A two-step sulfation in antibiotic biosynthesis requires a type III polyketide synthase

Nat Chem Biol. 2013 Oct;9(10):610-5. doi: 10.1038/nchembio.1310. Epub 2013 Aug 4.

Abstract

Caprazamycins (CPZs) belong to a group of liponucleoside antibiotics inhibiting the bacterial MraY translocase, an essential enzyme involved in peptidoglycan biosynthesis. We have recently identified analogs that are decorated with a sulfate group at the 2″-hydroxy of the aminoribosyl moiety, and we now report an unprecedented two-step sulfation mechanism during the biosynthesis of CPZs. A type III polyketide synthase (PKS) known as Cpz6 is used in the biosynthesis of a group of new triketide pyrones that are subsequently sulfated by an unusual 3'-phosphoadenosine-5'-phosphosulfate (PAPS)-dependent sulfotransferase (Cpz8) to yield phenolic sulfate esters, which serve as sulfate donors for a PAPS-independent arylsulfate sulfotransferase (Cpz4) to generate sulfated CPZs. This finding is to our knowledge the first demonstration of genuine sulfate donors for an arylsulfate sulfotransferase and the first report of a type III PKS to generate a chemical reagent in bacterial sulfate metabolism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / classification
  • Acyltransferases / metabolism*
  • Anti-Bacterial Agents / biosynthesis*
  • Anti-Bacterial Agents / chemistry
  • Molecular Structure
  • Sulfates / chemistry
  • Sulfates / metabolism*

Substances

  • Anti-Bacterial Agents
  • Sulfates
  • Acyltransferases
  • flavanone synthetase

Associated data

  • PubChem-Substance/163691595
  • PubChem-Substance/163691596
  • PubChem-Substance/163691597
  • PubChem-Substance/163691598
  • PubChem-Substance/163691599
  • PubChem-Substance/163691600