In enzymology, a dihydrolipoyllysine-residue succinyltransferase (EC 2.3.1.61) is an enzyme that catalyzes the chemical reaction
| dihydrolipoyllysine-residue succinyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 dihydrolipoamide succinyltransferase homo24mer | |||||||||
| Identifiers | |||||||||
| EC no. | 2.3.1.61 | ||||||||
| CAS no. | 9032-28-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- 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
editAs of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1BAL, 1BBL, 1C4T, 1E2O, 1GHJ, 1GHK, 1PMR, 1SCZ, 2BTG, 2BTH, and 2CYU.
References
edit- Derosier DJ, Oliver RM, Reed LJ (1971). "Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex". Proc. Natl. Acad. Sci. U.S.A. 68 (6): 1135–7. Bibcode:1971PNAS...68.1135D. doi:10.1073/pnas.68.6.1135. PMC 389136. PMID 4942179.
- Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 1, Academic Press, New York, 1970, p. 213-240.
- Knapp JE, Mitchell DT, Yazdi MA, Ernst SR, Reed LJ, Hackert ML (1998). "Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex". J. Mol. Biol. 280 (4): 655–68. doi:10.1006/jmbi.1998.1924. PMID 9677295.
- Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annu. Rev. Biochem. 69 (1): 961–1004. doi:10.1146/annurev.biochem.69.1.961. PMID 10966480.
