Substrate specificity of the loading didomain of the erythromycin polyketide synthase

A study that is an attractive prototype for the expression, analysis and engineering of acyltransferase domains in modular polyketide synthases has been carried out to look at substrate specificity of the loading didomain of the erythromycin polyketide synthase. The loading didomain of 6-deoxyerythronolide B synthase (DEBS) can accept a broad range of substrates. Sfp was found to efficiently modify the acyl carrier protein (ACP(sub.L)) domain of the acyltransferase (AT(sub.L))-ACP(sub.L) protein with phosphopantetheine in vivo. The holo-enzyme that resulted was tested against various substrates to study its ability to discriminate between structurally different primer units.