ALDH2

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(New page: ==ALDH2== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for your page '''Marek Földi/ALDH2'''. Click above on...)
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==ALDH2==
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== Introduction ==
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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Some kind of intro, where it’s located, coding gene is located on chromosome 12 (12q24.2), 44kpbs in lenght with 13 exons <ref>DOI:10.1074/jbc.M606477200</ref>…
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This is a default text for your page '''Marek Földi/ALDH2'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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== Structure ==
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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<StructureSection load='3N80' size='350' side='right' caption='Human mitochondrial aldehyde dehydrogenase, apo form (PDB entry [http://doi.org/10.2210/pdb3N80/pdb 3N80])' scene=''>
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Homotetramer ...
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</StructureSection>
== Function ==
== Function ==
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Detoxifying of toxic aldehydes, involved in many pathways such as ethanol breakdown, lipid metabolization, role in oxidative stress of cell.
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== Mutations ==
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<StructureSection load='3INL' size='350' side='right' caption='Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, complexed with agonist Alda-1 (PDB entry [http://doi.org/10.2210/pdb3INL/pdb 3INL])' scene=''>
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There are seven mutations observed in different ethnicies. Most studied of them is East Asian mutation connected with alcohol flushing syndrome and other diseases. <ref name="nov2020">DOI: 10.1016/j.ebiom.2020.102753</ref>
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== Disease ==
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{| class="wikitable"
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|-
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! ''ALDH2'' designation
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! Mutation
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! Location
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! AA change
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! Major ethnicity
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! Relative activity
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|-
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| '''WT (''ALDH2*1'')'''
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|
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|
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|
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|
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|-
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| '''''ALDH2*2'''''
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| E504K <ref>E504K https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99451499</ref>
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| 504
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| Glu → Lys<br />
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| East Asian
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| 0 %
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|-
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| '''''ALDH2*3'''''
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| I41V
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|
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|
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| African
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| 60 %
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|-
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| '''''ALDH2*4'''''
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| P92T <ref>P92T https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99454838</ref>
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| 92
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| Pro → Thr
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| Latino
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| 32 %
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|-
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| '''''ALDH2*5'''''
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| T244M <ref>T244M https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99452531</ref>
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| 244
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| Thr → Met
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| South Asian
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| 38 %
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|-
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| '''''ALDH2*6'''''
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| V304M <ref>V304M https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99451318</ref>
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| 304
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| Val → Met
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| Latino
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| 11 %<br />
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|-
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| '''''ALDH2*7'''''
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| R338W <ref>R338W https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99455550</ref>
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| 338
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| Arg → Trp
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| Finnish
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| 23 %
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|}
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</StructureSection>
== Relevance ==
== Relevance ==
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== Structural highlights ==
 
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
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</StructureSection>
 
== References ==
== References ==
<references/>
<references/>

Revision as of 21:06, 26 April 2022

Contents

Introduction

Some kind of intro, where it’s located, coding gene is located on chromosome 12 (12q24.2), 44kpbs in lenght with 13 exons [1]…

Structure

Human mitochondrial aldehyde dehydrogenase, apo form (PDB entry 3N80)

Drag the structure with the mouse to rotate

Function

Detoxifying of toxic aldehydes, involved in many pathways such as ethanol breakdown, lipid metabolization, role in oxidative stress of cell.

Mutations

Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, complexed with agonist Alda-1 (PDB entry 3INL)

Drag the structure with the mouse to rotate

Relevance

References

  1. ↑ Wenzel P, Hink U, Oelze M, Schuppan S, Schaeuble K, Schildknecht S, Ho KK, Weiner H, Bachschmid M, Munzel T, Daiber A. Role of reduced lipoic acid in the redox regulation of mitochondrial aldehyde dehydrogenase (ALDH-2) activity. Implications for mitochondrial oxidative stress and nitrate tolerance. J Biol Chem. 2007 Jan 5;282(1):792-9. doi: 10.1074/jbc.M606477200. Epub 2006 Nov , 13. PMID:17102135 doi:http://dx.doi.org/10.1074/jbc.M606477200
  2. ↑ Chen CH, Ferreira JCB, Joshi AU, Stevens MC, Li SJ, Hsu JH, Maclean R, Ferreira ND, Cervantes PR, Martinez DD, Barrientos FL, Quintanares GHR, Mochly-Rosen D. Novel and prevalent non-East Asian ALDH2 variants; Implications for global susceptibility to aldehydes' toxicity. EBioMedicine. 2020 May;55:102753. doi: 10.1016/j.ebiom.2020.102753. Epub 2020 May, 8. PMID:32403082 doi:http://dx.doi.org/10.1016/j.ebiom.2020.102753
  3. ↑ E504K https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99451499
  4. ↑ P92T https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99454838
  5. ↑ T244M https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99452531
  6. ↑ V304M https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99451318
  7. ↑ R338W https://cancer.sanger.ac.uk/cosmic/mutation/overview?id=99455550

Proteopedia Page Contributors and Editors (what is this?)

Michal Hub, Marek Földi, Michal Harel

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