Where to Start

McCracken, A. N., and Edinger, A. L. 2013. Nutrient transporters: The Achilles’ heel of anabolism. Trends Endocrin. Met. 24:200–208.

Curry, A. 2013. The milk revolution. Nature 500:20–22.

Bar-Even, A., Flamholz, A., Noor, E., and Milo, R. 2012. Rethinking glycolysis: On the biochemical logic of metabolic pathways. Nature Chem. Biol. 8:509–517.

Ward, P. S., and Thompson, C. B. 2012. Metabolic reprogramming: A cancer hallmark even Warburg did not anticipate. Cancer Cell 21:297–308.

Herling, A., König, M., Bulik, S., and Holzhütter, H.-G. 2011. Enzymatic features of the glucose metabolism in tumor cells. FEBS J. 278:2436–2459.

Lin, H. V., and Accili, D. 2011. Hormonal regulation of hepatic glucose production in health and disease. Cell Metab. 14:9–19.

Hirabayashi, J. 1996. On the origin of elementary hexoses. Quart. Rev. Biol.71:365–380.

Tong, L. 2013. Structure and function of biotin-dependent carboxylases. Cell. Mol. Life Sci. 70:863–891.

Frayn, K. N. 2010. Metabolic Regulation: A Human Perspective (3d ed.). Wiley-Blackwell.

Fell, D. 1997. Understanding the Control of Metabolism. Portland.

Fersht, A. 1999. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding. W. H. Freeman and Company.

Poortmans, J. R. (Ed.). 2004. Principles of Exercise Biochemistry. Krager.

Lietzan, A. D., and St. Maurice, M. 2013. A substrate-induced biotin binding pocket in the carboxyltransferase domain of pyruvate carboxylase. J. Biol. Chem. 288:19915−19925.

Banaszak, L., Mechin, I., Obmolova, G., Oldham, M., Chang, S. H., Ruiz, T., Radermacher, M., Kopperschläger, G., and Rypniewski, W. 2011. The crystal structures of eukaryotic phosphofructokinases from baker’s yeast and rabbit skeletal muscle. J. Mol. Biol. 407:284–297.

Lasso, G., Yu, L. P. C., Gil, D., Xiang, S., Tong, L., and Valle, M. 2010. Cryo-EM analysis reveals new insights into the mechanism of action of pyruvate carboxylase. Structure 18:1300–1310.

Ferreras, C., Hernández, E. D., Martínez-Costa, O. H., and Aragón, J. J. 2009. Subunit interactions and composition of the fructose 6-phosphate catalytic site and the fructose 2,6-bisphosphate allosteric site of mammalian phosphofructokinase. J. Biol. Chem. 284:9124–9131.

Hines, J. K., Chen, X., Nix, J. C., Fromm, H. J., and Honzatko. R. B. 2007. Structures of mammalian and bacterial fructose-1, 6-bisphosphatase reveal the basis for synergism in AMP/fructose-2, 6-bisphosphate inhibition. J. Biol. Chem. 282:36121–36131.

Ferreira-da-Silva, F., Pereira, P. J., Gales, L., Roessle, M., Svergun, D. I., Moradas-Ferreira, P., and Damas, A. M. 2006. The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures. J. Biol. Chem. 281:33433–33440.

Kim, S.-G., Manes, N. P., El-Maghrabi, M. R., and Lee, Y.-H. 2006. Crystal structure of the hypoxia-inducible form of 6-phosphofructo-2-kinase/fructose-2,6-phosphatase (PFKFB3): A possible target for cancer therapy. J. Biol. Chem. 281:2939–2944.

Aleshin, A. E., Kirby, C., Liu, X., Bourenkov, G. P., Bartunik, H. D., Fromm, H. J., and Honzatko, R. B. 2000. Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. J. Mol. Biol. 296:1001–1015.

