Dihydrolipoamide acetyltransferase
From Proteopedia
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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=''> | |
| - | <StructureSection load='3duf' size='350' side='right' caption='Dihydrolipoamide acetyltransferase complex with E1 (PDB entry [[3duf]])' scene=''> | + | |
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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> The DLAT structure contains 3 lipoyl domains, a binding domain and a catalytic domain. | + | '''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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| + | == Structural highlights == | ||
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| + | The DLAT structure contains 3 lipoyl domains, a binding domain and a catalytic domain. | ||
</StructureSection> | </StructureSection> | ||
==3D structures of dihydrolipoamide acetyltransferase== | ==3D structures of dihydrolipoamide acetyltransferase== | ||
Revision as of 12:05, 24 December 2015
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3D structures of dihydrolipoamide acetyltransferase
Updated on 24-December-2015
References
- ↑ 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
