Dihydrolipoyllysine-residue succinyltransferase

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
dihydrolipoyllysine-residue succinyltransferase
1e2o.jpg
dihydrolipoamide succinyltransferase homo24mer
Identifiers
EC number2.3.1.61
CAS number9032-28-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a dihydrolipoyllysine-residue succinyltransferase (EC 2.3.1.61) 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[edit]

As 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&ndash, 7. 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&ndash, 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&ndash, 1004. doi:10.1146/annurev.biochem.69.1.961. PMID 10966480.