PMID: 9545424Apr 18, 1998Paper

Heterologously expressed acyl carrier protein domain of rat fatty acid synthase functions in Escherichia coli fatty acid synthase and Streptomyces coelicolor polyketide synthase systems

Chemistry & Biology
S TropfM Schweizer

Abstract

Fatty acid synthases (FASs) catalyze the de novo biosynthesis of long-chain saturated fatty acids by a process common to eubacteria and eukaryotes, using either a set of monofunctional proteins (Type II FAS) or a polypeptide containing several catalytic functions (Type I FAS). To compare the features of a Type I domain with its Type II counterpart we expressed and characterized an acyl carrier protein (ACP) domain of the Type I rat FAS. An ACP domain of rat FAS was defined that allows expression of a small percentage of active holo-ACP both in Escherichia coli, increasing fivefold upon co-expression with an E. coli holo-ACP synthase, and in Streptomyces coelicolor. The rat ACP domain functions with some components of the E. coli FAS, and can replace the actinorhodin polyketide synthase (PKS) ACP in S. coelicolorA3(2). Purification of the rat ACP domain from E. coli resulted in loss of its functionality. Purified apo-ACP could be converted to its holo-form upon incubation with purified E. coli holo-ACP synthase in vitro, however, suggesting that the loss of functionality was not due to a conformational change. Functionality of the recombinant rat ACP was shown in distantly related and diverse enzyme systems, suggesting that Type...Continue Reading

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Citations

Apr 12, 2003·Progress in Lipid Research·Stuart SmithAnil K Joshi
Jun 15, 2005·Annual Review of Biochemistry·Stephen W White Rock
Oct 25, 2008·Current Opinion in Structural Biology·Marc LeibundgutNenad Ban
Aug 10, 2013·Biotechnology and Bioengineering·Christopher Leber, Nancy A Da Silva
Jul 29, 2010·The Biochemical Journal·David I Chan, Hans J Vogel
Jan 6, 2011·FEMS Microbiology Reviews·Gabriela GagoHugo Gramajo
Nov 1, 2007·The Journal of Biological Chemistry·Eliza PloskońMatthew P Crump
May 22, 2019·Nature Communications·Samuel C EpsteinLouise K Charkoudian

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