Wikipedia

Jlivschitz12

Joined 7 April 2016

Topic Outline:

Introduction:

  • Expand on this section, not enough written
  • Include more about its structure: tetrameter, 4 metal binding sites, etc[1][2]

Reaction:

  • Leave mostly as it is, not much more information here
  • Reverse Reaction
    • Gluconeogenesis:
      • Add in a bit more detail as well[3]
      • Hormonal Control[4]
      • Effect of Metaformin[5]

Properties and Characteristics

  • Isozymes in Vertebrates[6]
    • In Cats[7]
    • In Pigs[8]
    • In Rat
      • Liver: Two types found[9]

Regulation:

  • Already pretty thorough, fix it up a little bit and add some more detail[10]
  • In rat liver[11][12]
  • Carbohydrate response element binding protein[13]

Inhibition:

  • Inhibit by Oxygen Reactive Species (ROS)[14]
  • Inhibit by Phenylalanine and Phenylpyruvate[15]
  • Feedforward and Feedback Inhibition in Liver[16]

Clinical Applications: (make sure to use review articles, not primary sources)

  • Metabolism and Cancer Research
    • In e. Coli[17]
    • M2 Splice isoform [18][19]
    • Redox Metabolism in Respiring Cells[20]
  • Parasitic Disease[21]
  • Deficiency
    • Review of the last decade[22]
    • Mutations[23]
    • Progress of Molecular Genetics[24]
  • Methicillin-resistant Staphylococcus aureus[25]

Assay:

  • Briefly Mention and Discuss[26]

My topic:

  1. Pyruvate kinase[27][28][29][30][31][32][33][34][35][36] Extra information

Reference List:

