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Specificity of the ester bond forming condensation enzyme sgcc5 in c-1027 biosynthesis

Academic Article
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Overview

authors

  • Lin, S. J.
  • Huang, T. T.
  • Horsman, G. P.
  • Huang, S. X.
  • Guo, X.
  • Shen, Ben

publication date

  • May 2012

journal

  • Organic Letters  Journal

abstract

  • The SgcC5 condensation enzyme catalyzes the attachment of SgcC2-tethered (S)-3-chloro-5-hydroxy-β-tyrosine (2) to the enediyne core in C-1027 (1) biosynthesis. It is reported that SgcC5 (i) exhibits high stereospecificity toward the (S)-enantiomers of SgcC2-tethered β-tyrosine and analogues as donors, (ii) prefers the (R)-enantiomers of 1-phenyl-1,2-ethanediol (3) and analogues, mimicking the enediyne core, as acceptors, and (iii) can recognize a variety of donor and acceptor substrates to catalyze their regio- and stereospecific ester bond formations.

subject areas

  • Aminoglycosides
  • Catalysis
  • Citrate (si)-Synthase
  • Combinatorial Chemistry Techniques
  • Enediynes
  • Molecular Structure
  • Peptide Synthases
  • Stereoisomerism
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Identity

PubMed Central ID

  • PMC3345089

International Standard Serial Number (ISSN)

  • 1523-7060

Digital Object Identifier (DOI)

  • 10.1021/ol300720s

PubMed ID

  • 22519717
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Additional Document Info

start page

  • 2300

end page

  • 2303

volume

  • 14

issue

  • 9

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