Dihydrolipoamide dehydrogenase
From Proteopedia
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The regulation of Dihidrolipoamide dehydrogenase (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. This is through the E1 reaction of the complex, but necessarily effects the E3 reaction. However, the E1 portion of the complex is also regulated by phosphatase and kinase in phosphorylation and dephosphorylation reactions.‘<ref>Voet, Donald et al. 2008. Fundamentals of Biochemistry. 3rd ed. p.585</ref>’ | The regulation of Dihidrolipoamide dehydrogenase (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. This is through the E1 reaction of the complex, but necessarily effects the E3 reaction. However, the E1 portion of the complex is also regulated by phosphatase and kinase in phosphorylation and dephosphorylation reactions.‘<ref>Voet, Donald et al. 2008. Fundamentals of Biochemistry. 3rd ed. p.585</ref>’ | ||
- | </StructureSection> | ||
==3D structures of dihydrolipoamide dehydrogenase== | ==3D structures of dihydrolipoamide dehydrogenase== | ||
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**[[1zmc]], [[1zmd]] – hDLD + NAD<br /> | **[[1zmc]], [[1zmd]] – hDLD + NAD<br /> | ||
**[[6i4q]] – hDLD + FAD <br /> | **[[6i4q]] – hDLD + FAD <br /> | ||
- | **[[5j5z]], [[6hg8]], [[6i4p]], [[6i4r]], [[6i4s]], [[6i4t]], [[6i4u]], [[6i4z]] – hDLD (mutant) + FAD <br /> | + | **[[5j5z]], [[6hg8]], [[6i4p]], [[6i4r]], [[6i4s]], [[6i4t]], [[6i4u]], [[6i4z]], [[7psc]], [[7zyt]] – hDLD (mutant) + FAD <br /> |
**[[2ii3]], [[2ii4]], [[2ii5]] – bDLD + CoA<br /> | **[[2ii3]], [[2ii4]], [[2ii5]] – bDLD + CoA<br /> | ||
**[[1v59]] – yDLD + NAD<br /> | **[[1v59]] – yDLD + NAD<br /> | ||
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**[[6awa]] - PpDLD + FAD + AMP<br /> | **[[6awa]] - PpDLD + FAD + AMP<br /> | ||
**[[3ii4]] – MtDLD + inhibitor <br /> | **[[3ii4]] – MtDLD + inhibitor <br /> | ||
- | **[[4m52]] – MtDLD + sulfonamide inhibitor<br /> | + | **[[4m52]], [[8u0q]] – MtDLD + FAD + sulfonamide inhibitor<br /> |
+ | **[[8ct4]] – MtDLD + FAD + sulfonamide inhibitor – Cryo EM<br /> | ||
**[[7kmy]] – MtDLD + FAD + pyridine inhibitor<br /> | **[[7kmy]] – MtDLD + FAD + pyridine inhibitor<br /> | ||
**[[1ebd]] – DLD + dihydrolipoamide acetyltransferase binding domain – ''Geobacillus stearothermophilus''<br /> | **[[1ebd]] – DLD + dihydrolipoamide acetyltransferase binding domain – ''Geobacillus stearothermophilus''<br /> | ||
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**[[6uzi]] – DLD + FAD – ''Elizabethkingia anophelis<''br /> | **[[6uzi]] – DLD + FAD – ''Elizabethkingia anophelis<''br /> | ||
**[[6bz0]] – DLD + FAD – ''Acinetobacter baumannii''<br /> | **[[6bz0]] – DLD + FAD – ''Acinetobacter baumannii''<br /> | ||
+ | **[[8ajj]] – DLD + FAD – ''Staphylococcus aureus<''br /> | ||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
- | + | </StructureSection> | |
[[Category:Topic Page]] | [[Category:Topic Page]] |
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Michal Harel, Nicholas Rockefeller, Alexander Berchansky, David Canner, Shane Michael Evans, Jaime Prilusky