Dihydrolipoamide acetyltransferase

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<StructureSection load='3duf' size='350' side='right' caption='Dihydrolipoamide acetyltransferase (wheat, blue) complex with E1 subunit α (grey, pink, magenta, gold) and subunit β (green, yellow, cyan, red) (PDB entry [[3duf]])' scene='48/485632/Cv/1'>
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<StructureSection load='3duf' size='350' side='right' caption='Dihydrolipoamide acetyltransferase (blue) complex with E1 subunit α (pink, gold) and E1 subunit β (cyan, indianred) (PDB entry [[3duf]])' scene='48/485632/Cv/1'>
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'''Dihydrolipoamide acetyltransferase''' (DLAT) or E2 is part of the pyruvate dehydrogenase complex together with pyruvate dehydrogenase (E1) and dihydrolipoyl dehydrogenase (E3). The complex decarboxylates pyruvate thus linking the glycolysis to the citric acid cycle. DLAT catalyzes the transfer of acetyl group to CoA.<ref>PMID:14736882</ref>
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<scene name='48/485632/Cv/2'>Dihydrolipoamide acetyltransferase (DLAT) or E2</scene> is part of the pyruvate dehydrogenase complex together with pyruvate dehydrogenase (E1) and dihydrolipoyl dehydrogenase (E3). The complex decarboxylates pyruvate thus linking the glycolysis to the citric acid cycle. DLAT catalyzes the transfer of acetyl group to CoA.<ref>PMID:14736882</ref>
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== Structural highlights ==
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<scene name='48/485632/Cv/2'>DLAT</scene>. The DLAT structure contains 3 lipoyl domains, a binding domain and a catalytic domain.
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</StructureSection>
</StructureSection>
==3D structures of dihydrolipoamide acetyltransferase==
==3D structures of dihydrolipoamide acetyltransferase==

Revision as of 15:07, 29 December 2015

Dihydrolipoamide acetyltransferase (blue) complex with E1 subunit α (pink, gold) and E1 subunit β (cyan, indianred) (PDB entry 3duf)

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3D structures of dihydrolipoamide acetyltransferase

Updated on 29-December-2015

References

  1. Lai WL, Chou LY, Ting CY, Kirby R, Tsai YC, Wang AH, Liaw SH. The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation. J Biol Chem. 2004 Apr 2;279(14):13962-7. Epub 2004 Jan 21. PMID:14736882 doi:http://dx.doi.org/10.1074/jbc.M308849200

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