Information on EC 2.3.1.61 - dihydrolipoyllysine-residue succinyltransferase

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

EC NUMBER
COMMENTARY
2.3.1.61
-
RECOMMENDED NAME
GeneOntology No.
dihydrolipoyllysine-residue succinyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
oxidative decarboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
2-oxoglutarate decarboxylation to succinyl-CoA
-
2-oxoglutarate dehydrogenase complex
-
Biosynthesis of secondary metabolites
-
Citrate cycle (TCA cycle)
-
Lysine degradation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dihydrolipoamide succinyltransferase
-
-
-
-
dihydrolipoamide succinyltransferase
-
-
dihydrolipoamide succinyltransferase
Q6FYD4
-
dihydrolipoamide succinyltransferase
Q8GCY1
-
dihydrolipoamide succinyltransferase
-
-
dihydrolipoamide succinyltransferase
-
-
dihydrolipoamide succinyltransferase
-
-
dihydrolipoic transsuccinylase
-
-
-
-
dihydrolipolyl transsuccinylase
-
-
-
-
dihydrolipoyl succinyl transferase
-
-
dihydrolipoyl succinyltransferase
-
-
dihydrolipoyl transsuccinylase
-
-
-
-
DLST
-
-
E2 component of alpha-ketoglutarate dehydrogenase complex
-
-
lipoate succinyltransferase
-
-
-
-
lipoic transsuccinylase
-
-
-
-
lipoyl transsuccinylase
-
-
-
-
OGDC-E2
-
-
succinyl-CoA:dihydrolipoate S-succinyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9032-28-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
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
Brucella melitensis 16M
strain 16M, SwissProt ID Q9L6H8
SwissProt
Manually annotated by BRENDA team
synonym Brevibacterium lactofermentum
UniProt
Manually annotated by BRENDA team
nucleotide sequence deposited in the GenBank and DDBJ
SwissProt
Manually annotated by BRENDA team
H16, wild-type, ATCC 17699
-
-
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
Gluconacetobacter xylinus
-
-
-
Manually annotated by BRENDA team
male transgenic Tg19959 mice (model of amyloid deposition, 2 mutations in the human amyloid precursor protein) are crossed with dihydrolipoyl succinyltransferase deficient female mice (DLST+/-)
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
reduced enzyme activity increases H2O2-induced reactive oxygen species production and cell death, in human Alzheimer disease brains the activity of the alpha-ketoglutarate dehydrogenase enzyme complex is reduced, enzyme deficient mice show increased plaque burden, Abeta oligomers, and nitrotyrosine levels, the occurrence of spatial learning and memory deficits in female Tg19959 mice is accelerated
malfunction
-
enzyme deficient mice show reduced mRNA and protein levels and decreased brain mitochondrial alpha-ketoglutarate dehydrogenase activity (by about 40%), increased vulnerability to mitochondrial toxins: MPTP treatment enhances the severity of lipid peroxidation in the substantial nigra, reduced striatal dopamine (59% depletion in wild-type, 73% in enzyme deficient mutants), dopaminergic neurons (25% reduction in wild-type, 42% in mutants) and tyrosine hydroxylase-positive neurons, striatal lesions induced by malonate (mimicking Huntington's disease, 2fold larger lesions, smaller striatum) or 3-nitropropionic acid (5fold larger lesions than in wild-type) are significantly larger in enzyme deficient mice than in the wild-type, and the 3-nitropropionic acid-induced mitochondrial enzyme inhibition (25% lower citrate synthase activity than in wild-type), protein and DNA oxidation is enhanced in the cortex of enzyme deficient mice compared to wild-type
physiological function
-
key subunit of the alpha-ketoglutarate dehydrogenase enzyme complex, involved in NADH production, participation in oxidative stress and reactive oxygen species (ROS) production
physiological function
-
subunit of the alpha-ketoglutarate dehydrogenase complex
physiological function
Q8NNJ2
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
Gluconacetobacter xylinus
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
P20708
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
P16263
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-, Q9L6H8
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-, Q9L6H8
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
Q8NNJ2
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-, Q9RH46
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-, Q9RH46
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
P0AFG6
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
Q01205
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
P19262
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
Brucella melitensis 16M
Q9L6H8
-
-
?
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
Gluconacetobacter xylinus
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
P20708
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
P16263
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-, Q9L6H8
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
Q8NNJ2
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-, Q9RH46
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
P0AFG6
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
Q01205
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
P19262
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
-
plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
show the reaction diagram
Brucella melitensis 16M
Q9L6H8
-
-
-
?
