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='48/485632/Cv/1'> | ||
| - | <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=''> | ||
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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> | '''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> | ||
Revision as of 14:52, 29 December 2015
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3D structures of dihydrolipoamide acetyltransferase
Updated on 29-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
