PMID:2676605

Citation	Bayan, N and Thérisod, H (1989) Evidence for interactions of acyl carrier protein with glycerol-3-phosphate acyltransferase, an inner membrane protein of Escherichia coli. FEBS Lett. 255:330-4
Abstract	We [(1989) FEBS Lett., in press] have previously shown that membrane vesicles from Escherichia coli contain protein-binding sites for the acyl carrier protein (ACP). We report now that membrane vesicles prepared from a strain amplified for glycerol-3-phosphate acyltransferase (GPAT) contain a higher number of ACP-binding sites than the membrane vesicles prepared from a wild type strain. In addition, we show that GPAT is retained specifically on an ACP-Sepharose affinity column and that [3H]ACP binds to the enzyme solubilized by detergent. We conclude that GPAT, an inner membrane protein which catalyses the transesterification of a fatty acyl group from acyl coenzyme A or acyl ACP to glycerol-3-phosphate, possesses a binding site for ACP.
Links	PubMed
Keywords	Acyl Carrier Protein/metabolism; Acyltransferases/metabolism; Binding Sites; Cell Membrane/enzymology; Chromatography, Affinity; Escherichia coli/enzymology; Glycerol-3-Phosphate O-Acyltransferase/isolation & purification; Glycerol-3-Phosphate O-Acyltransferase/metabolism; Kinetics; Molecular Weight; Protein Binding
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