Talk:Pyruvate kinase

Wiki Education Foundation-supported course assignment
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)

Template Testing
I want to test a template... --Dan|(talk) 15:10, 3 June 2006 (UTC)

wild type condition
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)

Cofactors of pyruvate kinase
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)

Missing link of addition of hydrogen from PEP to Pyruvate
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)

Outline for New Edits
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. Reaction: Leave mostly as it is, not much more information here Reverse Reaction: Gluconeogenesis: Add in a bit more detail as well Hormonal Control Effect of Metaformin Regulation in Yeast Properties and Characteristics: PKLR Gene: Mutations Isozymes in Vertebrates: In Cats In Pigs In Rat: Liver, Two types found Regulation: Already pretty thorough, fix it up a little bit and add some more detail In rat liver Carbohydrate response element binding protein Inhibition: Inhibit by Oxygen Reactive Species (ROS) Inhibit by Phenylalanine and Phenylpyruvate Feedforward and Feedback Inhibition in Liver Clinical Applications: (make sure to use review articles, not primary sources) Metabolism and Cancer Research: In e. Coli M2 Splice isoform Redox Metabolism in Respiring Cells Parasitic Disease: Deficiency: Review of the last decade Mutations Progress of Molecular Genetics Methicillin-resistant Staphylococcus aureus: Assay: Briefly Mention and Discuss — Preceding unsigned comment added by Jlivschitz12 (talk • contribs) 11:54, 5 May 2016 (UTC)

Adding cancer related content to this page
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)

PK is not Rate-Limiting in Mammalian Cells
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)