title: In vitro reconstitution of the radical S-adenosylmethionine enzyme MqnC involved in the biosynthesis of futalosine-derived menaquinone.
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.
authors.affiliation: Department of Chemistry, Texas A&M University , College Station, Texas 77842, United States.
authors.forename: Lisa E
authors.initials: LE
authors.lastname: Cooper
authors.forename: Dmytro
authors.initials: D
authors.lastname: Fedoseyenko
authors.forename: Sameh H
authors.initials: SH
authors.lastname: Abdelwahed
authors.forename: Soong-Hyun
authors.initials: SH
authors.lastname: Kim
authors.forename: Tohru
authors.initials: T
authors.lastname: Dairi
authors.forename: Tadhg P
authors.initials: TP
authors.lastname: Begley
mesh_terms: D002851:Chromatography, High Pressure Liquid; D006867:Hydrolases / Q000378:metabolism*; D066298:In Vitro Techniques; D009705:Nucleosides / Q000378:metabolism*; D024482:Vitamin K 2 / Q000378:metabolism*
chemical_list: D009705:Nucleosides; C122040:futalosine; D024482:Vitamin K 2; D006867:Hydrolases; C019614:adenosylmethionine hydrolase