Talk:Pyruvate dehydrogenase complex

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Molecular Biology: MCB

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Untitled[edit]

It would probably be better if we didn't merge in unrelated articles like the reviewer suggested. —Preceding unsigned comment added by 71.195.51.123 (talk) 19:46, 2 December 2007 (UTC)[reply]

at http://www.rpi.edu/dept/bcbp/molbiochem/MBWeb/mb1/part2/krebs.htm "Pyruvate Dehydrogenase is a large complex, with multiple copies of each of three enzymes, E1, E2, and E3. The structure of the complex is depicted in figures on p. 769 & 774 of Biochemistry, 3rd Edition, by Voet & Voet. The core of the complex consists of 60 copies of E2. At the periphery of the complex are:

30 copies of E1 (itself a tetramer with subunits a2b2) and
12 copies of E3 (a homodimer), plus 12 copies of an E3 binding protein that links E3 to E2."

This conflicts with the article.GangofOne 07:07, 11 May 2005 (UTC)[reply]

EC number 1.2.4.1 is also a pyruvate dehydrogenase.

What about the influence of hormones like vasopressin and insulin on this reaction?Ankmin 03:22, 22 April 2006 (UTC))[reply]

Pyruvate transport[edit]

In the article, it is stated that "pyruvate cannot diffuse passively because it carries a negative charge". In the preceding sentence, the article then offers, without further clarification, that pyruvate transport is "active" and "requires energy". I don't know the veracity of the fragment regarding its transport being active, although pyruvate is negatively charged. What I'm not sure about is if the editor was fallaciously drawing a connection between the two clauses - just because passive diffusion is impossible does NOT mean active transport, requiring energy, is the only alternative. Pyruvate could also be facilitated in its transport. On the other hand, if pyruvate is moving against its concentration, or an electrical, gradient, its transport would indeed need energy. In summary, the section on pyruvate's transport needs review by someone who knows whether it is active or not, and the details of its transport regardless. - DrLight11 —Preceding unsigned comment added by 70.179.126.6 (talk) 02:50, 13 September 2010 (UTC)[reply]

If it helps I remember reading somewhere about the net ATP gain of glucose metabolism, that the transport requires ATP. Sorry no source, maybe I will double check later when I have time.158.132.137.233 (talk) 06:11, 17 April 2014 (UTC)[reply]

Unclear link between LDC inhibition and lower glucose metabolism[edit]

The part about regulation mentions starvation causes LDC inhibition, thus reducing the amount of pyruvate converted to Acetyl-CoA. It is not explicitly mentioned if pyruvate production(glycolysis) is also lowered, though if not then pyruvate would build up? It is also implied that after LDC inhibition fat metabolism will be promoted rather than fermentation, I guess because increased fermentation would decrease glucose stores faster. I think the regulation pathways could be better defined, as it is not clear how inhibition of LDC is substituted by other energy synthesis pathways (or apoptosis).158.132.137.233 (talk) 06:36, 17 April 2014 (UTC)[reply]

Of I meant PDC instead of LDC, of course. Mistake.158.132.137.233 (talk) 08:20, 17 April 2014 (UTC)[reply]

Assessment comment[edit]

The comment(s) below were originally left at Talk:Pyruvate dehydrogenase complex/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.

This is a very good article and the pyruvate decarboxylation article should be merged into it.

Last edited at 01:13, 22 November 2007 (UTC). Substituted at 03:35, 30 April 2016 (UTC)

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