Four Trypanosoma brucei fatty acyl-CoA synthetases: Fatty acid specificity of the recombinant proteins

D. W. Jiang, P. T. Englund

Research output: Contribution to journalArticle

Abstract

As part of our investigation of fatty acid metabolism in Trypanosoma brucei, we have expressed four acyl-CoA synthetase (TbACS) genes in Esherichia coli. The recombinant proteins, with His-tags on their C-termini, were purified to near homogeneity using nickel-chelate affinity chromatography. Although these enzymes are highly homologous, they have distinct specificities for fatty acid chain length. TbACS1 prefers saturated fatty acids in the range C11:0 to C14:0 and TbACS2 prefers shorter fatty acids, mainly C10:0. TbACS3 and 4, which have 95% sequence identity, have similar specificities, favouring fatty acids between C14:0 and C17:0. In addition, TbACS1, 3 and 4 function well with a variety of unsaturated fatty acids.

Original languageEnglish (US)
Pages (from-to)757-761
Number of pages5
JournalBiochemical Journal
Volume358
Issue number3
DOIs
StatePublished - Sep 15 2001

Keywords

  • ACS signature motif
  • Enzyme-coupled assay
  • Fatty acid chain length
  • Glycosyl phosphatidylinositol myristoylation
  • Recombinant acyl-CoA synthetases (ACS)

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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