Talk:Uncompetitive inhibition

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): Someoneskid, Asamulak. Peer reviewers: Asamulak.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 11:57, 17 January 2022 (UTC)

Wiki Education Foundation-supported course assignment
This article was the subject of a Wiki Education Foundation-supported course assignment, between 16 January 2019 and 22 March 2019. Further details are available on the course page. Student editor(s): Sazfar21.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 11:57, 17 January 2022 (UTC)

Formula derivations
Is someone willing to take a stab at making a derivation for non-competitive and uncompetitive inhibitions formulas? Competitive inhibition has an excellent derivation. It would be really helpful if these other types of inhibition also showed how the formula is derived. —Preceding unsigned comment added by 71.217.103.197 (talk) 03:43, 8 April 2011 (UTC)

Changes and Developing the Article
I plan to add a brief section to the general mechanism section explaining why Km decreases, since it is not currently very well explained and it's not particularly intuitive.

In the next few weeks, I am hoping to add a section regarding the significance of this form of inhibition on biological and biochemical systems and why this type of inhibition is uniquely important within systems. I've gathered a number of examples to thoroughly explain why the properties of uncompetitive inhibition are important within living systems and would appreciate any advice. Additionally, the mechanism section does not really explain restoration, which is a property discusses in some sources I saw; I am still unsure about whether that should be added under general mechanisms or relegated to just a biochemical significance section. Again, any advice would be greatly appreciated.

Here's my current list of sources, if anyone has advice: Ahern, Kevin (2017). Biochemistry Free For All Version 1.2. North Carolina: Creative Commons. pp. 367–368. Nahorski, S. R.; Ragan, C. I.; Challiss, R. A. (1991-8). "Lithium and the phosphoinositide cycle: an example of uncompetitive inhibition and its pharmacological consequences". Trends in Pharmacological Sciences. 12 (8): 297–303. ISSN 0165-6147. PMID 1658998. Check date values in: |date= (help) Lenaz, G.; Curatola, G.; Mazzanti, L.; Parenti-Castelli, G. (1978-11-30). "Biophysical studies on agents affecting the state of membrane lipids: biochemical and pharmacological implications". Molecular and Cellular Biochemistry. 22 (1): 3–32. ISSN 0300-8177. PMID 154058. Millán, J. L.; Fishman, W. H. (1995). "Biology of human alkaline phosphatases with special reference to cancer". Critical Reviews in Clinical Laboratory Sciences. 32 (1): 1–39. doi:10.3109/10408369509084680. ISSN 1040-8363. PMID 7748466. Nyce, Jonathan W. (2018-11). "Detection of a novel, primate-specific 'kill switch' tumor suppression mechanism that may fundamentally control cancer risk in humans: an unexpected twist in the basic biology of TP53". Endocrine-Related Cancer. 25 (11): R497–R517. doi:10.1530/ERC-18-0241. ISSN 1479-6821. PMC 6106910. PMID 29941676. Check date values in: |date= (help)

Sazfar21 (talk) 07:16, 11 February 2019 (UTC)

Michalis-Menton graph removed
I removed the graph under "Mechanism". This graph shows something very different from the cited source (Athel C (2014). Principles of Enzyme Kinetics. Elsevier Science. ISBN 978-1483164670. OCLC 897021733.) In particular, the graph clearly shows higher enzymatic activity at low substrate concentration when the inhibitor is present, but that is simply not the case. A version of that graph does appear in the free online textbook (Ahern K, Rajagopal I, Tan T (2017). Biochemistry Free For All Version 1.2. North Carolina: Creative Commons. pp. 367–368), but this contradicts not only Athel it also contradicts plots in multiple other biochemistry texts: (1) Nelson & Cox (2017) Lehninger Principles of Biochemistry Seventh Edition, W. H. Freeman, 978-1464126116; (2) Miesfeld & McEvoy (2017) Biochemistry (First Edition),  W. W. Norton & Company, 978-0393614022; (3) Voet & Voet (2010) Biochemistry, 4th Edition, Wiley, 978-0470570951.

It appears the erroneous source (as based on descriptions in Nelson & Cox and Voet & Voet) is showing what would happen if there were still some enzymatic activity with the inhibitor present (partial inhibition), but that is not what is described and makes the plot misleading.

It is also unfortunate that the only Creative Commons source has this error as it makes it much more tempting to put that plot in despite its incongruity with other appropriate sources.

Xargque (talk) 19:47, 12 October 2020 (UTC)

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