The type I rat fatty acid synthase ACP shows structural homology and analogous biochemical properties to type II ACPs

M. A C Reed, Michael Schweizer, Anna E. Szafranska, Chris Arthur, Thomas P. Nicholson, Russell J. Cox, John Crosby, Matthew P. Crump, Thomas J. Simpson

    Research output: Contribution to journalArticle

    36 Citations (Scopus)

    Abstract

    While X-ray and NMR structures are now available for most components of the Type II fatty acid synthase (FAS), there are no structures for Type I FAS domains. A region from the mammalian (rat) FAS, including the putative acyl carrier protein (ACP), has been cloned and over-expressed. Here we report multinuclear, multidimensional NMR studies which show that this isolated ACP domain contains four a-helices (residues 8-16 [1]; 41-51 [2]; 58-63 [3] and 66-74 [4]) and an overall global fold characteristic of ACPs from both Type II FAS and polyketide synthases (PKSs). ‡ The overall length of the structured ACP domain (67 residues) is smaller than the structured regions of the Eschericia coli FAS ACP (75 residues), the actinorhodin PKS ACP (78 residues) and the Bacillus subtilis FAS ACP (76 residues). We further show that the rat FAS ACP is recognised as an efficient substrate by enzymes known to modify Type II ACPs including phosphopantetheinyl and malonyl transferases, but not by the heterologous S, coelicolor minimal polyketide synthase.

    Original languageEnglish
    Pages (from-to)463-471
    Number of pages9
    JournalOrganic and Biomolecular Chemistry
    Volume1
    Issue number3
    DOIs
    Publication statusPublished - 7 Feb 2003

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