Jeffery, C. J., Bahnson, B. J., Chien, W., Ringe, D., and Petsko, G. A. 2000. Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator. Biochemistry 39:955–964.

Bernstein, B. E., and Hol, W. G. 1998. Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. Biochemistry 37:4429–4436.

Rigden, D. J., Alexeev, D., Phillips, S. E. V., and Fothergill-Gilmore, L. A. 1998. The 2.3 Å X-ray crystal structure of S. cerevisiae phosphoglycerate mutase. J. Mol. Biol. 276:449–459.

Zhang, E., Brewer, J. M., Minor, W., Carreira, L. A., and Lebioda, L. 1997. Mechanism of enolase: The crystal structure of asymmetric dimer enolase-2-phospho-d-glycerate/enolase-phosphoenolpyruvate at 2.0 Å resolution. Biochemistry 36:12526–12534.

Hasemann, C. A., Istvan E. S., Uyeda, K., and Deisenhofer, J. 1996. The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase reveals distinct domain homologies. Structure 4:1017–1029.

Tari, L. W., Matte, A., Pugazhenthi, U., Goldie, H., and Delbaere, L. T. J. 1996. Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg²⁺-oxalate ternary complex of Escherichia coli PEP carboxykinase. Nat. Struct. Biol. 3:355–363.

Soukri, A., Mougin, A., Corbier, C., Wonacott, A., Branlant, C., and Branlant, G. 1989. Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis. Biochemistry 28:2586–2592.

Bash, P. A., Field, M. J., Davenport, R. C., Petsko, G. A., Ringe, D., and Karplus, M. 1991. Computer simulation and analysis of the reaction pathway of triosephosphate isomerase. Biochemistry 30:5826–5832.

Knowles, J. R., and Albery, W. J. 1977. Perfection in enzyme catalysis: The energetics of triosephosphate isomerase. Acc. Chem. Res. 10: 105–111.

Liu, S., Ammirati, M. J., Song, X., Knafels, J. D., Zhang, J., Greasley, S. E., Pfefferkorn, J. A., and Qiu, X. 2012. Insights into mechanism of glucokinase activation: Observation of multiple distinct protein conformations. J. Biol. Chem. 287:13598–13610.

Brüser, A., Kirchberger, J., Kloos, M., Sträter, N., and Schöneberg, T. 2012. Functional linkage of adenine nucleotide binding sites in mammalian muscle 6-phosphofructokinase. J. Biol. Chem. 287: 17546–17553.

B17

Anderka, O., Boyken, J., Aschenbach, U., Batzer, A., Boscheinen, O., and Schmoll, D. 2008. Biophysical characterization of the interaction between hepatic glucokinase and its regulatory protein: Impact of physiological and pharmacological effectors. J. Biol. Chem. 283:31333–31340.

Iancu, C. V., Mukund, S., Fromm, H. J., and Honzatko, R. B. 2005. R-state AMP complex reveals initial steps of the quaternary transition of fructose-l,6-bisphosphatase. J. Biol. Chem. 280: 19737–19745.

Lee, Y. H., Li, Y., Uyeda, K., and Hasemann, C. A. 2003. Tissue-specific structure/function differentiation of the five isoforms of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. J. Biol. Chem. 278:523–530.

Gleeson, T. T. 1996. Post-exercise lactate metabolism: A comparative review of sites, pathways, and regulation. Annu. Rev. Physiol. 58:556–581.

Jitrapakdee, S., and Wallace, J. C. 1999. Structure, function and regulation of pyruvate carboxylase. Biochem. J. 340:1–16.

van de Werve, G., Lange, A., Newgard, C., Mechin, M. C., Li, Y., and Berteloot, A. 2000. New lessons in the regulation of glucose metabolism taught by the glucose 6-phosphatase system. Eur. J. Biochem. 267:1533–1549.

Blodgett, D. M., Graybill, C. and Carruthers, A. 2008. Analysis of glucose transporter topology and structural dynamics. J. Biol. Chem. 283:36416–36424.

