Dihydrolipoyl transacetylase

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dihydrolipoamide S-acetyltransferase (E2 component of pyruvate dehydrogenase complex)
Identifiers
Symbol	DLAT
Alt. Symbols	DLTA
Entrez	1737
HUGO	2896
OMIM	608770
RefSeq	NM_001931
UniProt	P10515
Other data
EC number	2.3.1.12
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.

External links

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v • d • e Transferases: acyltransferases (EC 2.3)
2.3.1: other than amino-acyl groups (mostly acetyltransferases)	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