Chapter 17
Where to Start
Sugden, M. C., and Holness, M. J. 2003. Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs. Am. J. Physiol. Endocrinol. Metab. 284:E855–
Owen, O. E., Kalhan, S. C., and Hanson, R. W. 2002. The key role of anaplerosis and cataplerosis for citric acid function. J. Biol. Chem. 277:30409–
Patel, K. P., O’Brien, T. W., Subramony, S. H., Shuster, J., and Stacpoole, P. W. 2012. The spectrum of pyruvate dehydrogenase complex deficiency: Clinical, biochemical and genetic features in 371 patients. Mol. Genet. Metab. 105:34–
Vijayakrishnan, S., Callow, P., Nutley, M. A., Mcgow, D. P., Gilbert, D., Kropholler, P., Cooper, A., Byron, O., and Lindsay, J. G. 2011. Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly. Biochem. J. 437:565–
Vijayakrishnan, S., Kelly, S. M., Gilbert, R. J., Callow, P., Bhella, D., Forsyth, T., Lindsay, J. G., and Byron, O. 2010. Solution structure and characterization of the human pyruvate dehydrogenase complex core assembly. J. Mol. Biol. 399:71–
Brautigam, C. A., Wynn, R. M., Chuang, J. L., and Chuang, D. T. 2009. Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex. J. Biol. Chem. 284:13086–
Hiromasa, Y., Fujisawa, T., Aso, Y., and Roche, T. E. 2004. Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-
Domingo, G. J., Chauhan, H. J., Lessard, I. A., Fuller, C., and Perham, R. N. 1999. Self-
B18
Fraser, M. E., Hayakawa, K., Hume, M. S., Ryan, D. G., and Brownie, E. R. 2006. Interactions of GTP with the ATP-
Yankovskaya, V., Horsefield, R., Törnroth, S., Luna-
Fraser, M. E., James, M. N., Bridger, W. A., and Wolodko, W. T. 1999. A detailed structural description of Escherichia coli succinyl-
Lloyd, S. J., Lauble, H., Prasad, G. S., and Stout, C. D. 1999. The mechanism of aconitase: 1.8 Å resolution crystal structure of the S642A:citrate complex. Protein Sci. 8:2655–
Rose, I. A. 1998. How fumarase recycles after the malate → fumarate reaction: Insights into the reaction mechanism. Biochemistry 37:17651–
Lambeth, D. O., Tews, K. N., Adkins, S., Frohlich, D., and Milavetz, B. I. 2004. Expression of two succinyl-
Velot, C., Mixon, M. B., Teige, M., and Srere, P. A. 1997. Model of a quinary structure between Krebs TCA cycle enzymes: A model for the metabolon. Biochemistry 36:14271–
Haggie, P. M., and Brindle, K. M. 1999. Mitochondrial citrate synthase is immobilized in vivo. J. Biol. Chem. 274:3941–
Morgunov, I., and Srere, P. A. 1998. Interaction between citrate synthase and malate dehydrogenase: Substrate channeling of oxaloacetate. J. Biol. Chem. 273:29540–
Shi, Q., Xu, H., Yu, H., Zhang, N., Ye, Y., Estevez, A. G., Deng, H., and Gibson, G. E. 2011. Inactivation and reactivation of the mitochondrial α-ketoglutarate dehydrogenase complex. J. Biol. Chem. 286:17640–
Phillips, D., Aponte, A. M., French, S. A., Chess, D. J., and Balaban, R. S. 2009. Succinyl-
Taylor, A. B., Hu, G., Hart, P. J., and McAlister-
Green, T., Grigorian, A., Klyuyeva, A., Tuganova, A., Luo, M., and Popov, K. M. 2008. Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase. J. Biol. Chem. 283:15789–
Hiromasa, Y., and Roche, T. E. 2003. Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferases. J. Biol. Chem. 278:33681–
Jitrapakdee, S., and Wallace, J. C. 1999. Structure, function and regulation of pyruvate carboxylase. Biochem. J. 340:1–
Wang, F., Travins, J., DeLaBarre, B., Penard-
Rohle, D., Popovici-
Losman, J.-A., Koivunen, P., Lee, S., Schneider, R. K., McMahon, C., Cowley, G. S., Root, D. E., Ebert, B. L., Kaelin, W. G. Jr., et al. 2013. (R)-2-
Sakai, C., Tomitsuka, T., Esumi, H., Harada, S., and Kita, K. 2012. Mitochondrial fumarate reductase as a target of chemotherapy: From parasites to cancer cells. Biochim. Biophys. Acta 1820:643–
Xekouki P., and Stratakis, C. A. 2012. Succinate dehydrogenase (SDHx) mutations in pituitary tumors: Could this be a new role for mitochondrial complex II and/or Krebs cycle defects? Endocr.-Relat. Cancer 19:C33–
Thompson, C. B. 2009. Metabolic enzymes as oncogenes or tumor suppressors. New Engl. J. Med. 360:813–
McFate, T., Mohyeldin, A., Lu, H., Thakar, J., Henriques, J., Halim, N. D., Wu, H., Schell, M. J., Tsang, T. M., Teahan, O., Zhou, S., Califano, J. A., Jeoung, M. N., Harris, R. A., and Verma, A. 2008. Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells. J. Biol. Chem. 283:22700–
Gogvadze, V., Orrenius, S., and Zhivotovsky, B. 2008. Mitochondria in cancer cells: What is so special about them? Trends Cell Biol. 18:165–
Meléndez-
Baldwin, J. E., and Krebs, H. 1981. The evolution of metabolic cycles. Nature 291:381–
Gest, H. 1987. Evolutionary roots of the citric acid cycle in prokaryotes. Biochem. Soc. Symp. 54:3–
Weitzman, P. D. J. 1981. Unity and diversity in some bacterial citric acid cycle enzymes. Adv. Microbiol. Physiol. 22:185–
Kornberg, H. 2000. Krebs and his trinity of cycles. Nat. Rev. Mol. Cell. Biol. 1:225–
Krebs, H. A., and Johnson, W. A. 1937. The role of citric acid in intermediate metabolism in animal tissues. Enzymologia 4:148–
Krebs, H. A. 1970. The history of the tricarboxylic acid cycle. Perspect. Biol. Med. 14:154–
Krebs, H. A., and Martin, A. 1981. Reminiscences and Reflections. Clarendon Press.