Editing Pyruvate dehydrogenase complex (section)

=== Dihydrolipoyl dehydrogenase (E3) ===
[[File:E3 Subunit Putida.png|thumb|Pymol-generated E3 subunit of pyruvate dehydrogenase complex in Pseudomonas putida]]

The E3 subunit, called the [[Dihydrolipoyl dehydrogenase]] enzyme, is characterized as a [[homodimer]] protein wherein two [[cysteine]] residues, engaged in [[disulfide bonding]], and the FAD cofactor in the active site facilitate its main purpose as an oxidizing catalyst. One example of E3 structure, found in ''[[Pseudomonas putida]]'', is formed such that each individual homodimer subunit contains two binding domains responsible for FAD binding and NAD binding, as well as a central domain and an interface domain.<ref>{{cite journal |last1=Billgren |first1=E. S. |last2=Cicchillo |first2=R. M. |last3=Nesbitt |first3=N. M. |last4=Booker |first4=S. J. |title=Lipoic Acid Biosynthesis and Enzymology |journal=Comprehensive Natural Products |date=2010 |volume=2 |issue=7 |pages=181–212 |doi=10.1016/B978-008045382-8.00137-4 }}</ref><ref>[PDB ID: 1LVL] {{cite journal |last1=Mattevia |first1=A. |last2=Obmolova |first2=G. |last3=Sokatch |first3=J. R. |last4=Betzel |first4=C. |last5=Hol |first5=W. G. |title=The refined crystal STRUCTURE of pseudomonas Putida LIPOAMIDE DEHYDROGENASE complexed with NAD+ at 2.45 Å resolution |journal=Proteins: Structure, Function, and Genetics |date=1992 |volume=13 |issue=4 |pages=336–351 |doi=10.1002/prot.340130406|pmid=1325638 |s2cid=23288363 }}</ref>