IUBMB Enzyme Nomenclature


Accepted name: dihydrolipoyllysine-residue succinyltransferase

Reaction: succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine

For diagram of reaction click here (mechanism).

Glossary: dihydrolipoyl group

Other name(s): 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

Systematic name: succinyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-succinyltransferase

Comments: A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC, oxoglutarate dehydrogenase (succinyl-transferring) and EC, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively succinylated by EC, and the only observed direction catalysed by EC is that where this succinyl group is passed to coenzyme A.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-28-4


1. Derosier, D.J., Oliver, R.M. and Reed, L.J. Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex. Proc. Natl. Acad. Sci. USA 68 (1971) 1135-1137. [PMID: 4942179]

2. Reed, L.J. and Cox, D.J. Multienzyme complexes. In: Boyer, P.D. (Ed.), The Enzymes 3rd ed., vol. 1, Academic Press, New York, 1970, pp. 213-240.

3. Knapp, J.E., Mitchell, D.T., Yazdi, M.A., Ernst, S.R., Reed, L.J. and Hackert, M.L. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 280 (1998) 655-668. [PMID: 9677295]

4. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]

[EC created 1978, modified 2003]

Return to EC 2.3.1 home page
Return to EC 2.3 home page
Return to EC 2 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page