Identification of PTE2, a human peroxisomal long-chain Acyl-CoA thioesterase

Jacob M. Jones, Stephen J. Gould

Research output: Contribution to journalArticlepeer-review

Abstract

Computer-based approaches identified PTE2 as a candidate human peroxisomal acyl-CoA thioesterase gene. The PTE2 gene product is highly similar to the rat cytosolic and mitochondrial thioesterases, CTE1 and MTE1, respectively, and terminates in a tripeptide sequence, serine-lysine-valine(COOH), that resembles the consensus sequence for type-1 peroxisomal targeting signals. PTE2 was targeted to peroxisomes and recombinant PTE2 showed intrinsic acyl-CoA thioesterase activity with a pH optimum of 8.5. A comparison of PTE2 and PTE1 thioesterase activities across multiple acyl-CoA substrates indicated that while PTE1 was most active on medium-chain acyl-CoAs, with little activity on long-chain acyl-CoAs, PTE2 displayed high activity on medium- and long-chain acyl-CoAs. The identification of PTE2 therefore offers an explanation for the observed long-chain acyl-CoA thioesterase activity of mammalian peroxisomes. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)233-240
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume275
Issue number1
DOIs
StatePublished - Aug 18 2000

Keywords

  • Coenzyme A
  • Fatty acid metabolism
  • Peroxisomes
  • Thioesterase
  • α-oxidation
  • β-oxidation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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