The Mitochondrial Protein MitoNEET as a Probe for the Allostery of Glutamate Dehydrogenase.

ABSTRACT: The proteins glutamate dehydrogenase (GDH) and mitoNEET are both targets of drug development efforts to treat metabolic disorders, cancer, and neurodegenerative diseases. However, these two proteins differ starkly in the current knowledge about ligand binding sites. MitoNEET is a [2Fe-2S]-containing protein with no obvious binding site for small ligands observed in its crystal structures. In contrast, GDH is known to have a variety of ligands at multiple allosteric sites thereby leading to complex regulation in activity. In fact, while GDH can utilize either NAD(H) or NADP(H) for catalysis at the active site, only NAD(H) binds at a regulatory site to inhibit GDH activity. Previously, we found that mitoNEET forms a covalent bond with GDH in vitro and increases the catalytic activity of the

SUBMITTER: Nnatubeugo C 

PROVIDER: S-EPMC9737137 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature