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Information on EC 2.3.1.61 - dihydrolipoyllysine-residue succinyltransferase and Organism(s) Corynebacterium glutamicum and UniProt Accession Q8NNJ2

for references in articles please use BRENDA:EC2.3.1.61
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EC Tree
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:
Corynebacterium glutamicum
UNIPROT: Q8NNJ2
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Word Map
The taxonomic range for the selected organisms is: Corynebacterium glutamicum
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
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dihydrolipoic transsuccinylase
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dihydrolipolyl transsuccinylase
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dihydrolipoyl transsuccinylase
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lipoate succinyltransferase
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lipoic transsuccinylase
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lipoyl transsuccinylase
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succinyl-CoA:dihydrolipoate S-succinyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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oxidative decarboxylation
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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
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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
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-
?
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
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-
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
isolated isoform AceF has solely transacetylase activity and no transsuccinylase activity. Oxoglutarate dehydrogenase complex OdhA specifically converts 2-oxoglutarate to succinyl-coenzyme A but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA. Presence of isoform AceF is required for both oxoglutarate dehydrogenase and pyruvate dehydrogenase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Hoffelder, M.; Raasch, K.; van Ooyen, J.; Eggeling, L.
The E2 domain of OdhA of Corynebacterium glutamicum has succinyltransferase activity dependent on lipoyl residues of the acetyltransferase AceF
J. Bacteriol.
192
5203-5211
2010
Corynebacterium glutamicum (Q8NNJ2)
Manually annotated by BRENDA team