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Evaluation of electron-transferring cofactor mediating enzyme systems involved in urolithin dehydroxylation in Gordonibacter urolithinfaciens DSM 27213.

Authors :
Watanabe, Hiroko
Kishino, Shigenobu
Kudoh, Masatake
Yamamoto, Hiroaki
Ogawa, Jun
Source :
Journal of Bioscience & Bioengineering. May2020, Vol. 129 Issue 5, p552-557. 6p.
Publication Year :
2020

Abstract

The gut bacterium Gordonibacter urolithinfaciens DSM 27213 metabolizes ellagic acid into three polyphenol compounds, namely, urolithin M5, urolithin M6, and urolithin C, which are collectively called urolithin. The key reactions of this metabolic pathway are the dehydroxylation of the phenolic hydroxy group, i.e., conversion of urolithin M5 to urolithin M6, and successive conversion of urolithin M6 to urolithin C. By testing the effects of various electron-transferring compounds on the dehydroxylation reactions, methylviologen was found to effectively support the dehydroxylation catalyzed by the cell free extracts. The urolithin dehydroxylating enzymes were found in the soluble fraction of the cell free extracts. The urolithin dehydroxylation was found to be coupled with reduction of dicationic methylviologen to a cation radical form catalyzed by enzymes with hydrogen as an electron donor, which was also found with the soluble fraction. Further investigation of the reaction in the presence of natural cofactors with or without methylviologen and hydrogen revealed the involvement of NADPH and FAD in the electron transportation systems of the urolithin dehydroxylation. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
13891723
Volume :
129
Issue :
5
Database :
Academic Search Index
Journal :
Journal of Bioscience & Bioengineering
Publication Type :
Academic Journal
Accession number :
142536790
Full Text :
https://doi.org/10.1016/j.jbiosc.2019.11.014