Information on EC 2.3.1.61 - dihydrolipoyllysine-residue succinyltransferase

New: Word Map on EC 2.3.1.61
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.3.1.61
-
RECOMMENDED NAME
GeneOntology No.
dihydrolipoyllysine-residue succinyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
oxidative decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-oxoglutarate decarboxylation to succinyl-CoA
-
-
2-oxoglutarate dehydrogenase complex
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Citrate cycle (TCA cycle)
-
-
citric acid cycle
-
-
Lysine degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
TCA cycle III (animals)
-
-
vitamin B1 metabolism
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
subsp. berkhoffii
SwissProt
Manually annotated by BRENDA team
strain S19
-
-
Manually annotated by BRENDA team
strain S19
-
-
Manually annotated by BRENDA team
strain 16M, SwissProt ID Q9L6H8
SwissProt
Manually annotated by BRENDA team
strain 16M, SwissProt ID Q9L6H8
SwissProt
Manually annotated by BRENDA team
nucleotide sequence deposited in the GenBank and DDBJ
SwissProt
Manually annotated by BRENDA team
enzyme is present at higher levels in ascites-resistant line broilers with ascites than in ascites resistant line broilers without ascites or ascites-susceptible line broilers with or without ascites
-
-
Manually annotated by BRENDA team
japanese monkey
-
-
Manually annotated by BRENDA team
wild-type and enzyme deficient mice (DLS+/-, C57BL/6, and 129SV/EV hybrid)
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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 + dihydrolipoic acid
CoA + succinyldihydrolipoate
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoyllysine
CoA + succinyldihydrolipoyllysine
show the reaction diagram
-
-
-
?
additional information
?
-
-
the DLST gene is bifunctionally involved in mitochondrial energy metabolism, the full-length DLST protein is involved in the Krebs cycle and the truncated version, MIRTD, contributes to the biogenesis of the respiratory chain. The genotype of the DLST gene is associated with Alztheimer‘s disease without a change of amino acid residues in the DLST protein: through a decrease in the expression of the truncated gene product MIRTD and the function of MIRTD. It remains unclear how much MIRTD actually contributes to the pathogenesis of Alzheimer‘s disease
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
additional information
?
-
-
the DLST gene is bifunctionally involved in mitochondrial energy metabolism, the full-length DLST protein is involved in the Krebs cycle and the truncated version, MIRTD, contributes to the biogenesis of the respiratory chain. The genotype of the DLST gene is associated with Alztheimer‘s disease without a change of amino acid residues in the DLST protein: through a decrease in the expression of the truncated gene product MIRTD and the function of MIRTD. It remains unclear how much MIRTD actually contributes to the pathogenesis of Alzheimer‘s disease
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Lipoyl-protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme Q0
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.2
Dihydrolipoamide
-
-
0.06 - 0.1
succinyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
at pH 7.2
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
peripheral blood cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41530
-
amino acid sequence
900000
-
analytical ultracentrifugation
958000
-
analytical ultracentrifugation
992000 - 1027000
-
different preparations of the enzyme, analytical ultracentrifugation
1000000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
-
12 * 75000, E2, gel filtration, SDS-PAGE
polymer
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
loss of activity is slow up to 70°C, but rapid beyond 75°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilized enzyme loses more than 50% of its original activity
-
stable to frequent freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 0.05 M potassium phosphate buffer, pH 7.0, containing 0.05 mM EDTA, stable for over 6 months without significant loss of activity, despite frequent freezing and thawing
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA encoding porcine E20 cloned, with expression vector pET-11d overexpressed in Escherichia coli
-
cDNA identification
cDNA, sequence analysis
-
cloning of the whole 2-oxoglutarase dehydrogenase complex structural genes, heterologous expression in Escherichia coli XL1-Blue and in the kgdA mutant Pseudomonas putida JS 347
-
expression in Escherichia coli
expression in Escherichia coli as a His-Nus A-tagged fusion protein
-
isolation of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex from a human genomic DNA library, cloning vector lambda EMBL3 subcloned into plasmid vector pUC18, gene is located on chromosome 14 at q24.2-q24.3, pseudogene is located on chromosome at p31
-
sucB gene cloned by immunological screening of a lambda EMBL3 genomic library from strain Nine Mile DNA, expressed in Escherichia coli
sucB gene encoding E2o cloned, sequenced and expressed in Escherichia coli
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10% recovery of enzyme activity after renaturation of SDS denatured enzyme (3%)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
the rSucB may be a candidate antigen for a specific serological diagnosis of Bartonella henselae infection
medicine
Show AA Sequence (5795 entries)
Longer loading times are possible. Please use the Sequence Search for a certain query.