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An alternative pentose phosphate pathway in human gut bacteria for the degradation of C5 sugars in dietary fibers
Author(s) -
Garschagen Laura S.,
Franke Thomas,
Deppenmeier Uwe
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15511
Subject(s) - transaldolase , pentose phosphate pathway , transketolase , pentose , biochemistry , biology , metabolic pathway , xylose metabolism , microbial metabolism , firmicutes , bacteria , chemistry , enzyme , xylose , microbiology and biotechnology , glycolysis , fermentation , genetics , 16s ribosomal rna , gene
Several gut bacteria do not convert pentoses via the well‐known pentose phosphate pathway because one of the key enzymes—the transaldolase—is absent. We demonstrated that the transaldolase reaction in Prevotella copri is replaced by the combined reaction of the pyrophosphate‐dependent phosphofructokinase and the fructose‐bisphosphate aldolase. This biochemical route is referred to as sedoheptulose 1,7‐phosphate pathway and is widespread in the gut microbiota.