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The bifunctional glyceryl transferase/phosphatase ozmb belonging to the had superfamily that diverts 1,3-bisphosphoglycerate into polyketide biosynthesis

Academic Article
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Overview

authors

  • Dorrestein, P. C.
  • Van Lanen, S. G.
  • Li, W. L.
  • Zhao, C. H.
  • Deng, Z. X.
  • Shen, Ben
  • Kelleher, N. L.

publication date

  • August 2006

journal

  • Journal of the American Chemical Society  Journal

abstract

  • The HAD superfamily protein OzmB from the oxazolomycin biosynthetic pathway is shown to divert the primary metabolite 1,3-diphosphoglycerate into the polyketide biosynthetic pathway as glycerate via loading of a carrier protein. Each of the steps-activation of d-3-phosphoglycerate, dephosphorylation while attached to a cysteine on OzmB, and subsequent transfer of glycerate to the phosphopantetheinyl thiol of an acyl carrier protein-was monitored by nanospray Fourier transform mass spectrometry. This activation of phosphoglycerate represents a general mechanism of diverting glycolytic metabolites into glyceryl-derived polyketides.

subject areas

  • Amino Acid Sequence
  • Diphosphoglyceric Acids
  • Enzyme Activation
  • Macrolides
  • Methyltransferases
  • Molecular Sequence Data
  • Oxazoles
  • Phosphoric Monoester Hydrolases
  • Pyrans
  • Pyrrolidinones
  • Sequence Alignment
  • Spiro Compounds
  • Substrate Specificity
  • Transferases
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja0639362

PubMed ID

  • 16895402
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Additional Document Info

start page

  • 10386

end page

  • 10387

volume

  • 128

issue

  • 32

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