Aldehydoxidase
| {{#if: | | Aldehydoxidase }} | |||||||||||||
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| Eigenschaften des menschlichen Proteins
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| Masse/Länge Primärstruktur | 1338 Aminosäuren
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| Sekundär- bis Quartärstruktur | Homodimer
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| Kofaktor | Molybdopterin, FAD, 2 (2Fe-2S)
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| {{#if:AO | Gen-Namen | Gen-Name}} | Gen-Name(n) }} | {{#if:553 | AOX1 | AOX1}}{{#if:AO |, AO}} }} | ||||||||||||
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| DrugBank | [2]
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| Wirkstoffklasse |
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| TCDB | [3]
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| EC, Kategorie | {{#if:1.2.3.1| 1.2.3.1}}{{#if: Oxidoreduktase|, Oxidoreduktase}} }} | ||||||||||||
| MEROPS | [4]}} | ||||||||||||
| MEROPS | [5]}} | ||||||||||||
| Reaktionsart | Addition eines Sauerstoffatoms
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| Substrat | Aldehyd + O2 + H2O
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| Produkte | Carbonsäure + H2O2
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Entrez
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style="background:#C3FDB8; color:#202122;" | Ensembl
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|- | style="background:#C3FDB8; color:#202122;" | UniProt {{ #if: Q06278 | | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|Q06278}}{{#if:|Vorlage:Abrufdatum}} | | }} {{ #if: | | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|}}{{#if:|Vorlage:Abrufdatum}} | | }} |- {{#if: NM_001159 | | style="background:#C3FDB8; color:#202122;" | Refseq (mRNA) {{ #if: NM_001159 | | NM_001159 | | }} {{ #if: | | [8] | | }} |}} |- {{#if: NP_001150 | | style="background:#C3FDB8; color:#202122;" | Refseq (Protein) {{ #if: NP_001150 | | NP_001150 | | }} {{ #if: | | [9] | | }} |}} |- {{#if: 2200585952200682241 | | style="background:#C3FDB8; color:#202122;" | Genlocus {{#if: 2 | {{#if: 200585952 | {{#if: 200682241 | | #if: |?db=|}}&position=chr2:200585952-200682241 Chr 2: {{#expr: 200585952 / 1000000 round 2}} – {{#expr: 200682241 / 1000000 round 2}} Mb | | }} | | }} | | }} {{#if: | {{#if: | {{#if: | | #if: |?db=|}}&position=chr:- Chr : {{#expr: / 1000000 round 2}} – {{#expr: / 1000000 round 2}} Mb | | }} | | }} | | }} |}} |- | style="background:#C3FDB8; color:#202122;" | PubMed-Suche {{ #if: 316 | | 316 | | }} {{ #if: | | [10] | | }}
| |- | colspan="3" style="background:#90EE90; color:#202122; text-align:center;" | Orthologe (Mensch) |- | style="background:#C3FDB8; color:#202122;" | Entrez | colspan="2" | 316
{{#if: ENSG00000138356
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| style="background:#C3FDB8; color:#202122;" | Ensembl | colspan="2" | ENSG00000138356 }} |- | style="background:#C3FDB8; color:#202122;" | UniProt | colspan="2" | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|Q06278}}{{#if:|Vorlage:Abrufdatum}}
{{#if: NM_001159
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| style="background:#C3FDB8; color:#202122;" | Refseq (mRNA) | colspan="2" | NM_001159 }}
{{#if: NP_001150
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| style="background:#C3FDB8; color:#202122;" | Refseq (Protein) | colspan="2" | NP_001150 }}
{{#if: 2
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| style="background:#C3FDB8; color:#202122;" | Genlocus | colspan="2" | #if: |?db=|}}&position=chr2:200585952-200682241 Chr 2: {{#expr: 200585952 / 1000000 round 2}} – {{#expr: 200682241 / 1000000 round 2}} Mb
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|- | style="background:#C3FDB8; color:#202122;" | PubMed-Suche | colspan="2" | 316 }} {{#if:
| {{#if:
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| Spezies2= ist definiert, es sind jedoch keine weiteren Angaben zu Spezies2 vorhanden.{{#ifeq:0|0| }} }}
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}} | {{#if: | | colspan="3" style="background:#90EE90; color:#202122; text-align:center;" | Orthologe
