Talk:Enzyme kinetics

message: Not really sure this is the right page for this but I wonder if we need a passage discussing the biological significance of Km. I think this would help people relate more to these numbers. For example, physiological substrate concentrations are often quite close to the  Km. Different isozymes can have different  Km values, depending on the location in a cell or tissue. This type of thing.  What do you think? David D. (Talk) 22:04, 26 September 2006 (UTC)
thread_title: biological significance

message: Would like to a see a little on that. Some material here
http://www.bio.brandeis.edu/classes/biochem102/hndEnzKin.pdf
and http://www.jbc.org/cgi/reprint/235/8/2440.pdf
cheers Shyamal 01:52, 27 September 2006 (UTC)
replies: text: Since these equations relate to allostery in general, not just enzyme kinetics, they would be best added to the page on cooperativity. I think deriving all the inhibition equations would take several pages and not add much to an article for the general reader. TimVickers 20:41, 19 October 2006 (UTC)
thread_title: Briggs-Haldane modification to the M-M scheme

message: The article says: "Some enzymes produce a sigmoid v by [S] plot, which often indicates cooperative binding of substrate to the active site." Could non-cooperative binding with multiple binding sites also produce sigmoidal curves? In other words, do sigmoidal curves always necessitate a ligand binding to one site to affect the affinity of other sites? Is there a counter-example? Can non-cooperative binding cause threshold effects via sigmoidal activation? (it seems so based on the following article, but I am not sure: http://arxiv.org/abs/physics/0609227)
Suu 14:35, 26 January 2007 (UTC)
replies: text: Substrate activation is a possibility in one active site, where ES2 is more active than ES. However, these two molecules of substrate must bind in different places, even if these are adjacent. However, I can envisage a model where an enzyme has two slowly-interconverting conformations with the active conformation being stabilised by substrate. I'll try to find if this has been observed. TimVickers 16:55, 26 January 2007 (UTC)
thread_title: Sigmoidal curves with non-cooperative binding?

message: I haven't been able to read the whole article yet, but through skimming and searching I can't see any mention of the action of temperature on enzyme kinetics (e.g. exponential increase of activity then sudden denaturation, different optimums in coldblooded and warmblooded animals, thermophiles etc), and there also seem to be little on the effects of chemical factors (such as pH changes, different environments in various organs and organelles). The article is no doubt of a high quality, but these seem to be serious omissions for a featured article. They are mentioned briefly in the enzyme article, and I was expecting the main discussion of them to be here. Richard001 04:45, 31 July 2007 (UTC)
replies: text: These are discussed briefly in Enzyme assay, but protein stability hasn't got much to do with enzyme kinetics. Temperature in particular is very badly described in these terms, since the "optimum" rate of an enzyme reaction is the product of two rates, the reaction rate and the denaturation rate. If you were to use an assay measuring activity for one second, it would give high activity at high temperatures, however if you were to use an assay measuring product formation over an hour, it would give you low activity at these temperatures. It is discussed in this paper in a bit more detail. Tim Vickers 16:02, 2 August 2007 (UTC)
replies: text: Oh, I hadn't looked at enzyme assay. It basically covers the areas I'm talking about, but doesn't go into great detail. Where would be the best article to expand on these factors? Richard001 04:38, 4 August 2007 (UTC)

text: Enzyme assay I suppose, it isn't a particularly good article at the moment so your edits could improve it a great deal. Tim Vickers 14:39, 4 August 2007 (UTC)

text: True 69.143.236.33 06:31, 22 October 2007 (UTC)
thread_title: The effects of temperature and environment on enzyme kinetics

message: M−1 s−1
# Tim Vickers 03:58, 26 October 2007 (UTC)
replies: text: I like a good poll. It seems if one is interested enough to read this far, a poll can be a better indicator of the current consensus than just another comment that makes this discussion even harder to read.71.238.71.180 18:23, 2 December 2007 (UTC)
replies: text: "Although for brevity and convenience all volumes are expressed in dm3, in all cases dm3 may be replaced identically with L or l (liter), and amount-of-substance concentrations may be expressed in M (molar), which is identical with mol dm-3. Both L and M may be used as primary units for forming multiples and submultiples such as mL, [mu]M, etc." 
That is to say, the recommendations of an international body writing on the specific point at hand differ from the recommendations of a standards body of a particular country, writing about the topic in generalities. -- 17:03, 6 December 2007 (UTC)
thread_title: Straw poll

message: # Gene Nygaard 13:55, 26 October 2007 (UTC)
replies: text: I like a good poll. It seems if one is interested enough to read this far, a poll can be a better indicator of the current consensus than just another comment that makes this discussion even harder to read.71.238.71.180 18:23, 2 December 2007 (UTC)
thread_title: Lack of foundation, object to relevance and phrasing and choices and much more

