In vitro reconstitution of the radical S-adenosylmethionine enzyme MqnC involved in the biosynthesis of futalosine-derived menaquinone

Biochemistry. 2013 Jul 9;52(27):4592-4. doi: 10.1021/bi400498d. Epub 2013 Jun 27.

Abstract

The radical S-adenosylmethionine enzyme MqnC catalyzes conversion of dehypoxanthine futalosine (DHFL) to the unique spiro compound cyclic DHFL in the futalosine pathway for menaquinone biosynthesis. This study describes the in vitro reconstitution of [4Fe-4S] cluster-dependent MqnC activity and identifies the site of abstraction of a hydrogen atom from DHFL by the adenosyl radical.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, High Pressure Liquid
  • Hydrolases / metabolism*
  • In Vitro Techniques
  • Nucleosides / metabolism*
  • Vitamin K 2 / metabolism*

Substances

  • Nucleosides
  • futalosine
  • Vitamin K 2
  • Hydrolases
  • adenosylmethionine hydrolase