Information on EC 2.3.1.61 - dihydrolipoyllysine-residue succinyltransferase

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

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EC NUMBER
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2.3.1.61
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RECOMMENDED NAME
GeneOntology No.
dihydrolipoyllysine-residue succinyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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oxidative decarboxylation
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-oxoglutarate decarboxylation to succinyl-CoA
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2-oxoglutarate dehydrogenase complex
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Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Citrate cycle (TCA cycle)
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Lysine degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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TCA cycle III (animals)
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citric acid cycle
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vitamin B1 metabolism
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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.
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CAS REGISTRY NUMBER
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9032-28-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
subsp. berkhoffii
SwissProt
Manually annotated by BRENDA team
strain S19
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-
Manually annotated by BRENDA team
strain S19
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-
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
gene zdlst
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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
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Manually annotated by BRENDA team
japanese monkey
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Manually annotated by BRENDA team
wild-type and enzyme deficient mice (DLS+/-, C57BL/6, and 129SV/EV hybrid)
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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dihydrolipoyl succinyltransferase catalyzes the citric acid cycle within the 2-oxoglutarate dehydrogenase complex
physiological function
additional information
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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
succinyl-CoA + dihydrolipoic acid
CoA + succinyldihydrolipoate
show the reaction diagram
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?
succinyl-CoA + dihydrolipoyllysine
CoA + succinyldihydrolipoyllysine
show the reaction diagram
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?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
show the reaction diagram
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?
additional information
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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
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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
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
show the reaction diagram
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?
additional information
?
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Lipoyl-protein
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METALS and IONS
ORGANISM
UNIPROT
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LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme Q0
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
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LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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LITERATURE
IMAGE
4.2
Dihydrolipoamide
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0.06 - 0.1
succinyl-CoA
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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peripheral blood cells
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
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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
40000
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24 * 40000
41000
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24 * 41000, sedimentation equilibrium
41530
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amino acid sequence
48000
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24 * 48000, SDS-PAGE
75000
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12 * 75000, E2, gel filtration, SDS-PAGE
900000
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analytical ultracentrifugation
958000
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analytical ultracentrifugation
992000 - 1027000
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different preparations of the enzyme, analytical ultracentrifugation
1000000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
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12 * 75000, E2, gel filtration, SDS-PAGE
polymer
trimer
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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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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loss of activity is slow up to 70°C, but rapid beyond 75°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilized enzyme loses more than 50% of its original activity
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stable to frequent freezing and thawing
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA encoding porcine E20 cloned, with expression vector pET-11d overexpressed in Escherichia coli
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cDNA identification
cDNA, sequence analysis
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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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expression in Escherichia coli
expression in Escherichia coli as a His-Nus A-tagged fusion protein
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gene zdlst, DNA and amino acid sequence determination and analysis, genetic fine-mapping, and quantitative real-time PCR enzyme expression analysis
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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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subcloning in Escherichia coli strain JM109
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
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ENGINEERING
ORGANISM
UNIPROT
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LITERATURE
D423A
site-directed mutagenesis, the corresponding Km value of the D423A variant is 233% of the wild-type enzyme Km, while the kcat value of the variant is 4% compared to the wild-type enzyme
D423E
site-directed mutagenesis, the corresponding activity of the D423E variant is 30% of the wild-type activity
D423G
site-directed mutagenesis, the corresponding Km value of the D423S variant is 200% of the wild-type enzyme Km
D423S
site-directed mutagenesis, the corresponding Km value of the D423S variant is 161% of the wild-type enzyme Km, while the kcat value of the variant is 9% compared to the wild-type enzyme
H419del
site-directed mutagenesis, the mutant is almost inactive
H419S
site-directed mutagenesis, the mutant shows a the kcat value of 6% compared to the wild-type
D423A
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site-directed mutagenesis, the corresponding Km value of the D423A variant is 233% of the wild-type enzyme Km, while the kcat value of the variant is 4% compared to the wild-type enzyme
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D423E
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site-directed mutagenesis, the corresponding activity of the D423E variant is 30% of the wild-type activity
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D423G
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site-directed mutagenesis, the corresponding Km value of the D423S variant is 200% of the wild-type enzyme Km
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D423S
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site-directed mutagenesis, the corresponding Km value of the D423S variant is 161% of the wild-type enzyme Km, while the kcat value of the variant is 9% compared to the wild-type enzyme
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H419S
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site-directed mutagenesis, the mutant shows a the kcat value of 6% compared to the wild-type
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additional information
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generation of enzyme knockout mutants, the zebrafish mutant schneckentempo, phenotype ste, exhibits bradycardia. The ste mutation is a guanine to adenine nucleotide transition in the splice donor site of intron 5 of the zdlst gene, ENSDARG00000014230
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10% recovery of enzyme activity after renaturation of SDS denatured enzyme (3%)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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the rSucB may be a candidate antigen for a specific serological diagnosis of Bartonella henselae infection
medicine
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.61)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)