Glutamate dehydrogenase 1 (GDH1) is an enzyme that is a key metabolic regulator in that it provides oxoglutarate for the Krebs cycle. It also plays a key role in the progression of type-2 diabetes. GDH1 is allosterically regulated by various small molecules, such as GTP, ADP, leucine, and palmitoyl-CoA, in higher order organisms. The [2Fe-2S] cluster protein mitoNEET, that is also a type-2 diabetes drug target, has been shown to activate GDH1. We examined the impact of the protein mitoNEET on the allostery of GDH1 to determine if these two classes of regulators act with synergy or interdependent of each other. Additionally, GDH1 may be able to metabolize the product of a mitoNEET catalyzed reaction. These studies will elucidate the interplay of these two proteins indicated to contribute to type-2 diabetes progression.

Impact of mitoNEET binding on GDH1 allostery

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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