message: I would like to point out that in the current version of the International Union of Biochemistry and Molecular Biology's nomenclature recommendations (http://www.iubmb.unibe.ch/ -> Publications -> Biochemical Nomenclature -> Nomenclature Website -> (http://www.chem.qmul.ac.uk/iubmb/nomenclature/) -> Enzyme Kinetics -> 13. Summary of recommended symbols) allows for the use of M (molar): 
::"Although for brevity and convenience all volumes are expressed in dm3, in all cases dm3 may be replaced identically with L or l (liter), and amount-of-substance concentrations may be expressed in M (molar), which is identical with mol dm-3. Both L and M may be used as primary units for forming multiples and submultiples such as mL, [mu]M, etc." 
That is to say, the recommendations of an international body writing on the specific point at hand differ from the recommendations of a standards body of a particular country, writing about the topic in generalities. -- 17:03, 6 December 2007 (UTC)
thread_title: Comments

message: I believe the arrows in the second half of the diagram are going the wrong direction - P and Q are leaving the complex, not being added, so the arrows should be pointing away from the hexagonal pathway.IMKatgrrl (talk) 11:01, 23 October 2009 (UTC)
replies: text: I believe so too, feel free to change it. It is still clear what is meant but it would be nicer if P and Q are leaving the complex. Greetings --hroest 12:08, 23 October 2009 (UTC)
replies: text: Good point! Tim Vickers (talk) 16:09, 23 October 2009 (UTC)
thread_title:  Random-order ternary-complex mechanism diagram 

message: I sincerely apologize if I am being stupid, but this picture, which appears in the first section after the lead in the article, makes very little sense to me. If I understand correctly, whenever the article talks about the rate of reaction for a given concentration of substrate, it means the instantaneous or initial rate. So I take "at relatively high substrate concentrations, the reaction rate asymptotically approaches the theoretical maximum; the enzyme active sites are almost all occupied and the reaction rate is determined by the intrinsic turnover rate of the enzyme" to mean that if you've got very concentrated substrate then the enzyme will just eat away at the substrate, and the reaction will go at pretty much the same speed, since it was at the maximum already, but then after a while the rate will drop as the substrate is depleted. The figure, on the other hand, appears to bear no relevance to the caption, showing enzymes making ... more and more substrate over time? Please explain. Leonxlin (talk) 04:14, 18 August 2011 (UTC)
replies: text: It's not meant to represent a change over time.  It just shows what happens under different concentrations of substrates.  Once all the enzymes are occupied, adding substrate has no more effect.  (Approximately - in practice there is always a binding equilibrium and there are thus always a few empty places, the number of which decrease depending on how quickly the substrate can reach them).   Probably the green arrows were a bad idea - I'd suggest editing the figure to take them out. Wnt (talk) 22:01, 4 September 2011 (UTC)

text: I took a stab at rewriting the figure legend.  Wnt (talk) 22:23, 4 September 2011 (UTC)
thread_title:  Confusing picture 

message: Under "Linear plots of the Michaelis–Menten equation" the article seems to be too focused on Lineweaver-Burk, which is probably the worst of all the plots mentioned. Would it be worth changing this to Eadie-Hofstee or Hanes-Woolf, or just removing the focus on any one plot?
Esotera (talk) 10:57, 4 January 2012 (UTC)
thread_title:  Too concentrated on Lineweaver-Burk plot? 

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thread_title:  External links modified 

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thread_title:  External links modified 

message: The use of the word "quickly" in the sentence "The two most important kinetic properties of an enzyme are how quickly the enzyme becomes saturated with a particular substrate, and the maximum rate it can achieve." (Enzyme kinetics#General_principles) is very misleading because it seems to relate to time, whereas the MM model describes steady-state kinetics... What about "how easily it is saturated..." instead? Lewisiscrazy (talk) 09:17, 21 January 2018 (UTC)
replies: text: Done --Lewisiscrazy (talk) 06:12, 20 March 2018 (UTC)
thread_title:  The meaning of Km in the section about "General principles" 

message: I think it would be useful to add a subsection entitled "Reversible catalysis and the Haldane equation" in the section about Single substrate reactions. I have worked on this draft https://fr.wikipedia.org/wiki/Utilisateur:Lewisiscrazy/Brouillon-2, what do you think? can somebody contribute? Lewisiscrazy (talk) 15:41, 21 January 2018 (UTC)
replies: text: Added: https://en.wikipedia.org/wiki/Enzyme_kinetics#Reversible_catalysis_and_the_Haldane_equation --Lewisiscrazy (talk) 14:32, 11 February 2018 (UTC)
replies: text: Check out WP:NOTTEXTBOOK.  Wikipedia presents knowledge, but does not explain it. That is the encyclopedic style that can be subtle to grasp. Sections that begin "We consider the case of .." are in appropriate.  --Smokefoot (talk) 13:08, 8 April 2018 (UTC)
thread_title:  Adding a subsection about reversible catalysis? 

message: This 2006 Featured article has not been maintained to WP:WIAFA standards. Unless someone can cite the considerable amount of uncited text, the article should be submitted to Featured article review.  SandyGeorgia (Talk)  21:03, 13 December 2020 (UTC)
thread_title:  [[WP:URFA/2020]]