Huang, S., and Czech, M. P. 2007. The GLUT4 glucose transporter. Cell Metab. 5:237–252.

Czech, M. P., and Corvera, S. 1999. Signaling mechanisms that regulate glucose transport. J Biol. Chem. 274:1865–1868.

Silverman, M. 1991. Structure and function of hexose transporters. Annu. Rev. Biochem. 60:757–794.

Thorens, B., Charron, M. J., and Lodish, H. F. 1990. Molecular physiology of glucose transporters. Diabetes Care 13:209–218.

Morgan, H. P., O’Reilly, F. J., Wear, M. A., O’Neill, J. R., Fothergill-Gilmore, L. A., Hupp, T., and Walkinshaw, M. D. 2013. M2 pyruvate kinase provides a mechanism for nutrient sensing and regulation of cell proliferation. Proc. Natl. Acad. Sci. U.S.A. 110: 5881–5886.

Schulze, A., and Harris, A. L. 2012. How cancer metabolism is tuned for proliferation and vulnerable to disruption. Nature 491:364–373.

Lunt, S. Y., and Vander Heiden, M. G. 2011. Aerobic glycolysis: Meeting the metabolic requirements of cell proliferation. Annu. Rev. Cell Dev. Biol. 27:441–64.

Vander Heiden, M. G., Cantley, L. C., and Thompson, C. B. 2009. Understanding the Warburg effect: The metabolic requirements of cell proliferation. Science 324:1029–1033.

Mathupala, S. P., Ko, Y. H., and Pedersen, P. L. 2009. Hexokinase-2 bound to mitochondria: Cancer’s stygian link to the “Warburg effect” and a pivotal target for effective therapy. Sem. Cancer Biol. 19:17–24.

Kroemer, G. K., and Pouyssegur, J. 2008. Tumor cell metabolism: Cancer’s Achilles’ heel. Cancer Cell 12:472–482.

Hsu, P. P., and Sabatini, D. M. 2008. Cancer cell metabolism: Warburg and beyond. Cell 134:703–707.

Orosz, F., Oláh, J., and Ovádi, J. 2009. Triosephosphate isomerase deficiency: New insights into an enigmatic disease. Biochim. Biophys. Acta 1792:1168–1174.

Scriver, C. R., Beaudet, A. L., Valle, D., Sly, W. S., Childs, B., Kinzler, K., and Vogelstein, B. (Eds.). 2001. The Metabolic and Molecular Basis of Inherited Disease (8th ed.). McGraw-Hill.

Dandekar, T., Schuster, S., Snel, B., Huynen, M., and Bork, P. 1999. Pathway alignment: Application to the comparative analysis of glycolytic enzymes. Biochem. J. 343:115–124.

Heinrich, R., Melendez-Hevia, E., Montero, F., Nuno, J. C., Stephani, A., and Waddell, T. G. 1999. The structural design of glycolysis: An evolutionary approach. Biochem. Soc. Trans. 27:294–298.

Walmsley, A. R., Barrett, M. P., Bringaud, F., and Gould, G. W. 1998. Sugar transporters from bacteria, parasites and mammals: Structure-activity relationships. Trends Biochem. Sci. 23: 476–480.

Maes, D., Zeelen, J. P., Thanki, N., Beaucamp, N., Alvarez, M., Thi, M. H., Backmann, J., Martial, J. A., Wyns, L., Jaenicke, R., et al. 1999. The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures. Proteins 37:441–453.

Friedmann, H. C. 2004. From Butyribacterium to E. coli: An essay on unity in biochemistry. Perspect. Biol. Med. 47:47–66.

Fruton, J. S. 1999. Proteins, Enzymes, Genes: The Interplay of Chemistry and Biology. Yale University Press.

Kalckar, H. M. (Ed.). 1969. Biological Phosphorylations: Development of Concepts. Prentice Hall.