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Information on EC 2.3.1.61 - dihydrolipoyllysine-residue succinyltransferase and Organism(s) Escherichia coli and UniProt Accession P0AFG6

for references in articles please use BRENDA:EC2.3.1.61
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IUBMB Comments
A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalysed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
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This record set is specific for:
Escherichia coli
UNIPROT: P0AFG6
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dihydrolipoamide succinyltransferase, ogdc-e2, dihydrolipoyl succinyltransferase, dihydrolipoamide s-succinyltransferase, dihydrolipoyl transsuccinylase, lipoate succinyltransferase, dihydrolipoyllysine-residue succinyltransferase, lipoyl transsuccinylase, dihydrolipoyl succinyl transferase, e2 component of alpha-ketoglutarate dehydrogenase complex, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydrolipoamide acyltransacetylase
-
dihydrolipoamide succinyltransferase
-
DSCD
catalytic enzyme domain
E2o
component of the 2-oxoglutarate dehydrogenase complex
dihydrolipoamide succinyltransferase
-
-
-
-
dihydrolipoic transsuccinylase
-
-
-
-
dihydrolipolyl transsuccinylase
-
-
-
-
dihydrolipoyl transsuccinylase
-
-
-
-
lipoate succinyltransferase
-
-
-
-
lipoic transsuccinylase
-
-
-
-
lipoyl transsuccinylase
-
-
-
-
succinyl-CoA:dihydrolipoate S-succinyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
oxidative decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-succinyltransferase
A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalysed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-28-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
show the reaction diagram
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
show the reaction diagram
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Lipoyl-protein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
3 * 37000, E2o is normally a 24-mer, found as a trimer, when E2o is expressed with a C-terminal [His]6 tag, SDS-PAGE
1000000
40000
-
24 * 40000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
3 * 37000, E2o is normally a 24-mer, found as a trimer, when E2o is expressed with a C-terminal [His]6 tag, SDS-PAGE
polymer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain, hanging drop vapor diffusion method, using 1 M sodium acetate, 50 mM cadmium sulfate, 50 mM HEPES pH 7.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D374A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 2.1% compared to the wild type enzyme
D374N
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 9.7% compared to the wild type enzyme
D379A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 9.5% compared to the wild type enzyme
H375A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 2fold compared to the wild type enzyme
H375C
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 1% compared to the wild type enzyme
H375G
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 5fold compared to the wild type enzyme
H375N
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 0.5% compared to the wild type enzyme
H375W
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 54fold compared to the wild type enzyme
R376A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 56% compared to the wild type enzyme
T323A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 45% compared to the wild type enzyme
T323S
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 43% compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography
Ni-Sepharose 6 column chromatography and Sephacryl S-300 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) pLysS cells
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reed, L.J.; Cox, D.J.
Multienzyme complexes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
1
213-240
1970
Bos taurus, Escherichia coli, Sus scrofa
-
Manually annotated by BRENDA team
Pettit, F.H.; Hamilton, L.; Munk, P.; Namihira, G.; Eley, M.H.; Willms, C.R.; Reed, L.J.
alpha-Keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex
J. Biol. Chem.
248
5282-5290
1973
Escherichia coli
Manually annotated by BRENDA team
Derosier, D.J.; Oliver, R.M.; Reed, L.J.
Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex
Proc. Natl. Acad. Sci. USA
68
1135-1137
1971
Escherichia coli
Manually annotated by BRENDA team
Angelides, K.J.; Hammes, G.G.
Structural and mechanistic studies of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli
Biochemistry
18
5531-5537
1979
Escherichia coli
Manually annotated by BRENDA team
White, R.H.; Bleile, D.M.; Reed, L.J.
Lipoic acid content of dihydrolipoyl transacylases determined by isotope dilution analysis
Biochem. Biophys. Res. Commun.
94
78-84
1980
Bos taurus, Escherichia coli
Manually annotated by BRENDA team
Robien, M.A.; Clore, G.M.; Omichinski, J.G.; Perham, R.N.; Appella, E.; Sakaguchi, K.; Gronenborn, A.M.
Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli
Biochemistry
31
3463-3471
1992
Escherichia coli
Manually annotated by BRENDA team
Koike, K.; Ishibashi, H.; Koike, M.
Immunoreactivity of porcine heart dihydrolipoamide acetyl- and succinyl-transferases (PDC-E2, OGDC-E2) with primary biliary cirrhosis sera: characterization of the autoantigenic region and effects of enzymic delipoylation and relipoylation
Hepatology
27
1467-1474
1998
Bos taurus, Escherichia coli, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Nguyen, S.V.; To, H.; Yamaguchi, T.; Fukushi, H.; Hirai, K.
Characterization of the Coxiella burnetii sucB gene encoding an immunogenic dihydrolipoamide succinyltransferase
Microbiol. Immunol.
43
743-749
1999
Coxiella burnetii (Q9RH46), Coxiella burnetii, Escherichia coli
Manually annotated by BRENDA team
Knapp, J.E.; Carroll, D.; Lawson, J.E.; Ernst, S.R.; Reed, L.J.; Hackert, M.L.
Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase
Protein Sci.
9
37-48
2000
Azotobacter vinelandii, Corynebacterium glutamicum (Q8NNJ2), Cupriavidus necator, Enterococcus faecalis, Escherichia coli (P0AFG6), Escherichia coli, Geobacillus stearothermophilus, Haemophilus influenzae, Homo sapiens, Pseudomonas aeruginosa, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Koike, K.; Suematsu, T.; Ehara, M.
Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex
Eur. J. Biochem.
267
3005-3016
2000
Azotobacter vinelandii, Bacillus subtilis, Bos taurus, Enterococcus faecalis, Escherichia coli, Homo sapiens, Rattus norvegicus, Saccharomyces cerevisiae, Sus scrofa
Manually annotated by BRENDA team
Zygmunt, M.S.; Diaz, M.A.; Teixeira-Gomes, A.P.; Cloeckaert, A.
Cloning, nucleotide sequence, and expression of the Brucella melitensis sucB gene coding for an immunogenic dihydrolipoamide succinyltransferase homologous protein
Infect. Immun.
69
6537-6540
2001
Brucella abortus, Brucella abortus S19, Brucella anthropi, Brucella melitensis (Q9L6H8), Brucella melitensis, Brucella melitensis 16M (Q9L6H8), Escherichia coli (P0AFG6), Escherichia coli, Phyllobacterium myrsinacearum
Manually annotated by BRENDA team
Andi, B.; Soares, A.S.; Shi, W.; Fuchs, M.R.; McSweeney, S.; Liu, Q.
Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form a tale of a common protein crystallization contaminant
Acta Crystallogr. Sect. F
75
616-624
2019
Escherichia coli (P0AFG6), Escherichia coli
Manually annotated by BRENDA team
Chakraborty, J.; Nemeria, N.S.; Farinas, E.; Jordan, F.
Catalysis of transthiolacylation in the active centers of dihydrolipoamide acyltransacetylase components of 2-oxo acid dehydrogenase complexes
FEBS Open Bio
8
880-896
2018
Escherichia coli (P0AFG6), Escherichia coli
Manually annotated by BRENDA team