Abstract
Widely distributed among prokaryotes, short chain fatty acid kinases provide a path for fatty acid entry into central metabolic pathways. These enzymes catalyze the reversible, ATP-dependent synthesis of acyl-phosphates, which leads to the production of acyl-CoA derivatives by a coordinate acyltransferase. To date, characterized representatives of short chain fatty acid kinases exhibit relatively narrow substrate specificity. In this work, biochemical characterization of a predicted acetate kinase from Rhodobacter sphaeroides reveals a novel enzyme with broad substrate specificity for primary fatty acids of varying lengths (C2-–C8).
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Acknowledgements
The authors would like to thank the following for financial support of this work: the Scott and Alice Thomson Fellowship Program (award to MJB), the UW-Parkside Committee on Research and Creative Activity, and the UW-Parkside College of Natural and Health Sciences.
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Investigation was performed by MVA (molecular cloning and pH experiments) and MJB (temperature, substrate specificity and kinetics). RDB contributed conceptualization and resources for the project. MJB and RDB prepared the manuscript for publication.
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Communicated by Johann Heider.
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Bachochin, M.J., Van Allen, M. & Barber, R.D. Characterization of a Rhodobacter sphaeroides primary fatty acid kinase. Arch Microbiol 203, 861–864 (2021). https://doi.org/10.1007/s00203-020-02055-y
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DOI: https://doi.org/10.1007/s00203-020-02055-y