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

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

• Begley, Tadhg

published proceedings

• Biochemistry

altmetric score

• 3

author list (cited authors)

• Cooper, L. E., Fedoseyenko, D., Abdelwahed, S. H., Kim, S., Dairi, T., & Begley, T. P.

citation count

• 32

complete list of authors

• Cooper, Lisa E||Fedoseyenko, Dmytro||Abdelwahed, Sameh H||Kim, Soong-Hyun||Dairi, Tohru||Begley, Tadhg P

publication date

• July 2013

publisher

• American Chemical Society (ACS)  Publisher

published in

• Biochemistry  Journal

keywords

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

PubMed Central ID

• 23763543

Digital Object Identifier (DOI)

• 10.1021/bi400498d

start page

• 4592

end page

• 4594

volume

• 52

issue

• 27

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fbi400498d