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Publication Abstract from PubMed

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.

Crystal Structures of 6-Phosphogluconate Dehydrogenase from Corynebacterium glutamicum.,Yu H, Hong J, Seok J, Seu YB, Kim IK, Kim KJ J Microbiol Biotechnol. 2023 Oct 28;33(10):1361-1369. doi: , 10.4014/jmb.2305.05002. Epub 2023 Jun 27. PMID:37417004^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.