ALDH3A2-1 oxidises HD2NAL to PALM

Stable Identifier
Reaction [transition]
Homo sapiens
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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
Catalyst Activity

aldehyde dehydrogenase (NAD+) activity of ALDH3A2-1 dimer [endoplasmic reticulum membrane]

Orthologous Events
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