Pyruvate dehydrogenase

From Biocrawler, the free encyclopedia.

Pyruvate dehydrogenase (EC 1.2.1.51 (http://ca.expasy.org/cgi-bin/nicezyme.pl?1.2.1.51)) is an allosteric enzyme that transforms pyruvate into acetyl-CoA which is then used in the citric acid cycle.

It is inhibited when either of the three following ratios are increased: [ATP]/[ADP], [NADH]/[NAD+] and [acetyl-CoA]/[CoASH].

Pyruvate dehydrogenase is actually a big complex composed of 60 subunits: 24 pyruvate dehydrogenase (E1), 24 dihydrolipoyl transacetylase (E2) and 12 dihydrolipoyl dehydrogenase (E3).

The global reaction catalysed by pyruvate dehydrogenase is:

pyruvate + CoA + NAD⁺ ⇒ acetyl-CoA + NADH + H⁺ + CO₂

Wikipedia (http://en.wikipedia.org/wiki/Main_Page) Pyruvate_dehydrogenase (http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase) version history (http://en.wikipedia.org/w/index.php?title=Pyruvate_dehydrogenase&action=history) GNU Free Documentation Lizenz (http://en.wikipedia.org/wiki/Wikipedia:Text_of_the_GNU_Free_Documentation_License) CC-by-sa (http://creativecommons.org/licenses/by-sa/2.5/)

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