Christopher T. Calderone Copyright (c) 2009 All rights reserved. http://works.bepress.com/christopher_calderone Recent documents in Christopher T. Calderone en-us Sun, 31 May 2009 04:24:50 PDT 3600 Polyunsaturated fatty-acid-like trans-enoyl reductases utilized in polyketide biosynthesis http://works.bepress.com/christopher_calderone/3 http://works.bepress.com/christopher_calderone/3 Mon, 05 Jan 2009 10:06:12 PST Polyketide biosynthesis is typically directed by cis-acting catalytic domains. In the case of the Bacillus subtilis secondary metabolite dihydrobacillaene, the cis-acting domains are not sufficient to generate the saturated C14′−C15′ bond. In this communication, we identify PksE as a trans-acting enoyl reductase utilized in the biosynthesis of this portion of dihydrobacillaene. PksE is homologous to the enzymes predicted to serve as enoyl reductases in polyunsaturated fatty acid (PUFA) biosynthesis, and we confirmed this functional assignment in vitro. These results suggest a general enoyl reduction pathway in polyketide biosynthesis and a means by which PUFA-like biosynthetic machinery can modulate small-molecule function. Stephanie B. Bumpus Isoprenoid-like alkylations in polyketide biosynthesis http://works.bepress.com/christopher_calderone/2 http://works.bepress.com/christopher_calderone/2 Mon, 05 Jan 2009 09:59:44 PST Christopher T. Calderone A ketoreductase domain in the PksJ protein of the bacillaene assembly line carries out both α- and β-ketone reduction during chain growth http://works.bepress.com/christopher_calderone/1 http://works.bepress.com/christopher_calderone/1 Mon, 05 Jan 2009 09:50:30 PST Christopher T. Calderone