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

Neurochemical Research
Hong Q SmithThomas J Smith

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.

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Citations

Oct 15, 2019·Protein Science : a Publication of the Protein Society·Omneya M NassarB Montgomery Pettitt
Oct 9, 2020·Signal Transduction and Targeted Therapy·Huai-Qiang JuRui-Hua Xu
Jan 22, 2021·The Journal of Biological Chemistry·Miles H BlackVincent S Tagliabracci
Feb 20, 2021·Bioscience, Biotechnology, and Biochemistry·Yanjie ZhaoHe Li
Mar 19, 2020·Trends in Endocrinology and Metabolism : TEM·Rebecca L PfeifferBryan W Jones
Apr 18, 2020·Trends in Cell Biology·Kiran Kurmi, Marcia C Haigis
Apr 15, 2021·Cancer Cell International·Yuhong GuoZhiping Zhang
Nov 20, 2020·Experimental Cell Research·Kristopher MontroseJuha Saarikangas
Aug 31, 2021·Frontiers in Bioengineering and Biotechnology·Giannina EspinaJenny M Blamey
Nov 9, 2021·Proteins·Barsa Kanchan Jyotshna GodsoraPrasenjit Bhaumik

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Methods Mentioned

BETA
deamination
transgenic

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