edit
  1. ^ Gupta, Vibhor; Bamezai, Rameshwar N.K. (2010-11-01). "Human pyruvate kinase M2: A multifunctional protein". Protein Science. 19 (11): 2031–2044. doi:10.1002/pro.505. ISSN 1469-896X. PMC 3005776. PMID 20857498.
  2. ^ "Pyruvate Kinase - Worthington Enzyme Manual". www.worthington-biochem.com. Retrieved 2016-05-05.
  3. ^ Rognstad, R.; Katz, J. (1977-03-25). "Role of pyruvate kinase in the regulation of gluconeogenesis from L-lactate". Journal of Biological Chemistry. 252 (6): 1831–1833. ISSN 0021-9258. PMID 845145.
  4. ^ Feliú, J. E.; Hue, L.; Hers, H. G. (1976-08-01). "Hormonal control of pyruvate kinase activity and of gluconeogenesis in isolated hepatocytes". Proceedings of the National Academy of Sciences. 73 (8): 2762–2766. ISSN 0027-8424. PMC 430732. PMID 183209.
  5. ^ Argaud, Doriane; Roth, Hubert; Wiernsperger, Nicolas; Leverve, Xavier M. (1993-05-01). "Metformin decreases gluconeogenesis by enhancing the pyruvate kinase flux in isolated rat hepatocytes". European Journal of Biochemistry. 213 (3): 1341–1348. doi:10.1111/j.1432-1033.1993.tb17886.x. ISSN 1432-1033.
  6. ^ Hall, Elizabeth R.; Larry Cottam, G. (1978-01-01). "Isozymes of pyruvate kinase in vertebrates: their physical, chemical, kinetic and immunological properties". International Journal of Biochemistry. 9 (11): 785–794. doi:10.1016/0020-711X(78)90027-7.
  7. ^ Stuart, David I.; Levine, Michael; Muirhead, Hilary; Stammers, David K. (1979-10-15). "Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å". Journal of Molecular Biology. 134 (1): 109–142. doi:10.1016/0022-2836(79)90416-9.
  8. ^ Berglund, L.; Ljungström, O.; Engström, L. (1977-09-10). "Purification and characterization of pig kidney pyruvate kinase (type A)". Journal of Biological Chemistry. 252 (17): 6108–6111. ISSN 0021-9258. PMID 893398.
  9. ^ Tanaka, Takehiko; Harano, Yutaka; Morimura, Hiroko; Mori, Ryosuke (1965-10-08). "Evidence for the presence of two types of pyruvate kinase in rat liver". Biochemical and Biophysical Research Communications. 21 (1): 55–60. doi:10.1016/0006-291X(65)90425-0.
  10. ^ "Regulation of Glycolysis:". cmgm.stanford.edu. Retrieved 2016-05-05.
  11. ^ Titanji, Vincent P. K.; Zetterqvist, Örjan; Engström, Lorentz (1976-01-23). "Regulation in vitro of rat liver pyruvate kinase by phosphorylation-dephosphorylation reactions, catalyzed by cyclic-AMP dependent protein kinases and a histone phosphatase". Biochimica et Biophysica Acta (BBA) - Enzymology. 422 (1): 98–108. doi:10.1016/0005-2744(76)90011-5.
  12. ^ Blair, J. B.; Cimbala, M. A.; Foster, J. L.; Morgan, R. A. (1976-06-25). "Hepatic pyruvate kinase. Regulation by glucagon, cyclic adenosine 3'-5'-monophosphate, and insulin in the perfused rat liver". Journal of Biological Chemistry. 251 (12): 3756–3762. ISSN 0021-9258. PMID 180008.
  13. ^ Kawaguchi, Takumi; Takenoshita, Makoto; Kabashima, Tsutomu; Uyeda, Kosaku (2001-11-20). "Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein". Proceedings of the National Academy of Sciences. 98 (24): 13710–13715. doi:10.1073/pnas.231370798. ISSN 0027-8424. PMC 61106. PMID 11698644.
  14. ^ Anastasiou, Dimitrios; Poulogiannis, George; Asara, John M.; Boxer, Matthew B.; Jiang, Jian-kang; Shen, Min; Bellinger, Gary; Sasaki, Atsuo T.; Locasale, Jason W. (2011-12-02). "Inhibition of Pyruvate Kinase M2 by Reactive Oxygen Species Contributes to Cellular Antioxidant Responses". Science. 334 (6060): 1278–1283. doi:10.1126/science.1211485. ISSN 0036-8075. PMC 3471535. PMID 22052977.
  15. ^ Weber, George (1969-08-01). "Inhibition of Human Brain Pyruvate Kinase and Hexokinase by Phenylalanine and Phenylpyruvate: Possible Relevance to Phenylketonuric Brain Damage". Proceedings of the National Academy of Sciences. 63 (4): 1365–1369. ISSN 0027-8424. PMC 223473. PMID 5260939.
  16. ^ Tanaka, Takehiko; Sue, Fumiaki; Morimura, Hiroko (1967-11-17). "Feed-forward activation and feed-back inhibition of pyruvate kinase type L of rat liver". Biochemical and Biophysical Research Communications. 29 (3): 444–449. doi:10.1016/0006-291X(67)90477-9.
  17. ^ Emmerling, Marcel; Dauner, Michael; Ponti, Aaron; Fiaux, Jocelyne; Hochuli, Michel; Szyperski, Thomas; Wüthrich, Kurt; Bailey, J. E.; Sauer, Uwe (2002-01-01). "Metabolic Flux Responses to Pyruvate Kinase Knockout in Escherichia coli". Journal of Bacteriology. 184 (1): 152–164. doi:10.1128/JB.184.1.152-164.2002. ISSN 0021-9193. PMC 134756. PMID 11741855.
  18. ^ Christofk, Heather R.; Heiden, Matthew G. Vander; Harris, Marian H.; Ramanathan, Arvind; Gerszten, Robert E.; Wei, Ru; Fleming, Mark D.; Schreiber, Stuart L.; Cantley, Lewis C. "The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth". Nature. 452 (7184): 230–233. doi:10.1038/nature06734.
