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Crystal Structures of 6-Phosphogluconate Dehydrogenase from

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Date 2023 Jul 7
PMID 37417004
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Abstract

() has been considered a very important and meaningful industrial microorganism for the production of amino acids worldwide. To produce amino acids, cells require nicotinamide adenine dinucleotide phosphate (NADPH), which is a biological reducing agent. The pentose phosphate pathway (PPP) can supply NADPH in cells via the 6-phosphogluconate dehydrogenase (6PGD) enzyme, which is an oxidoreductase that converts 6-phosphogluconate (6PG) to ribulose 5-phosphate (Ru5P), to produce NADPH. In this study, we identified the crystal structure of 6PGD_apo and 6PGD_NADP from ATCC 13032 (6PGD) and reported our biological research based on this structure. We identified the substrate binding site and co-factor binding site of 6PGD, which are crucial for understanding this enzyme. Based on the findings of our research, 6PGD is expected to be used as a NADPH resource in the food industry and as a drug target in the pharmaceutical industry.

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