PMID:9545424

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Citation

Tropf, S, Revill, WP, Bibb, MJ, Hopwood, DA and Schweizer, M (1998) Heterologously expressed acyl carrier protein domain of rat fatty acid synthase functions in Escherichia coli fatty acid synthase and Streptomyces coelicolor polyketide synthase systems. Chem. Biol. 5:135-46

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.

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Keywords

Acyl Carrier Protein/genetics; Acyl Carrier Protein/isolation & purification; Acyl Carrier Protein/metabolism; Animals; Carbon Radioisotopes; Chromatography, Thin Layer; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Fatty Acid Synthetase Complex/chemistry; Fatty Acid Synthetase Complex/metabolism; Mass Spectrometry; Multienzyme Complexes/chemistry; Multienzyme Complexes/metabolism; Protein Processing, Post-Translational; Rats; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Streptomyces/enzymology

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