Dihydrolipoyllysine-residue succinyltransferase

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

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

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.

Transferases: acyltransferases (EC 2.3)

2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase N-Acetylglutamate synthase Choline acetyltransferase Dihydrolipoyl transacetylase Acetyl-CoA C-acyltransferase Beta-galactoside transacetylase Chloramphenicol acetyltransferase N-acetyltransferase Serotonin N-acetyl transferase HGSNAT ARD1A Histone acetyltransferase P300/CBP NAT2 palmitoyltransferases: Carnitine O-palmitoyltransferase CPT1 CPT2 Serine C-palmitoyltransferase SPTLC1 SPTLC2 other: Acyltransferase like 2 Aminolevulinic acid synthase Beta-ketoacyl-ACP synthase Glyceronephosphate O-acyltransferase Lecithin—cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase 2-acylglycerol-3-phosphate O-acyltransferase ABHD5

2.3.2: Aminoacyltransferases	Gamma-glutamyl transpeptidase Peptidyl transferase Transglutaminase Tissue transglutaminase Keratinocyte transglutaminase Factor XIII

2.3.3: converted into alkyl on transfer	Citrate synthase ATP citrate lyase HMG-CoA synthase Malate synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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