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Purification and characterization of the acyl carrier protein of the streptomyces-glaucescens tetracenomycin-c polyketide synthase

Academic Article
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Overview

authors

  • Shen, Ben
  • Summers, R. G.
  • Gramajo, H.
  • Bibb, M. J.
  • Hutchinson, C. R.

publication date

  • June 1992

journal

  • Journal of Bacteriology  Journal

abstract

  • The acyl carrier protein (ACP) of the tetracenomycin C polyketide synthase, encoded by the tcmM gene, has been expressed in both Streptomyces glaucescens and Escherichia coli and purified to homogeneity. Expression of the tcmM gene in E. coli results mainly in the TcmM apo-ACP, whereas expression in S. glaucescens yields solely the holo-ACP. The purified holo-TcmM is active in a malonyl coenzyme A:ACP transacylase assay and is labeled by radioactive beta-alanine, confirming that it carries a 4'-phosphopantetheine prosthetic group.

subject areas

  • Acyl Carrier Protein
  • Amino Acid Sequence
  • Apoproteins
  • Base Sequence
  • Escherichia coli
  • Molecular Sequence Data
  • Multienzyme Complexes
  • Naphthacenes
  • Sequence Homology, Nucleic Acid
  • Streptomyces
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Identity

PubMed Central ID

  • PMC206074

International Standard Serial Number (ISSN)

  • 0021-9193

PubMed ID

  • 1592832
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Additional Document Info

start page

  • 3818

end page

  • 3821

volume

  • 174

issue

  • 11

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