Characterization of the calicheamicin orsellinate C2-O-methyltransferase CalO6

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

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

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
JournalChemBioChem
Volume15
Issue number10
DOIs
StatePublished - Jul 7 2014

Funding

FundersFunder number
National Center for Advancing Translational Sciences (NCATS)UL1TR000117
National Institutes of Health (NIH)RO1 CA84374
National Childhood Cancer Registry – National Cancer InstituteR01CA084374

    Keywords

    • 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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