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Enzyme Research
Volume 2011, Article ID 939068, 13 pages
http://dx.doi.org/10.4061/2011/939068
Research Article

Asp295 Stabilizes the Active-Site Loop Structure of Pyruvate Dehydrogenase, Facilitating Phosphorylation of Ser292 by Pyruvate Dehydrogenase-Kinase

1Department of Biochemistry, University of Missouri, Columbia, MO 65211, USA
2Interdisciplinary Plant Group, University of Missouri, Columbia, MO 65211, USA
3Plant Genetics Research Unit, USDA, Agricultural Research Service, Columbia, MO 65211, USA

Received 23 September 2010; Accepted 5 November 2010

Academic Editor: Heung Chin Cheng

Copyright © 2011 Tripty A. Hirani et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Citations to this Article [2 citations]

The following is the list of published articles that have cited the current article.

  • Hailan Yu, Xiaoqiu Du, Fengxia Zhang, Fang Zhang, Yong Hu, Shichang Liu, Xiangning Jiang, Guodong Wang, and Dong Liu, “A mutation in the E2 subunit of the mitochondrial pyruvate dehydrogenase complex in Arabidopsis reduces plant organ size and enhances the accumulation of amino acids and intermediate products of the TCA Cycle,” Planta, vol. 236, no. 2, pp. 387–399, 2012. View at Publisher · View at Google Scholar
  • Nagib Ahsan, Kirby N. Swatek, Jingfen Zhang, Jan A. Miernyk, Dong Xu, and Jay J. Thelen, “"Scanning mutagenesis" of the amino acid sequences flanking phosphorylation site 1 of the mitochondrial pyruvate dehydrogenase complex,” Frontiers in Plant Science, vol. 3, 2012. View at Publisher · View at Google Scholar