Talk:Pyruvate kinase

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Wiki Education Foundation-supported course assignment[edit]

This article is or was the subject of a Wiki Education Foundation-supported course assignment. Further details are available on the course page. Student editor(s): Jlivschitz12.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 07:32, 17 January 2022 (UTC)[reply]

Template Testing[edit]

I want to test a template... PDB: 1a49​ --Dan|(talk) 15:10, 3 June 2006 (UTC)[reply]

wild type condition[edit]

Wild type is refrecne to the genes that produce the enzyme so when you say wild type you mean in a health indivdual. i dont belive this to be correct and if it is , it should be ellbarated on alittle —Preceding unsigned comment added by 131.227.105.67 (talk) 10:26, 28 May 2010 (UTC)[reply]

Cofactors of pyruvate kinase[edit]

Can someone reference the statement that pyruvate kinase requires manganese ion (Mn)? As in Voet Biochemistry text book 3rd edition on pp584, it says Mg2+ and K+. Otivaeey (talk) 19:14, 13 February 2011 (UTC) —Preceding unsigned comment added by 129.31.204.25 (talk) 19:04, 13 February 2011 (UTC)[reply]

Missing link of addition of hydrogen from PEP to Pyruvate[edit]

Can someone add on about where the extra H in pyruvate comes from? It doesn't seem like from water. I think this is always a vague point in this particular reaction analysis of glycolysis pathway. — Preceding unsigned comment added by Otivaeey (talk • contribs) 19:09, 13 February 2011 (UTC)[reply]

Outline for New Edits[edit]

Hi! I am taking a biochemistry class at UCLA and I have picked this page to update. I have created the following outline for the direction I plan to take on this page. Please let me know if you have any advice, comments, suggestions, etc.

 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]
Regulation in Yeast [6]

Properties and Characteristics: 

PKLR Gene:
Mutations [7]
Isozymes in Vertebrates:[8]
In Cats [9]
In Pigs [10]
In Rat:
Liver, Two types found [11]

Regulation: 

Already pretty thorough, fix it up a little bit and add some more detail [12]
In rat liver [13] [14]
Carbohydrate response element binding protein [15]

Inhibition: 

Inhibit by Oxygen Reactive Species (ROS)[16]
Inhibit by Phenylalanine and Phenylpyruvate [17]
Feedforward and Feedback Inhibition in Liver [18]

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

Metabolism and Cancer Research: 
In e. Coli [19]
M2 Splice isoform [20] [21]
Redox Metabolism in Respiring Cells [22]
Parasitic Disease:[23]
Deficiency:
Review of the last decade [24]
Mutations [25]
Progress of Molecular Genetics [26]
Methicillin-resistant Staphylococcus aureus: [27]

Assay: 

Briefly Mention and Discuss [28]  — Preceding unsigned comment added by Jlivschitz12 (talk • contribs) 11:54, 5 May 2016 (UTC)[reply]

References

  1. ^ Gupta, V. and Bamezai, R. N.K. (2010), Human pyruvate kinase M2: A multifunctional protein. Protein Science, 19: 2031–2044. doi:10.1002/pro.505
  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. ^ Gancedo, J M; Gancedo, C; Sols, A (1967-02-01). "Regulation of the concentration or activity of pyruvate kinase in yeasts and its relationship to gluconeogenesis.". Biochemical Journal 102 (2): 23C–25C. ISSN 0264-6021. PMC 1270297. PMID 6029596.
  7. ^ Canu, Giulia; De Bonis, Maria; Minucci, Angelo; Capoluongo, Ettore (2016-03-01). "Red blood cell PK deficiency: An update of PK-LR gene mutation database". Blood Cells, Molecules, and Diseases 57: 100–109. doi:10.1016/j.bcmd.2015.12.009
  8. ^ 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
  9. ^ 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.
  10. ^ 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.
  11. ^ 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
  12. ^ "Regulation of Glycolysis:". cmgm.stanford.edu. Retrieved 2016-05-05.
  13. ^ 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
  14. ^ 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.
  15. ^ 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.
  16. ^ 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.
  17. ^ 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
  18. ^ 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.
  19. ^ 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
  20. ^ 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
  21. ^ 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.
  22. ^ 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
  23. ^ 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>
  24. ^ 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
  25. ^ 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.
  26. ^ 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.
  27. ^ 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.
  28. ^ "Pyruvate Kinase - Assay". www.worthington-biochem.com. Retrieved 2016-05-05.

Adding cancer related content to this page[edit]

Hi! I am taking a biochemistry course at UCLA and wish to add discussions about how pyruvate cancer is involved in cancer. Does anyone have any thoughts or suggestions? Thanks Tkadali (talk) 05:24, 13 February 2019 (UTC)[reply]

PK is not Rate-Limiting in Mammalian Cells[edit]

The section on Glycolysis/Regulation states that Pyruvate Kinase is rate-limiting. I don't think it is, at least not in mammalian cells, see the paper "Tanner et al, Four Key Steps Control Glycolytic Flux in Mammalian Cells, 2018, Cell Systems". Table 1 in the paper shows that PK (PKM1) has a flux control coefficient of less than 0.1, not exactly limiting. PKM2 is not limiting at all. I've not looked at yeast data or other organisms where PK might well have a higher flux control coefficient. This should be clarified in the text especially given the number of students that are likely to read this page. Rhodydog (talk) 18:20, 28 January 2021 (UTC)[reply]

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