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Trends Biochem Sci. 2008 Nov;33(11):557-64. doi: 10.1016/j.tibs.2008.07.007. Epub 2008 Sep 24.

Untangling the glutamate dehydrogenase allosteric nightmare.

Author information

1
Donald Danforth Plant Science Center, Saint Louis, MO 63132, USA. tsmith@danforthcenter.org

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.

PMID:
18819805
DOI:
10.1016/j.tibs.2008.07.007
[Indexed for MEDLINE]

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