dihydrolipoamide S-acetyltransferase (E2 component of pyruvate dehydrogenase complex)
|Locus||Chr. 11 q23.1|
Dihydrolipoyl transacetylase (or dihydrolipoamide acetyltransferase) is the structural and catalytic core of the multienzyme pyruvate dehydrogenase complex, playing a crucial role in the architecture of the complex. All dihydrolipoyl transacetylases have a unique multidomain structure consisting of (from N to C); 3 lipoyl domains; and interaction domain; and the catalytic domain (see the domain architecture at Pfam). Interestingly all the domains are connected by disordered, low complexity linker regions.
The catalytic domains are assembled into trimers, and in some organisms eight trimers are arranged into a hollow truncated cube. The active site is located in the subunit interface.
Transferases: acyltransferases (EC 2.3)
|2.3.1: other than amino-acyl groups|
|N-Acetylglutamate synthase - Choline acetyltransferase - Acetyl-Coenzyme A acetyltransferase - Dihydrolipoyl transacetylase - Acetyl-CoA C-acyltransferase - Beta-galactoside transacetylase - Carnitine O-palmitoyltransferase (CPT1, CPT2) - Acyltransferase like 2 - Chloramphenicol acetyltransferase - Aminolevulinic acid synthase - Beta-ketoacyl-ACP synthase - Glyceronephosphate O-acyltransferase - Lecithin-cholesterol acyltransferase - Histone acetyltransferase (P300/CBP) - Serotonin N-acetyl transferase|
|2.3.2 - Aminoacyltransferases||Gamma glutamyl transpeptidase - Peptidyl transferase - Transglutaminase (Tissue transglutaminase, Keratinocyte transglutaminase, Factor XIII)|
|2.3.3 - converted into alkyl on transfer||Citrate synthase - ATP citrate lyase - HMG-CoA synthase|
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