Phosphorylation-mediated regulation of the NADPH-dependent glutamate dehydrogenase, SpGdh1, from Schizosaccharomyces pombe.

ABSTRACT: Glutamate dehydrogenase from the 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 SpGdh1 is phosphorylated at several residues, the impact of phosphorylation on enzyme activity and the underlying molecular mechanisms remains unclear. To elucidate the phosphorylation-mediated regulation of SpGdh1, we determined the crystal structure of SpGdh1 binding 2-iminoglutarate (2-IG) and NADP⁺. The results of the structural analysis revealed that four serine residues for phosphorylation were located near the active site. Ser252 directly interacted with the 2'-phosphate group of the adenine ribose moiety of NADP⁺, suggesting that the phosphorylation of Ser252

SUBMITTER: Wang YF 

PROVIDER: S-EPMC12301742 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature