A peroxisomal acyltransferase in mouse identifies a novel pathway for taurine conjugation of fatty acids

Sarah Jayne Reilly, Ethna M. O'Shea, Ulla Andersson, James O'Byrne, Stefan E.H. Alexson, Mary C. Hunt

Research output: Contribution to journalArticlepeer-review

Abstract

A wide variety of endogenous carboxylic acids and xenobiotics are conjugated with amino acids, before excretion in urine or bile. The conjugation of carboxylic acids and bile acids with taurine and glycine has been widely characterized, and de novo synthesized bile acids are conjugated to either glycine or taurine in peroxisomes. Peroxisomes are also involved in the oxidation of several other lipid molecules, such as very long chain acyl-CoAs, branched chain acyl-CoAs, and prostaglandins. In this study, we have now identified a novel peroxisomal enzyme called acyl-coenzyme A:amino acid N-acyltransferase (ACNAT1). Recombinantly expressed ACNAT1 acts as an acyltransferase that efficiently conjugates very long-chain and long-chain fatty acids to taurine. The enzyme shows no conjugating activity with glycine, showing that it is a specific taurine conjugator. Acnat1 is mainly expressed in liver and kidney, and the gene is localized in a gene cluster, together with two further acyltransferases, one of which conjugates bile acids to glycine and taurine. In conclusion, these data describe ACNAT1 as a new acyltransferase, involved in taurine conjugation of fatty acids in peroxisomes, identifying a novel pathway for production of N-acyltaurines as signaling molecules or for excretion of fatty acids.

Original languageEnglish
Pages (from-to)99-107
Number of pages9
JournalFASEB Journal
Volume21
Issue number1
DOIs
Publication statusPublished - Jan 2007
Externally publishedYes

Keywords

  • Acyl-coenzyme A
  • Fatty acid amide hydrolase
  • N-acyltaurine

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