In enzymology, a dihydrolipoyllysine-residue succinyltransferase () is an enzyme that catalyzes the chemical reaction succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine Thus, the two substrates of this enzyme are succinyl-CoA and enzyme N6-(dihydrolipoyl)lysine, whereas its two products are CoA and enzyme N6-(S-succinyldihydrolipoyl)lysine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is succinyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-succinyltransferase. Other names in common use include dihydrolipoamide S-succinyltransferase, dihydrolipoamide succinyltransferase, dihydrolipoic transsuccinylase, dihydrolipolyl transsuccinylase, dihydrolipoyl transsuccinylase, lipoate succinyltransferase (Escherichia coli), lipoic transsuccinylase, lipoyl transsuccinylase, succinyl-CoA:dihydrolipoamide S-succinyltransferase, succinyl-CoA:dihydrolipoate S-succinyltransferase, and enzyme-dihydrolipoyllysine:succinyl-CoA S-succinyltransferase. This enzyme participates in citrate cycle (tca cycle) and lysine degradation. Structural studies As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and . References Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 1, Academic Press, New York, 1970, p. 213-240. EC 2.3.1 Enzymes of known structure