Dihydrolipoamide acetyltransferase
From Proteopedia
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| - | <StructureSection load='3rnm' size=' | + | <StructureSection load='3rnm' size='350' side='right' caption='Human dihydrolipoamide acetyltransferase binding domain (cyan, green) complex with E3 binding domain (magenta), FAD, CHES and mercaptodthanol (PDB entry [[3rnm]])' scene='48/485632/Cv/3'> |
'''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 15:42, 19 October 2017
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3D structures of dihydrolipoamide acetyltransferase
Updated on 19-October-2017
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
