Overexpression of human antiquitin in E. coli: enzymatic characterization of twelve ALDH7A1 missense mutations associated with pyridoxine-dependent epilepsy

Mol Genet Metab. 2012 Aug;106(4):478-81. doi: 10.1016/j.ymgme.2012.06.008. Epub 2012 Jun 22.

Abstract

Pyridoxine dependent epilepsy is an autosomal recessive disorder characterized by early onset seizures responsive to pyridoxine and caused by a defect in the α-aminoadipic semialdehyde dehydrogenase (antiquitin) gene (ALDH7A1). In order to characterize the effects of a series of twelve disease-associated ALDH7A1 missense mutations on antiquitin activity, we generated the mutations in a recombinant human antiquitin cDNA and expressed them in Escherichia coli. We developed an automated spectrophotometric assay of antiquitin enzymatic activity using the natural substrate α-aminoadipic semialdehyde. The substrate was generated using a recombinant lysine aminotransferase gene (lat) from Streptomyces clavuligerus. In the E. coli expression system all the mutants were stably expressed but lacked enzymatic activity. This is consistent with pathogenicity of these mutations in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehyde Dehydrogenase / genetics*
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Assays
  • Epilepsy / enzymology*
  • Epilepsy / genetics*
  • Escherichia coli / metabolism*
  • Humans
  • Mutant Proteins / metabolism
  • Mutation, Missense / genetics*
  • Time Factors

Substances

  • Mutant Proteins
  • ALDH7A1 protein, human
  • Aldehyde Dehydrogenase

Supplementary concepts

  • Pyridoxine-dependent epilepsy