Editing Pyruvate dehydrogenase complex (section)

=== Dihydrolipoyl transacetylase (E2) ===
The E2 subunit, or dihydrolipoyl acetyltransferase, for both prokaryotes and eukaryotes, is generally composed of three domains. The N-terminal domain (the lipoyl domain), consists of 1–3 lipoyl groups of approximately 80 amino acids each. The peripheral subunit binding domain (PSBD), serves as a selective binding site for other domains of the E1 and E3 subunits. Finally, the C-terminal (catalytic) domain catalyzes the transfer of acetyl groups and acetyl-CoA synthesis.<ref>{{cite journal |last1=Patel |first1=M. S. |last2=Nemeria |first2=N. S. |last3=Furey |first3=W. |last4=Jordan |first4=F. |title=The pyruvate dehydrogenase complexes: structure-based function and regulation |journal=The Journal of Biological Chemistry |date=2014 |volume=289 |issue=24 |pages=16615–16623 |doi=10.1074/jbc.R114.563148 |pmid=24798336 |pmc=4059105 |doi-access=free }}</ref> In Gammaproteobacteria, 24 copies of E2 form the cubic core of the pyruvate dehydrogenase complex, in which 8 E2 homotrimers are located at the vertices of the cubic core particle.