Talk:Catalase

message: I've been researching catalase and keep coming up with conflicting figures.  Everyone says "it's one of the most efficient enzymes," but after that, numbers diverge.  In this article alone, it is purported to "convert 5 million molecules of hydrogen peroxide to water and oxygen each minute" and "500,000/second."  Which is it?  Are the numbers refering to two different things, maybe?  If so, can we clarify that in the article a little better?  Also, sources?
Thanks for your time.
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This page quotes M.B.V. Roberts, author of "Biology A Functional Approach" as saying that catalase has a turnover number of 6 million/min
Kb ganesh 18:18, 29 August 2006 (UTC)
replies: text: I think part of the problem is that there are different kinds of catalase. Another problem is that the rate of reaction is heavily influenced by the conditions in which it occurs. I'll work on making this clear in the article. Galanskov 01:57, 12 February 2007 (UTC)
replies: text: First, do the math: 500,000/sec only three times 5,000,000/min. So they're not that different, on the sort of scale we're talking about. Enzyme efficiency also depends upon environmental factors. In other words, it's a rough estimate. Fearwig 08:48, 10 August 2007 (UTC)
replies: text: 500,000/sec is actually six times 5,000,000/min. And that isn't "not that different", it's actually quite a lot. It's true they're on a big scale.. but having differences of up to 6 times bigger is still a lot. - Draygen 19:43, 9 February 2009 (UTC)
thread_title:  5 Million? 30,000,000? Both? Neither? 

message: Please semiprotect this page. It has been a target of vandalism by someone by the IP 85.12.64.148. --Gray Porpoise 17:26, 28 June 2006 (UTC)
thread_title:  Protection 

message: The catalase test bit doesn't really explain what it's for very well. A biologist of any calling will probably have no problem guessing what it's for with the info currently given but someone else might go, what the heck? Nil Einne 14:37, 11 October 2006 (UTC)
replies: text: It is also apparent that the Action of Catalase and Catalase Test (under Human application) say the same exact thing. This should be rectified, but I don't have the time nor the knowledge to do so. Helixer (talk) 02:29, 25 November 2008 (UTC)
thread_title:  Catalase test 

message: I would like to know the temperature at which catalase activity is optimized. Is it significantly different for human catalase as opposed to the catalase found in bovines? —The preceding unsigned comment was added by 207.71.230.77 (talk) 05:33, 12 December 2006 (UTC)
thread_title:  optimum temperature for catalase activity 

message: This sentence used to be:
Hydrogen peroxide is formed as a waste product of metabolism in many living organisms
It is now:
Hydrogen peroxide is not as a neverof metabolism in many dead organisms.
I believe that the previous edition is correct, but I don't know much about biology. Maybe the editor didn't know much english. —The preceding unsigned comment was added by 66.67.107.143 (talk) 00:27, 13 December 2006 (UTC)
thread_title:  The first sentence after the "Role in organs" 

message: Is it clear the number of cells that have catalase in it?  I think people come out of microbiology after they learn about staph aureus and the catalase test used to distinguish it and think that it is one of the few "cells" organisms that have catalase and maybe it should be emphasized more that a lot of cells have catalase in them.  An exhaustive list would be cool but maybe impossible (?). —The preceding unsigned comment was added by 207.151.236.42 (talk) 22:41, 28 January 2007 (UTC)
replies: text: The article actually makes it sound as though almost every organism has catalase in it, which is dead wrong. There are a wide variety of bacteria (aerobic and anaerobic) that don't, and contrary to what the article says, there are a lot of fungi (especially higher fungi) that apparently do. Otherwise, peroxide would be an absolutely rotten sanitizer, which it isn't. Unless I'm misunderstanding something, that is. Fearwig 08:52, 10 August 2007 (UTC)
thread_title:  Could you list every cell that has catalase in it?

message: I can't find any information to add about the catalytic strategy of catalase, and I believe this is important. Hopefully someone can tell me HOW catalase reduces the activation energy of (what?) This info seems to be non-existent.
As soon as I get the chance I'd like to add the source:
Vetrano, Anna M., et al. "Characterization of the Oxidase Activity in Mammalian Catalase." The Journal of biological chemistry 280.42 (2005):35372-.
Thanks, cyanide_sunshine —The preceding unsigned comment was added by 139.225.66.202 (talk) 20:03, 11 April 2007 (UTC)
thread_title:  Catalytic Strategies of Catalase 

message: The catalase FAQ link is dead.  should it be removed? soldierx40k 20:41, 29 September 2007 (UTC)
thread_title: Dead link