  19. ^ Christofk, Heather R.; Heiden, Matthew G. Vander; Wu, Ning; Asara, John M.; Cantley, Lewis C. "Pyruvate kinase M2 is a phosphotyrosine-binding protein". Nature. 452 (7184): 181–186. doi:10.1038/nature06667.
  20. ^ Grüning, Nana-Maria; Rinnerthaler, Mark; Bluemlein, Katharina; Mülleder, Michael; Wamelink, Mirjam M. C.; Lehrach, Hans; Jakobs, Cornelis; Breitenbach, Michael; Ralser, Markus (2011-09-07). "Pyruvate Kinase Triggers a Metabolic Feedback Loop that Controls Redox Metabolism in Respiring Cells". Cell Metabolism. 14 (3): 415–427. doi:10.1016/j.cmet.2011.06.017. ISSN 1550-4131. PMC 3202625. PMID 21907146 21907146, 21907146. {{cite journal}}: Check |pmid= value (help)
  21. ^ University of Edinburgh. "Enzyme discovery paves way to tackling deadly parasite diseases." ScienceDaily. ScienceDaily, 24 September 2014. <www.sciencedaily.com/releases/2014/09/140924113655.htm>.
  22. ^ Grace, Rachael F.; Zanella, Alberto; Neufeld, Ellis J.; Morton, D. Holmes; Eber, Stefan; Yaish, Hassan; Glader, Bertil (2015-09-01). "Erythrocyte pyruvate kinase deficiency: 2015 status report". American Journal of Hematology. 90 (9): 825–830. doi:10.1002/ajh.24088. ISSN 1096-8652. PMID 26087744.
  23. ^ Climent, Fernando; Roset, Feliu; Repiso, Ada; Pérez de la Ossa, Pablo (2009-06-01). "Red cell glycolytic enzyme disorders caused by mutations: an update". Cardiovascular & Hematological Disorders Drug Targets. 9 (2): 95–106. ISSN 2212-4063. PMID 19519368.
  24. ^ Miwa, Shiro; Kanno, Hitoshi; Fujii, Hisaichi (1993-01-01). "Pyruvate kinase deficiency: Historical perspective and recent progress of molecular genetics". American Journal of Hematology. 42 (1): 31–35. doi:10.1002/ajh.2830420108. ISSN 1096-8652.
  25. ^ Kumar, Nag S.; Dullaghan, Edie M.; Finlay, B. Brett; Gong, Huansheng; Reiner, Neil E.; Jon Paul Selvam, J.; Thorson, Lisa M.; Campbell, Sara; Vitko, Nicholas (2014-03-01). "Discovery and optimization of a new class of pyruvate kinase inhibitors as potential therapeutics for the treatment of methicillin-resistant Staphylococcus aureus infections". Bioorganic & Medicinal Chemistry. 22 (5): 1708–1725. doi:10.1016/j.bmc.2014.01.020.
  26. ^ "Pyruvate Kinase - Assay". www.worthington-biochem.com. Retrieved 2016-05-05.
  27. ^ Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert; Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert (2002-01-01). Biochemistry (5th ed.). W H Freeman. ISBN 0716730510.
  28. ^ Voet, Donald, Charlotte W. Pratt, and Judith G. Voet. Fundamentals of Biochemistry: Life at the Molecular Level. Hoboken, NJ: John Wiley & Sons, 2012.
  29. ^ Nelson, David L., Michael M. Cox, and Albert L. Lehninger. Lehninger Principles of Biochemistry. New York: W.H. Freeman, 2013.
  30. ^ Grace, Rachael F.; Zanella, Alberto; Neufeld, Ellis J.; Morton, D. Holmes; Eber, Stefan; Yaish, Hassan; Glader, Bertil (2015-09-01). "Erythrocyte pyruvate kinase deficiency: 2015 status report". American Journal of Hematology. 90 (9): 825–830. doi:10.1002/ajh.24088. ISSN 1096-8652. PMID 26087744.
  31. ^ Gopinath, Prakasam; Singh, Rajnish Kumar; Iqbal, Mohammad Askandar; Tiku, Ashu Bhan; Bamezai, Rameshwar N. K. (2016-04-26). "Regulation of Pyruvate Kinase M Switch towards PKM1 by LKB1-AMPK Axis Tolerates Hypoglycemic Stress in Cancer Cells". The Journal of Biological Chemistry. doi:10.1074/jbc.M116.729079. ISSN 1083-351X. PMID 27129277.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  32. ^ Blair, J. B.; Cimbala, M. A.; Foster, J. L.; Morgan, R. A. (1976-06-25). "Hepatic pyruvate kinase. Regulation by glucagon, cyclic adenosine 3'-5'-monophosphate, and insulin in the perfused rat liver". Journal of Biological Chemistry. 251 (12): 3756–3762. ISSN 0021-9258. PMID 180008.
  33. ^ Christofk, Heather R.; Vander Heiden, Matthew G.; Wu, Ning; Asara, John M.; Cantley, Lewis C. (2008-03-13). "Pyruvate kinase M2 is a phosphotyrosine-binding protein". Nature. 452 (7184): 181–186. doi:10.1038/nature06667. ISSN 0028-0836.
  34. ^ Kawaguchi, Takumi; Takenoshita, Makoto; Kabashima, Tsutomu; Uyeda, Kosaku (2001-11-20). "Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein". Proceedings of the National Academy of Sciences. 98 (24): 13710–13715. doi:10.1073/pnas.231370798. ISSN 0027-8424. PMC 61106. PMID 11698644.
  35. ^ Jurica, Melissa S; Mesecar, Andrew; Heath, Patrick J; Shi, Wuxian; Nowak, Thomas; Stoddard, Barry L (1998-02-15). "The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate". Structure. 6 (2): 195–210. doi:10.1016/S0969-2126(98)00021-5.
  36. ^ "Regulation of Glycolysis:". cmgm.stanford.edu. Retrieved 2016-05-01.
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