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Long-chain-aldehyde dehydrogenase

From Wikipedia, the free encyclopedia
(Redirected fromALDH3A2)
Protein-coding gene in the species Homo sapiens

ALDH3A2
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

4QGK

Identifiers
AliasesALDH3A2, aldehyde dehydrogenase 3 family, member A2, ALDH10, FALDH, SLS, aldehyde dehydrogenase 3 family member A2
External IDsOMIM:609523;MGI:1353452;HomoloGene:55458;GeneCards:ALDH3A2;OMA:ALDH3A2 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for ALDH3A2
Genomic location for ALDH3A2
Band17p11.2Start19,648,136bp[1]
End19,685,760bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for ALDH3A2
Genomic location for ALDH3A2
Band11 B2|11 37.96 cMStart61,114,243bp[2]
End61,158,290bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right adrenal cortex

  • left adrenal gland

  • left adrenal cortex

  • skin of thigh

  • skin of hip

  • skin of abdomen

  • hair follicle

  • kidney tubule

  • nipple

  • skin of arm
Top expressed in
  • right kidney

  • left lobe of liver

  • gastrula

  • granulocyte

  • mucous cell of stomach

  • lacrimal gland

  • decidua

  • duodenum

  • yolk sac

  • gallbladder
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

224

11671

Ensembl

ENSG00000072210

ENSMUSG00000010025

UniProt

P51648

P47740

RefSeq (mRNA)
NM_000382
NM_001031806
NM_001369136
NM_001369137
NM_001369138

NM_001369139
NM_001369146
NM_001369148

NM_007437
NM_001331114
NM_001331115

RefSeq (protein)
NP_000373
NP_001026976
NP_001356065
NP_001356066
NP_001356067

NP_001356068
NP_001356075
NP_001356077

NP_001318043
NP_001318044
NP_031463

Location (UCSC)Chr 17: 19.65 – 19.69 MbChr 11: 61.11 – 61.16 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Fatty aldehyde dehydrogenase (orlong-chain-aldehyde dehydrogenase) is analdehyde dehydrogenase enzyme that in human is encoded in theALDH3A2 gene on chromosome 17.Aldehyde dehydrogenase enzymes function to remove toxicaldehydes that are generated by the metabolism of alcohol and by lipid peroxidation.

Structure

[edit]

ALDH3A2 belongs to thealdehyde dehydrogenasesuperfamily and is a membrane-associated protein typically containing 485 residues. The mature protein functions as adimer. The structure was resolved using X-ray crystallography at 2.1 Angstrom resolution. It contains an element in the C-terminal region referred to as a "gatekeeper" helix, which is adjacent to the membrane-anchored transmembrane domain and the catalytic core. The gatekeeper helix appears to control access of molecular substrates to the catalytic core and allows efficient transit between membranes and catalytic sites.[5]

Function

[edit]

ALDH3A2 catalyzes the oxidation of long-chain aliphatic aldehydes into fatty acids. It is known to act on a variety of both saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length, as well as dihydrophytal, a 20-carbon branched chain aldehyde.[6] It requiresNAD+ as aco-factor. The encoded enzyme is responsible for conversion of thesphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid. ALD3H2 is expressed in the humanliver and has been found to localize themicrosome fraction inside the cell.[7]

At least twoalternative splicing isoforms of ALDH3A2 are known to exist. The alternative transcript differs by an additional exon and anchors differently to the endoplasmic reticulum vs. the peroxisome[8]

Clinical significance

[edit]

Mutations and deletions within theALDH3A2 gene have been widely associated with the autosomal recessiveSjögren-Larsson syndrome, anautosomal recessive neurocutaneous disease.[9] Multiple mutations have been found in different families, including those that molecularly disrupts the protein dimerization interface or reducesmRNA stability.[citation needed] Absence or insufficiency of ALDH3A2 protein products in mutant cells are known to cause abnormal metabolism of sphingosine 1-phosphate to ether-linkedglycerolipids and the abnormal accumulation of lipid precursors.

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000072210Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000010025Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^Keller MA, Zander U, Fuchs JE, Kreutz C, Watschinger K, Mueller T, Golderer G, Liedl KR, Ralser M, Kräutler B, Werner ER, Marquez JA (2014)."A gatekeeper helix determines the substrate specificity of Sjögren-Larsson Syndrome enzyme fatty aldehyde dehydrogenase".Nat Commun.5: 4439.Bibcode:2014NatCo...5.4439K.doi:10.1038/ncomms5439.PMC 4109017.PMID 25047030.
  6. ^Kelson TL, Secor McVoy JR, Rizzo WB (1997). "Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization".Biochim. Biophys. Acta.1335 (1–2):99–110.doi:10.1016/s0304-4165(96)00126-2.PMID 9133646.
  7. ^Kelson TL, Secor McVoy JR, Rizzo WB (1997). "Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization".Biochim. Biophys. Acta.1335 (1–2):99–110.doi:10.1016/s0304-4165(96)00126-2.PMID 9133646.
  8. ^Rogers GR, Markova NG, De Laurenzi V, Rizzo WB, Compton JG (1997)."Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH)".Genomics.39 (2):127–35.doi:10.1006/geno.1996.4501.PMID 9027499.
  9. ^Nakahara K, Ohkuni A, Kitamura T, Abe K, Naganuma T, Ohno Y, Zoeller RA, Kihara A (2012)."The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway".Mol. Cell.46 (4):461–71.doi:10.1016/j.molcel.2012.04.033.hdl:2115/49428.PMID 22633490.

Further reading

[edit]
Family 1
Family 2 (mitochondrial)
Family 3
Other
Synthesis
Malonyl-CoA synthesis
Fatty acid synthesis/
Fatty acid synthase
Fatty aciddesaturases
Triacyl glycerol
Degradation
Acyl transport
Beta oxidation
General
Unsaturated
Odd chain
Other
Toacetyl-CoA
Aldehydes
Aldehyde/oxooxidoreductases (EC 1.2)
1.2.1:NAD orNADP
1.2.2:cytochrome
1.2.3:oxygen
1.2.4:disulfide
1.2.7:iron–sulfur protein
Activity
Regulation
Classification
Kinetics
Types
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