Structural Studies of Glutamate Dehydrogenase (Isoform 1) From Arabidopsis thaliana, an Important Enzyme at the Branch-Point Between Carbon and Nitrogen Metabolism.

ABSTRACT: Glutamate dehydrogenase (GDH) releases ammonia in a reversible NAD(P)⁺-dependent oxidative deamination of glutamate that yields 2-oxoglutarate (2OG). In current perception, GDH contributes to Glu homeostasis and plays a significant role at the junction of carbon and nitrogen assimilation pathways. GDHs are members of a superfamily of ELFV (Glu/Leu/Phe/Val) amino acid dehydrogenases and are subdivided into three subclasses, based on coenzyme specificity: NAD⁺-specific, NAD⁺/NADP⁺ dual-specific, and NADP⁺-specific. We determined in this work that the mitochondrial AtGDH1 isozyme from A. thaliana is NAD⁺-specific. Altogether, A. thaliana expresses three GDH isozymes (AtGDH1-3) targeted to mitochondri

SUBMITTER: Grzechowiak M 

PROVIDER: S-EPMC7326016 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature