Talk:Enzyme
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[edit] A turd...?
Why is there a picture of a turd on this page...? Is it vandalism or does it have something to do with enzymes? —The preceding unsigned comment was added by 64.203.165.125 (talk)
- Vandalism. Duly reverted. Fvasconcellos 19:08, 11 October 2006 (UTC)
[edit] 'High energy' ATP?
ATP is a high-energy compound, is it? What nonsense! The cell keeps ATP concentrations at much higher levels relative to ADP than the equilibrium. When an unfavourable reaction is coupled to the ATP to ADP reaction, the high concentration of ATP drives the reaction forwards. It's the concentration of ATP that is crucial, not some magic bond attaching the third phosphate (usually drawn with a ~ as if it's some sort of special bond).
Also from the thermodynamics section: "However, the uncatalyzed, "spontaneous" reaction might lead to different products than the catalyzed reaction." This could be construed as meaning that the enzyme can change the products of the reaction. How about "Without catalysis, the reaction might be so slow that other reactions (leading to different products) might occur instead." Ewen 08:07, 11 October 2006 (UTC)
- Certainly the high concentration of the ATP is can increase the energy charge and the available free energy from hydrolysis. Nevertheless, the fact that the hydrolysis has a large negative free energy would not be true except for the properties of the magic bond. Without the large difference in resonance stabilization before and after hydrolysis even a high concentration of ATP would be worthless for coupling unfavourable reactions. David D. (Talk) 08:41, 11 October 2006 (UTC)
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- Just checking the figures given in Stryer: The equilibrium for a coupled reaction is increased by a factor of about 105 by the ATP/ADP+Pi reaction, but an additional factor of about 103 is due to the high levels of ATP maintained in the cell. Ok, that means the standard free energy of reaction itself is about 100 times more important than the ATP levels in coupling. On the other hand, if ATP levels were allowed to fall then eventually the low ATP concentration would negate the favourable free energy of the hydrolysis. Also worth considering is that ATP is not particularly special. Phosphoenolpyruvate, for example, has a much larger free energy of hydrolysis. How 'magic' is that bond, then? If the standard free energy was all that was important, then ATP would be a poor choice of energy currency. I feel that refering to ATP as having some sort of high energy magic bond is misleading. Ewen 09:27, 11 October 2006 (UTC)
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- Clearly both are important. And it depends what kind of magic you are looking for in the bond. With respect to ATP, being an intermediate energy bond is the magic, ADP can easily be phosphorylated (PEP as a source of phosphate for one) as well as ATP being able to couple reactions. Both are required for the ATP to be so versatile as an energy carrier. See if Stryer discusses that idea or not. I agree that it is not the highest energy bond but it is high energy enough to drive endergonic reactions (combined with the high energy charge). David D. (Talk) 15:01, 11 October 2006 (UTC)
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- I agree that the term "high-energy bond" is misleading as it is displacement from equilibrium that provides useful energy, not really any property unique to ATP itself. I have reworded the section on spontaneous reactions. TimVickers 15:30, 11 October 2006 (UTC)
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[edit] Promiscuous
In http://en.wikipedia.org/wiki/Enzyme#Specificity the word promiscuous is a wikilink but links to the word as it is generally used. I would recommend either creating a disambiguation page with a red link, eg. for Promiscuous (biology) or perhaps, consider not wikilinking it at all. It depends on whether it is a term that gets used, and hence, whether it will ever get a page of its own. 128.250.6.247 10:22, 11 October 2006 (UTC)
- Removed link and reworded, since plant secondary metabolites are produced by quite specific enzymes. GSTs and P450s are the broad-specificity enzymes. TimVickers 15:33, 11 October 2006 (UTC)
[edit] Diagram captions
The text below the "Induced fit" diagram is slightly misleading - perhaps clearer might be "substrate entering active site on enzyme" and "product leaving active site on enzyme' Paul venter 10:31, 11 October 2006 (UTC)
- I'm thinking it's supposed to be read as enzyme + substrate-entering-active-site. but i agree, it's very confusing. It's makes it sound like as if both the enzyme and the substrate were entering/leaving the active site. --`/aksha 12:19, 11 October 2006 (UTC)
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- It is confusing, will need new diagram. TimVickers 15:34, 11 October 2006 (UTC)
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- New diagram uploaded. TimVickers 18:26, 11 October 2006 (UTC)
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[edit] Catalytically perfect enzymes
I really think that comment "TIM is catalytically perfect, meaning its conversion rate is limited, or nearly limited, to its substrate diffusion rate." should be removed from the caption of the TIM picture.
It's not a particularly important/significiant enzyme concept, putting it up in the caption for that picture basically means it will be one of the first things a reader reads when they reach the article.
For someone who doesn't already know about enzymes and hasn't already read the article, the comment is a bit out of place and confusing, even with the "meaning its conversion rate is limited, or nearly limited, to its substrate diffusion rate." explaination.
