Christopher T. Calderone Copyright (c) 2011 All rights reserved. http://works.bepress.com/christopher_calderone Recent documents in Christopher T. Calderone en-us Wed, 22 Jun 2011 09:55:28 PDT 3600 Poster: Characterization of Enzymes Involved in Biosynthesis of the Hydroxamate-Containing Siderophore Triacetylfusarinine C in Aspergillus nidulans http://works.bepress.com/christopher_calderone/7 http://works.bepress.com/christopher_calderone/7 Fri, 03 Jun 2011 10:02:55 PDT


]]> Christopher T. Calderone et al. Poster: Towards the Characterization of Prenylation of the Sirodesmin Precursor Phomamide in Leptosphaeria maculans. http://works.bepress.com/christopher_calderone/6 http://works.bepress.com/christopher_calderone/6 Fri, 03 Jun 2011 09:58:25 PDT


]]> Christopher T. Calderone et al. Cloning and Expression of Truncated Polyketide Synthase Enzymes for Structural Analysis. http://works.bepress.com/christopher_calderone/5 http://works.bepress.com/christopher_calderone/5 Tue, 07 Sep 2010 12:59:31 PDT


]]> Christopher T. Calderone et al. Expression of Protein involved in Siderophore Biosynthesis in Aspergillus nidulans. http://works.bepress.com/christopher_calderone/4 http://works.bepress.com/christopher_calderone/4 Tue, 07 Sep 2010 12:57:42 PDT


]]> Christopher T. Calderone et al. 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 et al. 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 et al.