dihydrolipoamide succinyltransferase homo24mer
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / QuickGO|
- succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine CoA + 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.
- 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. 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.
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