Can we remove the comment and/or replace it with something more general that would be fitting for an article introduction? Something like "Ribbon diagram of the enzyme TIM. TIM is an essential enzyme for efficient energy production, and is found in almost all organisms...etc"
Catalytically perfect enzymes are already mentioned in the article body anyway, in a place that's appropriate (i.e. under Kinetics, not at the really top of the article.) --`/aksha 12:18, 11 October 2006 (UTC)
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- I agree, reworded caption to be as simple as possible. TimVickers 15:37, 11 October 2006 (UTC)
[edit] Mass edits and vandalism
Why has this article become the target of vandals with too much time on their hands? --HashiriyaGDB 12:22, 11 October 2006 (UTC)
- Why are you surprised? If you're wanting to vandalise wikipedia but you don't know which article to choose, why not start with the one which is on the front page? featured article = tons of attention = tons of attention from vandals as well. --`/aksha 12:27, 11 October 2006 (UTC)
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- Yep - perfectly normal syndrome - only time makes them go away. Paul venter 13:23, 11 October 2006 (UTC)
[edit] Catalase
Should we briefly mention the turnover rate of catalase or something to give people an idea of how effective enzymes can be? Nil Einne 14:32, 11 October 2006 (UTC)
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- This was in the lead but was removed. Now added back to second section of kinetics section. TimVickers 15:28, 11 October 2006 (UTC)
[edit] Vectorized diagram
I believe this has been discussed before, but here goes: I have created a vectorized version of Image:Competitive inhibition.png (properly vectorized, not embedded the .PNG in an .SVG file) and uploaded it to Commons as Image:Competitive inhibition.svg. I made no noteworthy changes whatsoever, it is practically a facsimile of the .PNG, and have replaced it in the article. If anyone wishes to change it back, go right ahead. I can also vectorize the remaining .PNG diagrams (induced fit and Inhibiteur competitif on Enzyme inhibitor) – would that be OK? Fvasconcellos 15:37, 11 October 2006 (UTC)
- Looks great, thanks. Go right ahead, but I'd hold off on the Induced Fit diagram since this will be changing soon, as per above discussion. TimVickers 15:40, 11 October 2006 (UTC)
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- Agreed. Thanks, Fvasconcellos 15:41, 11 October 2006 (UTC)
[edit] Confusing Fig Refs or Missing Figures?
Several figure references have confused me:
In the "Cofactors" section, the reference "a cofactor is carbonic anhydrase, and is shown in the diagram above with four zinc cofactors bound in its active sites" was a little confusing because the referent image is two images above, and several screens (on this low-res display).
In the "Inhibition" section, what figures are meants by "(right, top)" and "(right, bottom)"? I believe I understand that the bottom figure shows an enzyme and an inhibitor, but not the act of inhibition, whereas the top diagram does show the act. It's be less confusing if the top diagram had a third section showing competitive inhibition.
Maybe a good fix is to label all figures and refer by label? It'd be nice if wikipedia automated this...
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- I have tried to reword this to be less confusing. TimVickers 19:44, 11 October 2006 (UTC)
I still find this confusing; also, there is a lot of overlap, but with different diagrams and text, with Enzyme Inhibition.
[edit] Contact Lens Cleaner
Probable error:
- "To remove proteins on contact lens to prevent inflections."
I would fix this myself but I'm not 100% and it is a featured article today. I assume it is suposed to be infections. Perhaps this is a technical term in this narrow area having to do with internal reflections?--Nick Y. 19:17, 11 October 2006 (UTC)
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- Typo indeed. Corrected. TimVickers 19:43, 11 October 2006 (UTC)
[edit] Enzymes that slow reactions?
Can anybody think of an example? TimVickers 16:30, 17 October 2006 (UTC)
- I'm not sure I see where this is going. What made you think of this? To answer your question, I cannot think of one off the top of my head. David D. (Talk) 16:42, 17 October 2006 (UTC)
See the edit histtory, somebody was saying some enzymes slow reactions. Antioxidant enzymes just remove the oxidants, so they speed removal reactions - reducing the steady-state concentration of things such as H2O2 or superoxide. TimVickers 18:24, 17 October 2006 (UTC)
- Many enzymes will effectively slow down a reaction, by promoting a different reaction. However, I don't know an enzyme that actually slows a reaction - by default this would not be catalysis - so I don't think you could even call it an enzyme maybe an "anti-enzyme" :-) Hichris 18:30, 17 October 2006 (UTC)
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- Chaperones don't appear to be enzymes themselves. DMacks 20:29, 17 October 2006 (UTC)
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- Yes, if a chaperone just binds to the unfolded state then this is a simple ligand binding process, so not really a chemical reaction. Even inhibitory kinases or phosphatases accelerate their reaction and it's the effects of this accelerated reaction that slow a second, independent reaction. TimVickers 20:45, 17 October 2006 (UTC)
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Enzymes are by definition biological catalysts. You can't catalyse something to not happen, or to happen more slowly. It would be a contradiction in itself. A protein that slowed down a reaction or stopped it would be an inhibitor of some kind. A enzyme could catalyse a reaction that results in the slowing down or prevention of some other reaction from occuring, but the primary purpose of the enzyme would still be to speed up a reaction. --`/aksha 04:19, 18 October 2006 (UTC)
[edit] New lead image
I'm not sure who added the new lead image but I personally prefer it to the older image with the black back ground. I have not seen that style of ribbon and space filling model before, it is quite effective. David D. (Talk) 00:26, 31 October 2006 (UTC)
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- It came in the blizzard of edits on our day in the sun. I like it too and am glad my namesake enzyme is still on top! TimVickers 00:30, 31 October 2006 (UTC)