Crystal structure of prephenate dehydrogenase from Aquifex aeolicus. Insights into the catalytic mechanism

The Journal of Biological Chemistry
Warren SunDinesh Christendat

Abstract

The enzyme prephenate dehydrogenase catalyzes the oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate for the biosynthesis of tyrosine. Prephenate dehydrogenases exist as either monofunctional or bifunctional enzymes. The bifunctional enzymes are diverse, since the prephenate dehydrogenase domain is associated with other enzymes, such as chorismate mutase and 3-phosphoskimate 1-carboxyvinyltransferase. We report the first crystal structure of a monofunctional prephenate dehydrogenase enzyme from the hyper-thermophile Aquifex aeolicus in complex with NAD+. This protein consists of two structural domains, a modified nucleotide-binding domain and a novel helical prephenate binding domain. The active site of prephenate dehydrogenase is formed at the domain interface and is shared between the subunits of the dimer. We infer from the structure that access to the active site is regulated via a gated mechanism, which is modulated by an ionic network involving a conserved arginine, Arg250. In addition, the crystal structure reveals for the first time the positions of a number of key catalytic residues and the identity of other active site residues that may participate in the reaction mechanism; these residues include Ser1...Continue Reading

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Citations

Sep 2, 2011·The Journal of Biological Chemistry·Leo Y-C LinNatalie C J Strynadka
Mar 13, 2009·The Journal of Biological Chemistry·Warren SunDinesh Christendat
Oct 15, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Hsiu Ju ChiuIan A Wilson
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Nov 18, 2014·Nature Chemical Biology·Craig A SchenckHiroshi A Maeda
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Jul 4, 2017·Nature Chemical Biology·Craig A SchenckHiroshi A Maeda
Feb 27, 2018·Phytochemistry·Craig A Schenck, Hiroshi A Maeda
Jul 30, 2011·International Journal of Biological Macromolecules·Hyung-Keun KuSoo Jae Lee

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