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• W1514973939 abstract "Enediyne natural products are extremely potent antitumor antibiotics with a remarkable core structure consisting of two acetylenic groups conjugated to a double bond within either a 9‐ or 10‐membered ring. Biosynthesis of this fascinating scaffold is catalyzed in part by an unusual iterative type I polyketide synthase, PKSE, that is shared among all enediyne biosynthetic pathways whose gene clusters have been sequenced to date. The PKSE is unusual in two main respects: (1) it contains an acyl carrier protein (ACP) domain with no sequence homology to any known proteins, and (2) it is self‐phosphopantetheinylated by an integrated phosphopantetheinyl transferase (PPTase) domain. The unusual domain architecture and biochemistry of the PKSE hold promise both for the rapid identification of new enediyne natural products and for obtaining fundamental catalytic insights into enediyne biosynthesis. This chapter describes methods for rapid PCR‐based classification of conserved enediyne biosynthetic genes, heterologous production of 9‐membered PKSE proteins and isolation of the resulting polyene product, and in vitro characterization of the PKSE ACP domain." @default.
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• W1514973939 date "2009-01-01" @default.
• W1514973939 modified "2023-10-18" @default.
• W1514973939 title "chapter 5 Iterative Type I Polyketide Synthases for Enediyne Core Biosynthesis" @default.
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• W1514973939 doi "https://doi.org/10.1016/s0076-6879(09)04605-9" @default.
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