Evans sandbox 1: Difference between revisions

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==Regulation==
==Regulation==
The regulation of E3 kinetically comes through regulation of the entire Pyruvate Dehydrogenase complex.  As would be expected, one of the main regulators is the presence of its product, acetyl-CoA as well as NADH.  NADH competes with NAD+ with the binding site on E3, therefor regulating the entire pyruvate dehydrogenase complex when NADH is in high concentration.‘<ref>Voet, Donald et al. 2008. Fundamentals of Biochemistry. 3rd ed. p.585</ref>’  
The regulation of E3 kinetically comes through regulation of the entire Pyruvate Dehydrogenase complex.  As would be expected, one of the main regulators is the presence of its product, acetyl-CoA as well as NADH.  NADH competes with NAD+ with the binding site on E3, therefore regulating the entire pyruvate dehydrogenase complex when NADH is in high concentration.‘<ref>Voet, Donald et al. 2008. Fundamentals of Biochemistry. 3rd ed. p.585</ref>’  




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Shane Michael Evans