Untangling the glutamate dehydrogenase allosteric nightmare

Thomas Smith, Charles A. Stanley

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

Glutamate dehydrogenase (GDH) is found in all living organisms, but only animal GDH is regulated by a large repertoire of metabolites. More than 50 years of research to better understand the mechanism and role of this allosteric network has been frustrated by its sheer complexity. However, recent studies have begun to tease out how and why this complex behavior evolved. Much of GDH regulation probably occurs by controlling a complex ballet of motion necessary for catalytic turnover and has evolved concomitantly with a long antenna-like feature of the structure of the enzyme. Ciliates, the 'missing link' in GDH evolution, might have created the antenna to accommodate changing organelle functions and was refined in humans to, at least in part, link amino acid catabolism with insulin secretion.

Original languageEnglish (US)
Pages (from-to)557-564
Number of pages8
JournalTrends in Biochemical Sciences
Volume33
Issue number11
DOIs
StatePublished - Nov 2008
Externally publishedYes

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Glutamate Dehydrogenase
Dancing
Antennas
Metabolites
Organelles
Animals
Insulin
Amino Acids
Enzymes
Research

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Untangling the glutamate dehydrogenase allosteric nightmare. / Smith, Thomas; Stanley, Charles A.

In: Trends in Biochemical Sciences, Vol. 33, No. 11, 11.2008, p. 557-564.

Research output: Contribution to journalArticle

Smith, Thomas ; Stanley, Charles A. / Untangling the glutamate dehydrogenase allosteric nightmare. In: Trends in Biochemical Sciences. 2008 ; Vol. 33, No. 11. pp. 557-564.
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