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Talk:Pyruvate kinase

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Wiki Education Foundation-supported course assignment

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Latest comment: 2 years ago1 comment1 person in discussion

  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

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Latest comment: 18 years ago1 comment1 person in discussion

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

wild type condition

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Latest comment: 14 years ago1 comment1 person in discussion

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

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Latest comment: 13 years ago1 comment1 person in discussion

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

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Latest comment: 13 years ago1 comment1 person in discussion

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

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Latest comment: 8 years ago1 comment1 person in discussion

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

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Latest comment: 5 years ago1 comment1 person in discussion

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

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Latest comment: 3 years ago1 comment1 person in discussion

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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