include numerous odorants. Using a mass spectrometry approach, we characterized the most highly expressed members of these families in the human nasal mucus sampled in the olfactory vicinity. Their expression was also demonstrated using immunohistochemistry in human epitheliums sampled in the olfactory vicinity. Recombinant enzymes corresponding to three highly expressed human oxidoreductases (ALDH1A1, ALDH3A1, AKR1B10) were used to demonstrate the high enzymatic activity of these enzymes toward aldehyde odorants. The structureâfunction relationship set based on the enzymatic parameters characterization of a series of aldehyde odorant compounds was supported by the X-ray structure resolution of human ALDH3A1 in complex with octanal. | |||
Characterization of human oxidoreductases involved in aldehyde odorant metabolism.,Boichot V, Menetrier F, Saliou JM, Lirussi F, Canon F, Folia M, Heydel JM, Hummel T, Menzel S, Steinke M, Hackenberg S, Schwartz M, Neiers F Sci Rep. 2023 Mar 25;13(1):4876. doi: 10.1038/s41598-023-31769-4. PMID:36966166<ref>PMID:36966166</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Neiers | <div class="pdbe-citations 8bb8" style="background-color:#fffaf0;"></div> | ||
[[Category: Schwartz | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Neiers F]] | |||
[[Category: Schwartz M]] | |||
Revision as of 12:25, 19 April 2023
Crystal structure of human aldehyde dehydrogenase ALDH3A1 in complex with octanalCrystal structure of human aldehyde dehydrogenase ALDH3A1 in complex with octanal
Structural highlights
FunctionAL3A1_HUMAN ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes. Publication Abstract from PubMedOxidoreductases are major enzymes of xenobiotic metabolism. Consequently, they are essential in the chemoprotection of the human body. Many xenobiotic metabolism enzymes have been shown to be involved in chemosensory tissue protection. Among them, some were additionally shown to be involved in chemosensory perception, acting in signal termination as well as in the generation of metabolites that change the activation pattern of chemosensory receptors. Oxidoreductases, especially aldehyde dehydrogenases and aldo-keto reductases, are the first barrier against aldehyde compounds, which include numerous odorants. Using a mass spectrometry approach, we characterized the most highly expressed members of these families in the human nasal mucus sampled in the olfactory vicinity. Their expression was also demonstrated using immunohistochemistry in human epitheliums sampled in the olfactory vicinity. Recombinant enzymes corresponding to three highly expressed human oxidoreductases (ALDH1A1, ALDH3A1, AKR1B10) were used to demonstrate the high enzymatic activity of these enzymes toward aldehyde odorants. The structureâfunction relationship set based on the enzymatic parameters characterization of a series of aldehyde odorant compounds was supported by the X-ray structure resolution of human ALDH3A1 in complex with octanal. Characterization of human oxidoreductases involved in aldehyde odorant metabolism.,Boichot V, Menetrier F, Saliou JM, Lirussi F, Canon F, Folia M, Heydel JM, Hummel T, Menzel S, Steinke M, Hackenberg S, Schwartz M, Neiers F Sci Rep. 2023 Mar 25;13(1):4876. doi: 10.1038/s41598-023-31769-4. PMID:36966166[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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