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.
Main Authors: | , , , , , , , , , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2022-08-01
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Series: | Communications Chemistry |
Online Access: | https://doi.org/10.1038/s42004-022-00711-6 |
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author | 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 |
author_facet | 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 |
author_sort | Trilok Neupane |
collection | DOAJ |
description | 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. |
first_indexed | 2024-04-11T21:35:03Z |
format | Article |
id | doaj.art-b2e554daf1fb49c2b8306775749eb555 |
institution | Directory Open Access Journal |
issn | 2399-3669 |
language | English |
last_indexed | 2024-04-11T21:35:03Z |
publishDate | 2022-08-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Communications Chemistry |
spelling | doaj.art-b2e554daf1fb49c2b8306775749eb5552022-12-22T04:01:47ZengNature PortfolioCommunications Chemistry2399-36692022-08-015111310.1038/s42004-022-00711-6Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinoneTrilok Neupane0Lydia R. Chambers1Alexander J. Godfrey2Melina M. Monlux3Evan J. Jacobs4Sophia Whitworth5Jamie E. Spawn6Seo Hee K. Clingman7Kathleen L. Vergunst8Fair M. Niven9James J. Townley10Iris W. Orion11Carly R. Goodspeed12Kathryn A. Cooper13Jeff D. Cronk14Jennifer N. Shepherd15David N. Langelaan16Department of Biochemistry & Molecular Biology, Dalhousie UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Biochemistry & Molecular Biology, Dalhousie UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Chemistry and Biochemistry, Gonzaga UniversityDepartment of Biochemistry & Molecular Biology, Dalhousie UniversityThe 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.https://doi.org/10.1038/s42004-022-00711-6 |
spellingShingle | 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 Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinone Communications Chemistry |
title | Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinone |
title_full | Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinone |
title_fullStr | Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinone |
title_full_unstemmed | Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinone |
title_short | Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinone |
title_sort | microbial rhodoquinone biosynthesis proceeds via an atypical rqua catalyzed amino transfer from s adenosyl l methionine to ubiquinone |
url | https://doi.org/10.1038/s42004-022-00711-6 |
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