View source for Deacetyl-(citrate-(pro-3S)-lyase) S-acetyltransferase

{{enzyme
| Name = dihydrolipoyllysine-residue succinyltransferase
| EC_number = 2.3.1.61
| CAS_number = 9032-28-4
| IUBMB_EC_number = 2/3/1/61
| GO_code = 0004149
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''dihydrolipoyllysine-residue succinyltransferase''' ({{EC number|2.3.1.61}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:succinyl-CoA + enzyme N<sub>6</sub>-(dihydrolipoyl)lysine <math>\rightleftharpoons</math> CoA + enzyme N<sub>6</sub>-(S-succinyldihydrolipoyl)lysine

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[succinyl-CoA]] and [[enzyme N6-(dihydrolipoyl)lysine]], whereas its two [[product (chemistry)|products]] are [[coenzyme A|CoA]] and [[enzyme N6-(S-succinyldihydrolipoyl)lysine]].

This enzyme belongs to the family of [[transferase]]s, specifically those [[acyltransferase]]s 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 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1BAL}}, {{PDB link|1BBL}}, {{PDB link|1C4T}}, {{PDB link|1E2O}}, {{PDB link|1GHJ}}, {{PDB link|1GHK}}, {{PDB link|1PMR}}, {{PDB link|1SCZ}}, {{PDB link|2BTG}}, {{PDB link|2BTH}}, and {{PDB link|2CYU}}.

==References==
{{reflist|1}}
* {{cite journal | author = Derosier DJ, Oliver RM, Reed LJ | date = 1971 | title = Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex | journal = Proc. Natl. Acad. Sci. U.S.A.  | volume = 68 | pages = 1135&ndash;7  | pmid = 4942179 | doi = 10.1073/pnas.68.6.1135 | issue = 6 | pmc = 389136 }}
* Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 1, Academic Press, New York, 1970, p. 213-240.
* {{cite journal | author = Knapp JE, Mitchell DT, Yazdi MA, Ernst SR, Reed LJ, Hackert ML | date = 1998 | title = Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex | journal = J. Mol. Biol.  | volume = 280 | pages = 655&ndash;68  | pmid = 9677295 | doi = 10.1006/jmbi.1998.1924 | issue = 4 }}
* {{cite journal | author = Perham RN | date = 2000 | title = Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions | journal = Annu. Rev. Biochem.  | volume = 69 | issue = 1 | pages = 961&ndash;1004  | pmid = 10966480 | doi = 10.1146/annurev.biochem.69.1.961 }}

{{transferase-stub}}

[[Category:EC 2.3.1]]
[[Category:Enzymes of known structure]]