Characterization of the calicheamicin orsellinate C2-O-methyltransferase CalO6

Shanteri Singh, Nitin S. Nandurkar, Jon S. Thorson

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Although bacterial iterative type I polyketide synthases are now known to participate in the biosynthesis of a small set of diverse natural products, the subsequent downstream modification of the resulting polyketide products is poorly understood. We report the functional characterization of the putative orsellinic acid C2-O-methyltransferase, which is involved in calicheamicin biosynthesis. This study suggests that C2-O-methylation precedes C3-hydroxylation/methylation and C5-iodination and requires a coenzyme A- or acyl carrier protein-bound substrate.

Original languageEnglish
Pages (from-to)1418-1421
Number of pages4
Issue number10
StatePublished - Jul 7 2014


  • AdoMet
  • S-adenosylmethionine
  • acyl carrier proteins
  • iterative PKSs
  • orsellinic acid
  • polyketides

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry


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