Purification and characterization of the acyl carrier protein of the Streptomyces glaucescens tetracenomycin C polyketide synthase.

作者: B Shen , R G Summers , H Gramajo , M J Bibb , C R Hutchinson

DOI: 10.1128/JB.174.11.3818-3821.1992

关键词: Malonyl Coenzyme AEscherichia coliStreptomycesAcyl carrier proteinCofactorStreptomycetaceaePolyketide synthaseBiologyBiochemistryActinomycetales

摘要: The acyl carrier protein (ACP) of the tetracenomycin C polyketide synthase, encoded by tcmM gene, has been expressed in both Streptomyces glaucescens and Escherichia coli purified to homogeneity. Expression gene E. results mainly TcmM apo-ACP, whereas expression S. yields solely holo-ACP. holo-TcmM is active a malonyl coenzyme A:ACP transacylase assay labeled radioactive beta-alanine, confirming that it carries 49-phosphopantetheine prosthetic group. Images

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