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Lipoyl-protein
-
transsuccinylase core consists of 24 similar polypeptide chains, 12 of these chains contain a covalently bound lipoyl moiety
Lipoyl-protein
-
-
Lipoyl-protein
-
enzyme contains 8 mol of protein-bound lipoic acid per mol of enzyme
Lipoyl-protein
-
contains 1 lipoyl moiety per chain
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.2
-
Dihydrolipoamide
-
-
0.06
-
succinyl-CoA
-
-
0.1
-
succinyl-CoA
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
at pH 7.2
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
peripheral blood cells
Manually annotated by BRENDA team
-
the DLST gene has two gene-products, one of which, gene product MIRTD, mediates the molecular assembly of the cytochrome c oxidase complex whose defect has been a candidate of the causes of Alzheimers disease. Since levels of MIRTD mRNA in the brains of Alzheimers disease patients are significantly low, a decrease in MIRTD could affect energy production
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
41530
-
-
amino acid sequence
45000
-
-, Q9L6H8
SDS-PAGE
50000
-
-, Q9RH46
SDS-PAGE
900000
-
Gluconacetobacter xylinus
-
analytical ultracentrifugation
958000
-
-
analytical ultracentrifugation
992000
1027000
-
different preparations of the enzyme, analytical ultracentrifugation
1000000
-
-
sucrose density gradient centrifugation, sedimentation equilibrium
1000000
-
-
sedimentation equlibrium
1000000
-
-
-
1000000
-
-
gel filtration, FPLC
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 50000, SDS-PAGE
dodecamer
Gluconacetobacter xylinus
-
12 * 75000, E2, gel filtration, SDS-PAGE
polymer
-
consists of 8 morphological subunits arranged in a cube-like structure
polymer
-
24 * 39000-42000, sedimentation equilibrium analysis; 24 * 47000-51000, SDS-PAGE; made up of 24 similar structurally identical polypeptide chains
polymer
-
24 * 41000, sedimentation equilibrium; 24 * 48000, SDS-PAGE
polymer
-
24 * 40000
polymer
-
made up of 24 similar structurally identical polypeptide chains
polymer
-
multienzyme complex contains 24 copies of the E20 subunit as an octahedral core that forms a truncated cube
polymer
-
-
polymer
-
24 * 48000, SDS-PAGE
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
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
-
-
loss of activity is slow up to 70°C, but rapid beyond 75°C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
lyophilized enzyme loses more than 50% of its original activity
-
stable to frequent freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Gluconacetobacter xylinus
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recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli as a His-Nus A-tagged fusion protein
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expression in Escherichia coli
-, Q6FYD4
expression in Escherichia coli
-, Q8GCY1
cDNA identification
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sucB gene encoding E2o cloned, sequenced and expressed in Escherichia coli
-, Q9L6H8
sucB gene cloned by immunological screening of a lambda EMBL3 genomic library from strain Nine Mile DNA, expressed in Escherichia coli
-, Q9RH46
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
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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
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cDNA, sequence analysis
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cDNA encoding porcine E20 cloned, with expression vector pET-11d overexpressed in Escherichia coli
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cDNA identification
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Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
10% recovery of enzyme activity after renaturation of SDS denatured enzyme (3%)
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diagnostics
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the rSucB may be a candidate antigen for a specific serological diagnosis of Bartonella henselae infection
medicine
-, Q6FYD4
mounting of an anti-SucB response floows infection. Antibodies against Coxiella burnetti, Franciscella tularensis, and Rickettsia typhi also react with recombinant Bartonella SucB. Potential SuV antigenic cross-reactivity presents a challenge to the development of serodiagnostic tests for other intracellular pathogens that cause diseases such as Q fever, rickettsioses, brucelloses, tularemia, and other bartelloses
medicine
-, Q8GCY1
mounting of an anti-SucB response floows infection. Antibodies against Coxiella burnetti, Franciscella tularensis, and Rickettsia typhi also react with recombinant Bartonella SucB. Potential SuV antigenic cross-reactivity presents a challenge to the development of serodiagnostic tests for other intracellular pathogens that cause diseases such as Q fever, rickettsioses, brucelloses, tularemia, and other bartelloses
medicine
-, Q9L6H8
most pathogenic species for human
medicine
Brucella melitensis 16M
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most pathogenic species for human
-
medicine
-, Q9RH46
enzyme may serve as a potential target antigen for diagnostic assays for Q fever
medicine
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possible relationship between enzyme and familial Alzheimer's disease is discussed
medicine
-
-
medicine
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the DLST gene has two gene-products, one of which, gene product MIRTD, mediates the molecular assembly of the cytochrome c oxidase complex whose defect has been a candidate of the causes of Alzheimers disease. Since levels of MIRTD mRNA in the brains of Alzheimers disease patients are significantly low, a decrease in MIRTD could affect energy production