Reactome | ALDH3A2-1 oxidises HD2NAL to PALM

ALDH3A2-1 oxidises HD2NAL to PALM

Stable Identifier

R-HSA-5692261

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, endoplasmic reticulum membrane

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Fatty aldehyde dehydrogenase family 3 member A2, isoform 1 (ALDH3A2-1) in the endoplasmic reticulum membrane can catalyse the oxidation of long-chain aliphatic aldehydes to fatty acids (Kelson et al. 1997; Rizzo et al. 2001). Structural studies suggest that the enzyme is a homodimer (Keller et al. 2010), and expression studies of the homologous mouse proteins in cultured cells indicate that ALDH3A2 isoform 1 to the endoplasmic reticulum while isoform 2 is localized to peroxisomes (Ashibe et al. 2007). The sphingosine 1-phosphate (S1P) degradation product hexadec-2-enal (HD2NAL) can be oxidised to hexadecenoic acid (palmitic acid, PALM) (Nakahara et al. 2012). Defective ALDH3A2 results in Sjoegren-Larsson syndrome (SLS; MIM:270200), a neurocutaneous disorder characterised by a combination of severe mental retardation, spastic di- or tetraplegia and congenital ichthyosis. Accumulation of the S1P metabolite HD2NAL contributes to the pathogenesis of SLS (De Laurenzi et al. 1996, Sillen et al. 1998).

Literature References

PubMed ID	Title	Journal	Year
17510064	Dual subcellular localization in the endoplasmic reticulum and peroxisomes and a vital role in protecting against oxidative stress of fatty aldehyde dehydrogenase are achieved by alternative splicing Hirai, T, Ashibe, B, Motojima, K, Higashi, K, Sekimizu, K	J. Biol. Chem.	2007
22633490	The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway Abe, K, Ohkuni, A, Nakahara, K, Zoeller, RA, Ohno, Y, Kitamura, T, Kihara, A, Naganuma, T	Mol. Cell	2012
19965611	Monitoring of fatty aldehyde dehydrogenase by formation of pyrenedecanoic acid from pyrenedecanal Lindner, HH, Werner-Felmayer, G, Werner, ER, Golderer, G, Keller, MA, Maglione, M, Wanders, RJA, Sarg, B, Terrinoni, A, Watschinger, K	J. Lipid Res.	2010
8528251	Sjögren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene Rizzo, WB, Steinert, PM, Markova, N, Rogers, GR, Hamrock, DJ, Compton, JG, Marekov, LN, De Laurenzi, V	Nat. Genet.	1996
11306053	Fatty aldehyde dehydrogenase: genomic structure, expression and mutation analysis in Sjögren-Larsson syndrome Lin, Z, Rizzo, WB, Carney, G	Chem. Biol. Interact.	2001
9829906	Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjögren-Larsson syndrome Küster, W, Anton-Lamprecht, I, Jagell, S, Braun-Quentin, C, Sillén, A, Ayuso, C, Wadelius, C, Kraus, CS, Sayli, BS	Hum. Mutat.	1998
9133646	Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization Rizzo, WB, Secor McVoy, JR, Kelson, TL	Biochim. Biophys. Acta	1997