Fatty aldehyde dehydrogenase: Genomic structure, expression and mutation analysis in Sjögren-Larsson syndrome

William B. Rizzo, Zhili Lin, Gael Carney

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

Fatty aldehyde dehydrogenase (FALDH) is a microsomal enzyme that catalyzes the oxidation of medium- and long-chain aliphatic aldehydes derived from metabolism of fatty alcohol, phytanic acid, ether glycerolipids and leukotriene B4. The FALDH gene (ALDH3A2) in man and mouse consists of 11 exons and is closely linked to the gene for ALDH3. In both species, alternative splicing results in formation of a second minor protein, FALDHv, that has a unique carboxy-terminal end. The functional significance of this alternate protein is not known. In humans, mutations in the FALDH gene cause Sjögren-Larsson syndrome (SLS), which is characterized by ichthyosis, mental retardation and spasticity. Missense mutations involving 24 amino acid positions in FALDH have been identified. These amino acids are more highly conserved among related class 3 aldehyde dehydrogenase enzymes than expected, suggesting that they are critically important for protein folding, catalysis or stability. Studies of mutations in SLS should prove useful for understanding structure-function correlations in FALDH and other aldehyde dehydrogenase proteins.

Original languageEnglish (US)
Pages (from-to)297-307
Number of pages11
JournalChemico-Biological Interactions
Volume130-132
DOIs
StatePublished - Jan 30 2001

Keywords

  • Aldehyde dehydrogenase
  • Fatty aldehyde
  • Mutation
  • Sjögren-Larsson syndrome

ASJC Scopus subject areas

  • Toxicology

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