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Neurochem Res. 2019 Jan;44(1):117-132. doi: 10.1007/s11064-017-2428-0. Epub 2017 Oct 27.

Glutamate Dehydrogenase, a Complex Enzyme at a Crucial Metabolic Branch Point.

Author information

1
Department of Biochemistry and Molecular Biology, University of Texas Medical Branch at Galveston, Galveston, TX, USA.
2
Division of Endocrinology, The Children's Hospital of Philadelphia, Philadelphia, PA, USA.
3
Department of Biochemistry and Molecular Biology, University of Texas Medical Branch at Galveston, Galveston, TX, USA. thosmith@UTMB.EDU.

Abstract

In-vitro, glutamate dehydrogenase (GDH) catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate (α-KG). GDH is found in all organisms, but in animals is allosterically regulated by a wide array of metabolites. For many years, it was not at all clear why animals required such complex control. Further, in both standard textbooks and some research publications, there has been some controversy as to the directionality of the reaction. Here we review recent work demonstrating that GDH operates mainly in the catabolic direction in-vivo and that the finely tuned network of allosteric regulators allows GDH to meet the varied needs in a wide range of tissues in animals. Finally, we review the progress in using pharmacological agents to activate or inhibit GDH that could impact a wide range of pathologies from insulin disorders to tumor growth.

KEYWORDS:

Allostery; Glutamate dehydrogenase; Insulin

PMID:
29079932
PMCID:
PMC5924581
[Available on 2020-01-01]
DOI:
10.1007/s11064-017-2428-0
[Indexed for MEDLINE]

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