Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinone

Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinone

The RquA protein is required for rhodoquinone biosynthesis; however, its exact function is not yet known. Here, the authors demonstrate that RquA is homologous to SAM-dependent methyltransferases but functions as an aminotransferase using Mn2+ as cofactor to convert ubiquinone to rhodoquinone.

Bibliographic Details
Main Authors: Trilok Neupane, Lydia R. Chambers, Alexander J. Godfrey, Melina M. Monlux, Evan J. Jacobs, Sophia Whitworth, Jamie E. Spawn, Seo Hee K. Clingman, Kathleen L. Vergunst, Fair M. Niven, James J. Townley, Iris W. Orion, Carly R. Goodspeed, Kathryn A. Cooper, Jeff D. Cronk, Jennifer N. Shepherd, David N. Langelaan
Format: Article
Language:English
Published: Nature Portfolio 2022-08-01
Series:Communications Chemistry
Online Access:https://doi.org/10.1038/s42004-022-00711-6

Internet

https://doi.org/10.1038/s42004-022-00711-6

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