message: This article tries to do too much. It should be split into a main page with a treatment of catalases (which I believe are not all homologs) and the known catalases from the various organisms. AnteaterZot (talk) 00:14, 6 February 2008 (UTC)
replies: text: This page is short compared to many Wikipedia pages. Granted, it's not a stub, but if you broke it into to pages, then each one would be. And what do you mean by "treatment" of catalases? Furthermore, I don't think there is more than one kind of catalase. Heck, my spell-check says catalases isn't a word!  PhishRCool Talk / Contribs / Secret Page 21:47, 20 October 2008 (UTC)

text: I am studying for Step 2 of the US Medical Licensing Exam right now, and this article seems just right to me.Niels Olson (talk) 00:39, 21 November 2008 (UTC)
replies: text:  I think a split would be inappropriate. Since the proposal was over a year ago now, I have removed the tag. Parslad (talk) 15:15, 25 February 2009 (UTC)
thread_title: Split

message: http://www.webmd.com/skin-problems-and-treatments/news/20090225/why-hair-goes-gray
96.224.179.123 (talk) 10:24, 1 March 2009 (UTC)
thread_title:  I found a new article for you folks 

message: Many authors refer to both Streptococcus and Enterococcus species as being “aerobic bacteria” because of their ability to grow in the presence of oxygen. However, the species of those two genera do not use oxidative metabolism for their energetic needs. Instead, they are fermentative bacteria, and yes, the process of fermentation can occur in the presence of oxygen. Thus, more appropriate affiliation for Streptococcus and Enterococcus bacteria would be “oxygen-indifferent anaerobes”, which clearly indicates that they do not care if oxygen is present or not. They grow equally well in the presence or the absence of oxygen. By not using the oxygen (and therefore not having cytochrome oxidase complex) they do not generate hydrogen peroxide and do not require catalase for the elimination of this harmful by-product.  —Preceding unsigned comment added by Nedemandeplus (talk • contribs) 16:00, 10 March 2009 (UTC)
thread_title:  Catalase, Streptococci and Enterococci 

message: The section on how the Bombardier beetle uses catalase is a bit confusing and doesn't seem to conclude with what it does with that reaction. It might need rewording, but I'm not entirely sure what to change it to, maybe some one else might have the skill,  Abergabe (talk) 15:50, 28 June 2010 (UTC)
replies: text: The key point that was left out is that the oxidation reaction is very exothermic.  I have attempted to clarify this section in this edit. Cheers.  Boghog (talk) 18:30, 28 June 2010 (UTC)
thread_title: Catalase and the Bombardier Beetles

message: Does anyone know which foods are a good source of catalase? I would like to know, so I can consume these types of foods and try and restore the color of my hair which has gone a little grey. I believe that eating foods, which are a good source of catalase, is better than taking a vitamin supplement which contains catalase.204.80.61.110 (talk) 19:14, 4 August 2010 (UTC)
thread_title: Food sources of Catalase?

message: This is confusing.  Catalase reacts with hydrogen peroxide by turning it into water and oxygen?  Where does the extra oxygen atom come from?  It sounds like you're saying that FeIV becomes the extra atom.  I know I'm ignorant, can someone dumb it down for me?  Thetrellan (talk) 17:05, 5 July 2012 (UTC)
replies: text: Not at all a dumb question.  The answer is provided later in the article: 2 H2O2 → 2 H2O + O2  I am not sure how to fix this however since the lead is supposed to be kept dead simple and the answer to your question requires a somewhat more involved answer.  Boghog (talk) 18:30, 5 July 2012 (UTC)
thread_title:  Iron becomes oxygen? 

message: What's the empirical formula of catalase? Can't find it anywhere.Fletcherbrian (talk) 19:06, 9 July 2014 (UTC)
thread_title:  Empirical Formula? 

message: (English is not my native language, I'm sorry for possible grammar errors)
According to the Celluar Roles section of this page "the Human catalase works at an optimum temperature of 45 °C." 
But the source  doesn't mention a temperature of 45C anywhere, even when accessing the full pdf. 
I'm not a scientist or anything, just a student, and I most likely just made a error, but can someone else check if it is verified somewhere. 
Tijmen Wil (talk) 07:01, 26 October 2016 (UTC)
replies: text: I see someone's changed it to 37 °C in the meantime, but we are still lacking a good source. I can find a few rather dodgy book sources, and this article says that bovine catalase works best at 35 °C, both bound and free. --Slashme (talk) 18:37, 27 September 2017 (UTC)

text: Here's a 1956 article from Japan that gives the optimum temperatures for catalase from a variety of organisms. Not sure how accurate it is, though, because for bovine catalase it differs from a more recent article by 5 °C. --Slashme (talk) 18:40, 27 September 2017 (UTC)

text: This article finds a higher activity at 45 °C than 37, but didn't test at a higher temperature. I'm going to remove the statement about optimum temperature until someone finds a really good quality source. --Slashme (talk) 18:49, 27 September 2017 (UTC)
thread_title:  "Human catalase works at an optimum temperature of 45 °C" not comfirmed in source 

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