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Wiki Education Foundation-supported course assignment

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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): Sarahnkov.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 17:56, 16 January 2022 (UTC)[reply]

Untitled

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The article seems to say the same thing twice--about vitamins being organic and coenzymes.

  • It also says that cofactors can either be metal ions or organic things like vitamins twice.

Pasted from the disambig over at cofactor, some material could be integrated here:

Cofactor:a small, non-protein molecule or ion that is bound in the functional site of a protein and assists in ligand binding or catalysis or both. Some cofactors are bound covalently, others are not. For example, prosthetic groups and compounds such as NAD, NADP, flavin nucleotides, coenzyme A.

Template help

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If anyone has time, the {{Enzyme cofactors}} template would really benefit from your expertise. Thanks! :) Willow 19:11, 27 January 2007 (UTC)[reply]

Non-enzymatic cofactors

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Just FYI, here are examples of articles using the term in the broader sense I indicate in this section:

http://mcb.asm.org/cgi/content/abstract/22/6/1626 http://www.ncbi.nlm.nih.gov/pubmed/15860367 http://www.nature.com/nature/journal/v398/n6730/full/398824a0.html

Jbening (talk) 00:48, 16 October 2008 (UTC)[reply]

Biochemical stupidity

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I deleted the figure, because I do not what it shows, but I clearly know that succinate dehydrogenase is the typical example of an oxidoreductase that is NOT a heme protein, but an iron suflur protein. This can be verified in any biochemical textbook.

Lulubou (talk) 09:42, 9 March 2009 (UTC)[reply]

To see a clearer example of the cofactors in succinate dehydrogenase, refer to File:Succinate Dehydrogenase 1YQ3 Electron Carriers Labeled.png. The heme group is in the transmembrane domain of this complex. Would you prefer this image in the article? Tim Vickers (talk) 16:41, 9 March 2009 (UTC)[reply]

Yes, that one looks nice. Lulubou (talk) 18:35, 9 March 2009 (UTC)[reply]

OK, done! Tim Vickers (talk) 20:34, 9 March 2009 (UTC)[reply]

The picture seems to show that succinate and FAD enters during the same reaction cycle. Doesn't FAD enter much earlier and stay for several reactions? Narayanese (talk) 07:50, 11 March 2009 (UTC)[reply]


FAD is covalently bound in succinate dehydrogenase

Lulubou (talk) 11:38, 11 March 2009 (UTC)[reply]

Merger

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Great !. Good idea to merge the articles on cofactors, coenzymes and prosthetic groups. I have not yet looked at the details, but the article looks great and well structured.

I am just wondering, if those readers that are redirected from the terms ”coenzyme” and ”prosthetic group” mightl not be frustrated when they do not see these terms immediately. Maybe it would be good to add them in the title that could run : Cofactors, coenzymes and prosthetic groups. It would be nice if the terms "coenzymes" and "prosthetic group" already appear in the introduction with a small explanation.

Lulubou (talk) 11:38, 11 March 2009 (UTC)[reply]

Added to lead. Tim Vickers (talk) 16:35, 11 March 2009 (UTC)[reply]

The thiamine cofactor

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This article uses the term thiamine diphosphate (ThDP) and the article to which it links is titled thiamine pyrophosphate (TPP), but acknowledges the alternative term . I know it is a matter of in which enzymology circles you roam, but should we be internally consistent and call it TPP in this cofactors article? The problem I have with thiamine diphosphate is some people (a rather famous enzymologist included) abbreviate it TDP, and that gets confused with the thymidine diphosphate. Pdcook (talk) 15:38, 9 October 2009 (UTC)[reply]

You're right, I'd prefer TPP as well. Tim Vickers (talk) 17:29, 9 October 2009 (UTC)[reply]
Since there is no dissent, I'm going to change it to thiamine pyrophosphate.Pdcook (talk) 17:55, 13 October 2009 (UTC)[reply]

Cofactors are non-protein?

