Dataset for: 6-Phosphogluconolactonase is critical for the efficient functioning of the pentose phosphate pathway

Published: 14 June 2024| Version 1 | DOI: 10.17632/2rw5pz75yr.1
, Julien Pérochon,
, Fabien Letisse


In the oxidative branch of the pentose-phosphate pathway (oxPPP), a virtually ubiquitous metabolic pathway in eukaryotes and most bacteria, 6-phosphogluconolactone hydrolysis into 6-phosphogluconate is catalysed by 6-phosphogluconolactonase (Pgl) but in the absence of the latter, the oxPPP flux is thought to be maintained by spontaneous hydrolysis. However, in Deltapgl Escherichia coli, an extracellular pathway can also contribute to pentose-phosphate synthesis. This raises question as to whether a non-enzymatic reaction can compensate for the absence of 6-phosphogluconolactonase and, ultimately, on the role of 6-phosphogluconolactonase in central metabolism. Our results indicate that in the absence of Pgl, this bypass pathway accounts for the entire flux into the oxPPP, suggesting that non-enzymatic hydrolysis does not compensate for the absence of Pgl and demonstrating that Pgl is critical for an efficiently functioning oxPPP.