The Enzyme Database

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Accepted name: dihydrolipoyllysine-residue succinyltransferase
Reaction: succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
For diagram of the citric-acid cycle, click here and for diagram of oxo-acid dehydrogenase complexes, click here
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; enzyme-dihydrolipoyllysine:succinyl-CoA 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. [DOI] [PMID: 4942179]
2.  Reed, L.J. and Cox, D.J. Multienzyme complexes. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, 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. [DOI] [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. [DOI] [PMID: 10966480]
[EC created 1978, modified 2003]

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