Abstract 1494 Phosphorylation-mediated regulation of NADPH-dependent glutamate dehydrogenase, SpGdh1, from Schizosaccharomyces pombe

Glutamate dehydrogenase from yeast Schizosaccharomyces pombe (SpGdh1) is a pivotal enzyme that catalyzes the conversion of 2-oxoglutarate and ammonium to glutamate using NADPH as a coenzyme. Although a phosphoproteomics analysis reported that SpGdh1 was phosphorylated at several residues, the impact of the phosphorylation on the enzyme activity and the underlying molecular mechanism remains unclear. This study aims to elucidate the phosphorylation-mediated regulatory mechanism of SpGdh1. We determined the high-resolution crystal structure of SpGdh1 binding 2-iminoglutarate and NADP+ at 1.45 Å resolution.