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In vitro reconstitution of the radical S-adenosylmethionine enzyme MqnC involved in the biosynthesis of futalosine-derived menaquinone
Chemistry & Physics Faculty Publications
  • Lisa E. Cooper, Texas A&M University
  • Dmytro Fedoseyenko, Texas A&M University
  • Sameh H. Abdelwahed, Texas A&M University
  • Soong Hyun Kim, Texas A&M University
  • Tohru Dairi, Hokkaido University
  • Tadhg P. Begley, Texas A&M University
Document Type
Article
Publication Date
7-9-2013
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. © 2013 American Chemical Society.

Citation Information
Lisa E. Cooper, Dmytro Fedoseyenko, Sameh H. Abdelwahed, Soong Hyun Kim, et al.. "In vitro reconstitution of the radical S-adenosylmethionine enzyme MqnC involved in the biosynthesis of futalosine-derived menaquinone" (2013)
Available at: http://works.bepress.com/Sameh-Abdelwahed/15/