Recent Advances in the Structural and Functional Properties of Glutamate Dehydrogenase
A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Enzymology".
Deadline for manuscript submissions: 30 September 2024 | Viewed by 110
Special Issue Editor
Interests: glutamate dehydrogenase; neurodegeneration; enzymatic properties; structure-funcion relationships;
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Glutamate dehydrogenase (GDH) interconverts glutamate to a-ketoglutarate and ammonia. As it plays a crucial role in the interconnecting carbon and nitrogen metabolism, it is found in almost all living organisms. In eukaryotes, GDH is prominently expressed in the mitochondrial matrix, involved in the coupling of glutamate metabolism with energy homeostasis. In addition to the GLUD1 gene (encoding for hGDH1), humans and other apes possess GLUD2 (encoding for hGDH2), an intronless X-linked gene that has evolved through retroposition during primate evolution. In addition to distinct enzymatic and regulatory properties, hGDH2 displays a unique expression pattern compared to hGDH1. These distinct hGDH2 properties suggest a divergent role in nervous and other tissue function that remains to be elucidated. As the two hGDH iso-enzymes are involved in the pathogenesis of metabolic, neurodegenerative, and neoplastic disorders, they have been drawing increasing interest. The 3D structure of hGDH1, hGDH2, and the structures of several other mammalian and non-mammalian GDH1s were determined by X-ray crystallography. These studies show that the mammalian GDH is a symmetric homo-hexamer, with each subunit consisting of the glutamate-binding domain, the NAD+-binding domain, and the regulatory domain. Still, there is more research needed to better delineate structure-function relationships in GDH enzymes.
The aim of this Special Issue is to showcase recent advances in the field of the structure and function of GDH across species, and to display how these advances translate to a better understanding of human physiology and pathophysiology.
Dr. Ioannis Zaganas
Guest Editor
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Keywords
- glutamate dehydrogenase
- GLUD1
- GLUD2
- structure-function relationships
- neurodegenerative disorders