|- | style="background:#C3FDB8; color:#202122;" | | style="background:#C3FDB8; color:#202122; text-align:center;" | Mensch | style="background:#C3FDB8; color:#202122; text-align:center;" | |- | style="background:#C3FDB8; color:#202122;" | Entrez {{ #if: 316 | | 316 | | }} {{ #if: | | [11] | | }} |- {{#if: ENSG00000138356 | | style="background:#C3FDB8; color:#202122;" | Ensembl {{ #if: ENSG00000138356 || ENSG00000138356 || }} {{ #if: || [12] || }} |}} |- | style="background:#C3FDB8; color:#202122;" | UniProt {{ #if: Q06278 | | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|Q06278}}{{#if:|Vorlage:Abrufdatum}} | | }} {{ #if: | | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|}}{{#if:|Vorlage:Abrufdatum}} | | }} |- {{#if: NM_001159 | | style="background:#C3FDB8; color:#202122;" | Refseq (mRNA) {{ #if: NM_001159 | | NM_001159 | | }} {{ #if: | | [13] | | }} |}} |- {{#if: NP_001150 | | style="background:#C3FDB8; color:#202122;" | Refseq (Protein) {{ #if: NP_001150 | | NP_001150 | | }} {{ #if: | | [14] | | }} |}} |- {{#if: 2200585952200682241 | | style="background:#C3FDB8; color:#202122;" | Genlocus {{#if: 2 | {{#if: 200585952 | {{#if: 200682241 | | #if: |?db=|}}&position=chr2:200585952-200682241 Chr 2: {{#expr: 200585952 / 1000000 round 2}} – {{#expr: 200682241 / 1000000 round 2}} Mb | | }} | | }} | | }} {{#if: | {{#if: | {{#if: | | #if: |?db=|}}&position=chr:- Chr : {{#expr: / 1000000 round 2}} – {{#expr: / 1000000 round 2}} Mb | | }} | | }} | | }} |}} |- | style="background:#C3FDB8; color:#202122;" | PubMed-Suche {{ #if: 316 | | 316 | | }} {{ #if: | | [15] | | }}
| |- | colspan="3" style="background:#90EE90; color:#202122; text-align:center;" | Orthologe (Mensch) |- | style="background:#C3FDB8; color:#202122;" | Entrez | colspan="2" | 316
{{#if: ENSG00000138356
| |-
| style="background:#C3FDB8; color:#202122;" | Ensembl | colspan="2" | ENSG00000138356 }} |- | style="background:#C3FDB8; color:#202122;" | UniProt | colspan="2" | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|Q06278}}{{#if:|Vorlage:Abrufdatum}}
{{#if: NM_001159
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| style="background:#C3FDB8; color:#202122;" | Refseq (mRNA) | colspan="2" | NM_001159 }}
{{#if: NP_001150
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| style="background:#C3FDB8; color:#202122;" | Refseq (Protein) | colspan="2" | NP_001150 }}
{{#if: 2
| {{#if: 200585952
| {{#if: 200682241
| |-
| style="background:#C3FDB8; color:#202122;" | Genlocus | colspan="2" | #if: |?db=|}}&position=chr2:200585952-200682241 Chr 2: {{#expr: 200585952 / 1000000 round 2}} – {{#expr: 200682241 / 1000000 round 2}} Mb
| }}
| }}
| }}
|- | style="background:#C3FDB8; color:#202122;" | PubMed-Suche | colspan="2" | 316 }} {{#if:
| {{#if:
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|}{{#if:Aldehydoxidase.png||}}
Aldehydoxidase (AOX1) ist ein Enzym in Wirbeltieren, das den Abbau von Aldehyden katalysiert. Außerdem ist bekannt, dass AOX1 Nicotin zu Cotinin oxidiert. AOX1 ist daher wichtig für den Tryptophan-Stoffwechsel und die Biotransformation. Das Enzym ist beim Menschen im Zytosol von Leberzellen lokalisiert, aber auch in Lunge, Skelettmuskeln, Bauchspeicheldrüse und Fettzellen zu finden.<ref>{{#if: | | UniProt }} {{#if:|{{{titel}}}|Q06278}}{{#if:|Vorlage:Abrufdatum}}</ref><ref>Metacyc Enzyme: Aldehyde oxidase</ref>
AOX1 ist homolog zur Xanthindehydrogenase, mit der sie früher verwechselt wurde. Mangel an AOX1 ist ein Faktor bei der seltenen Molybdän-Cofaktor-Defizienz. Im Menschen produziert nur eines der AOX-Gene ein funktionsfähiges Enzym, im Gegensatz zu anderen Wirbeltieren.<ref>{{#invoke:Vorlage:Literatur|f}}{{#if:
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In Adipozyten ist AOX1 offenbar unabdingbar für die Adipogenese und die Ausschüttung von Adiponektin, wie aus Zellstudien gefolgert wurde. In Hepatozyten wird AOX1 durch Adiponektin herunterreguliert. Da es mit dem ABCA-1-Transporter coexprimiert wird, führt AOX1-Mangel durch ABCA1-Mangel zu reduziertem Lipidexport aus den Zellen.<ref>{{#invoke:Vorlage:Literatur|f}}{{#if:
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Einzelnachweise
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Weblinks
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