Transacylase activity of lactating bovine mammary fatty acid synthase

Gregory J. Anderson, Soma Kumar

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

An assay for the transacylation reaction catalyzed by fatty acid synthase was developed which does not require model substrates or labelled acyl-derivatives of CoA. It involves the transfer of the acyl group from unlabelled CoA to [3H]CoA. This assay shows the occurrence of transacylation at a relatively high rate with a variety of substrates that the enzyme is able to utilize. The activity is unaffected by dissociation of the enzyme or modification by iodoacetamide or 2-chloroacetyl-CoA.

Original languageEnglish (US)
Pages (from-to)323-326
Number of pages4
JournalFEBS Letters
Volume220
Issue number2
DOIs
StatePublished - Aug 17 1987

Keywords

  • Acyl exchange
  • Fatty acid synthase
  • Substrate specificity
  • Transacylase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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