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

Hong Q. Smith, Changhong Li, Charles A. Stanley, Thomas Smith

Research output: Contribution to journalArticle

7 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1-16
Number of pages16
JournalNeurochemical Research
DOIs
StateAccepted/In press - Oct 27 2017

Keywords

  • Allostery
  • Glutamate dehydrogenase
  • Insulin

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Fingerprint Dive into the research topics of 'Glutamate Dehydrogenase, a Complex Enzyme at a Crucial Metabolic Branch Point'. Together they form a unique fingerprint.

  • Cite this