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Information on EC 2.3.1.61 - dihydrolipoyllysine-residue succinyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q01205

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:
Rattus norvegicus
UNIPROT: Q01205
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The taxonomic range for the selected organisms is: Rattus norvegicus
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 succinyltransferase
dihydrolipoic transsuccinylase
-
-
-
-
dihydrolipolyl transsuccinylase
-
-
-
-
dihydrolipoyl transsuccinylase
-
-
-
-
E2 component of alpha-ketoglutarate dehydrogenase complex
-
-
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 + 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 + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme Q0
-
formation of coenzyme Q0-dihydrolipoamide adducts in the E2 components of the alpha-ketoglutarate complex (i.e. dihydrolipoamide succinyltransferase) partially explains the cellular toxicity of coenzyme Q0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ODO2_RAT
454
0
48925
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
x * 50000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA, sequence analysis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hein, S.; Steinbuechel, A.
Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex
FEMS Microbiol. Lett.
136
231-238
1996
Azotobacter vinelandii (P20708), Bacillus subtilis (P16263), Cupriavidus necator, Rattus norvegicus (Q01205), Saccharomyces cerevisiae (P19262)
Manually annotated by BRENDA team
Matuda, S.; Kodama, J.; Goshi, N.; Takase, C.; Nakano, K.; Nakagawa, S.; Ohta, S.
A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle
Biochem. Biophys. Res. Commun.
241
151-156
1997
Homo sapiens, Rattus norvegicus
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
MacDonald, M.J.; Husain, R.D.; Hoffmann-Benning, S.; Baker, T.R.
Immunochemical identification of coenzyme Q0-dihydrolipoamide adducts in the E2 components of the alpha-ketoglutarate and pyruvate dehydrogenase complexes partially explains the cellular toxicity of coenzyme Q0
J. Biol. Chem.
279
27278-27285
2004
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team