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ApoC-II and apoA-I are protein cofactors for lipoprotein lipase (LPL) & lecithin-cholesterol acyltransferase (LCAT), respectively. I just linked the word "cofactor" in that article to this article, but the first thing this article says is contradictory to the function of these two apolipoproteins. What's up? Dcs002 (talk) 23:24, 18 July 2010 (UTC)[reply]

The strict definition is non-protein, but some people use the word more loosely. I'd just call these proteins enzyme activators myself, since their presence isn't essential for enzyme activity. Tim Vickers (talk) 00:50, 19 July 2010 (UTC)[reply]

Cofactors not yet discussed

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Several glutathione analogs are not yet discussed, including mycothiol, bacillithiol, and trypanothione.

Chlorophyll deserves to be discussed as a cofactor.

The page also should mention that a number of cofactors (e.g. heme) exist in a variety of forms. — Preceding unsigned comment added by Daniel haft (talkcontribs) 16:09, 19 March 2012 (UTC)[reply]

"Cofactors are inorganic" vs "five organic cofactors".

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Either one must be false. Please correct. -- 78.50.190.114 (talk) 16:53, 12 December 2012 (UTC)[reply]

Cofactor Binding

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The first paragraph states that "A cofactor is a non-protein chemical compound that is bound to a protein..." and the second paragraph states that "Cofactors can be classified depending on how tightly they bind to an enzyme...". These would seem to be in conflict. Are cofactors things that bind to protiens or bind to enzymes or is it both?

Assessment comment

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The comment(s) below were originally left at Talk:Cofactor (biochemistry)/Comments, and are posted here for posterity. Following several discussions in past years, these subpages are now deprecated. The comments may be irrelevant or outdated; if so, please feel free to remove this section.

Changed rating to "high" as this is high school/SAT biology content. - tameeria 21:45, 18 February 2007 (UTC)[reply]

Last edited at 21:45, 18 February 2007 (UTC). Substituted at 11:59, 29 April 2016 (UTC)

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Coenzyme and cofactor

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Hello Boghog,

Currently, Coenzyme is redirected to Cofactor.

I think that Coenzyme should stand by itself. I am willing to re-edit the entries. But, before I start working on this I would like to hear your opinion on the subject.

Rationale, Cofactor entry is currently too long. Coenzyme deserves an entry by itself.

Please inform what you think on this.

Genewiki1 (talk) 15:28, 11 February 2018 (UTC)[reply]

Hi @Genewiki1:. I hope you don't mind, but I move the discussion here to give others a chance to comment. I agree that cofactor is getting a bit too long and should be split. But I am undecided at the moment about the best way to do this. I have noticed that some text books define an inorganic cofactor as an activator with the following hierarchy:
So one way to do this is to have a parent cofactor article (perhaps renamed as enzyme cofactor) and move most of the material to the two daughter pages. The only problem is that enzyme activator has apparently two meanings, an inorganic cofactor and an allosteric activator which is usually organic. Perhaps we should rename the present enzyme activator article to enzyme activator (organic) and to split out a enzyme activator (inorganic) from the cofactor article. Does this make sense or is it too complicated? Boghog (talk) 17:19, 11 February 2018 (UTC)[reply]
Hi @Boghog:. Exactly as you wrote, the cofactor article should be the parent article. Initially, I did not like changing its name to 'enzyme cofactor". BUT, on second thought I like your suggestion. Currently, the Cofactor article appears as Cofactor_(Biochemistry), to distinguish it from other "cofactors". Your suggestion is better than "Cofactor_(Biochemistry)". What we are talking about matches the definition of these terms in Lehninger Principles of Biochemistry which from my perspective is the best and clear-cut definition of these terms.Genewiki1 (talk) 18:44, 11 February 2018 (UTC)[reply]

Protein-derived cofactors

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Where do "protein-derived cofactors" fit in the types of cofactors in the introduction? kupirijo (talk) 13:00, 3 October 2023 (UTC)[reply]