{Reference Type}: Journal Article
{Title}: Crystal Structures of 6-Phosphogluconate Dehydrogenase from Corynebacterium glutamicum.
{Author}: Yu H;Hong J;Seok J;Seu YB;Kim IK;Kim KJ;
{Journal}: J Microbiol Biotechnol
{Volume}: 33
{Issue}: 10
{Year}: 2023 Oct 28
{Factor}: 3.277
{DOI}: 10.4014/jmb.2305.05002
{Abstract}: Corynebacterium glutamicum (C. glutamicum) 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 C. glutamicum ATCC 13032 (Cg6PGD) and reported our biological research based on this structure. We identified the substrate binding site and co-factor binding site of Cg6PGD, which are crucial for understanding this enzyme. Based on the findings of our research, Cg6PGD is expected to be used as a NADPH resource in the food industry and as a drug target in the pharmaceutical industry.