Information on EC 6.2.1.5 - Succinate-CoA ligase (ADP-forming)

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

EC NUMBER
COMMENTARY
6.2.1.5
-
RECOMMENDED NAME
GeneOntology No.
Succinate-CoA ligase (ADP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
show the reaction diagram
reaction mechanism, Glu435 is a key active site residue, overview. Class I CoA-transferases first bind the acyl-CoA substrate, forming a carboxylate product and an enzyme-CoA thioester intermediate, which accounts for the observed ping-pong kinetics and susceptibility to borohydride inactivation
B3EY95
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
anaerobic energy metabolism (invertebrates, mitochondrial)
-
Biosynthesis of antibiotics
-
Biosynthesis of secondary metabolites
-
C5-Branched dibasic acid metabolism
-
Carbon fixation pathways in prokaryotes
-
Citrate cycle (TCA cycle)
-
citric acid cycle
BRENDA
BRENDA
BRENDA
incomplete reductive TCA cycle
-
Metabolic pathways
-
methylaspartate cycle
-
Microbial metabolism in diverse environments
-
Propanoate metabolism
-
pyruvate fermentation to acetate V
-
pyruvate fermentation to acetate VI
-
reductive TCA cycle I
-
reductive TCA cycle II
-
TCA cycle I (prokaryotic)
-
TCA cycle II (plants and fungi)
-
TCA cycle III (animals)
-
TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
-
TCA cycle VI (obligate autotrophs)
-
SYSTEMATIC NAME
IUBMB Comments
Succinate:CoA ligase (ADP-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A-SCS
-
-
-
-
A-SCS
-
-
A-STK
-
-
-
-
A-SUCL
P53597, Q9P2R7
-
AarC
B3EY95
-
ADP-forming succinyl-CoA synthase
-
-
ADP-forming succinyl-CoA synthetase
-
-
ADP-forming SUCL
P53597, Q9P2R7
-
ATP-specific succinate:CoA ligase
-
-
ATP-specific SUCL
-
-
SCACT
B3EY95
-
SCS-alpha
-
-
-
-
SCS-beta
-
-
-
-
SCS-betaA
-
-
-
-
ScsB
Q1KSE5
-
STK
-
-
-
-
SucCD
W0PAN5, W0PFR9
-
SucCD
W0PAN5, W0PFR9
-
-
SucCD
Q0VPF7, Q0VPF8
-
SucCD
Q0VPF7, Q0VPF8
-
-
SucCD
P0A836, P0AGE9
-
SucCD
Escherichia coli K-12 BL21
P0A836, P0AGE9
-
-
SucCDAm
B3TZD8, B3TZD9
gene name
succinate coenzyme A ligase
W0PAN5, W0PFR9
-
succinate coenzyme A ligase
W0PAN5, W0PFR9
-
-
succinate coenzyme A ligase
Q0VPF7, Q0VPF8
-
succinate coenzyme A ligase
Q0VPF7, Q0VPF8
-
-
succinate coenzyme A ligase
P0A836, P0AGE9
-
succinate coenzyme A ligase
Escherichia coli K-12 BL21
P0A836, P0AGE9
-
-
Succinate thiokinase
-
-
-
-
succinate-CoA ligase
W0PAN5, W0PFR9
-
succinate-CoA ligase
W0PAN5, W0PFR9
-
-
succinate-CoA ligase
Q0VPF7, Q0VPF8
-
succinate-CoA ligase
Q0VPF7, Q0VPF8
-
-
succinate-CoA ligase
P0A836, P0AGE9
-
succinate-CoA ligase
Escherichia coli K-12 BL21
P0A836, P0AGE9
-
-
succinate-CoA ligase
-
-
Succinic thiokinase
-
-
-
-
Succinyl coenzyme A synthetase
-
-
-
-
Succinyl coenzyme A synthetase
B3TZD8, B3TZD9
-
Succinyl coenzyme A synthetase (adenosine diphosphate-forming)
-
-
-
-
succinyl-CoA synthase
-
-
Succinyl-CoA synthetase
-
-
-
-
Succinyl-CoA synthetase
B3TZD8, B3TZD9
-
Succinyl-CoA synthetase
-
-
Succinyl-CoA synthetase
-
-
Succinyl-CoA synthetase
-
-
Succinyl-CoA synthetase
Q9P2R7
-
Succinyl-CoA synthetase
Q7Z941
-
Succinyl-CoA synthetase
-
-
Succinyl-CoA synthetase
-
-
Succinyl-CoA synthetase
Q1KSE5
-
Succinyl-CoA synthetase (ADP-forming)
-
-
-
-
succinyl-CoA-synthetase (ATP)
Q1KSE5
-
succinyl-CoA:acetate CoA-transferase
B3EY95
-
succinyl-coenzyme A:acetate CoA-transferase
B3EY95
-
SUCL
-
-
SUCLA2
Q9P2R7
-
Synthetase, succinyl coenzyme A (adenosine diphosphate-forming)
-
-
-
-
Tneu_1463
B1Y9F9 and B1Y9G0
locus name of subunit beta
Tneu_1463
Pyrobaculum neutrophilum DSDM 2338
B1Y9F9 and B1Y9G0
locus name of subunit beta
-
Tneu_1464
B1Y9F9 and B1Y9G0
locus name of subunit alpha
Tneu_1464
Pyrobaculum neutrophilum DSDM 2338
B1Y9F9 and B1Y9G0
locus name of subunit alpha
-
VEG239
-
-
-
-
VEG63
-
-
-
-
Vegetative protein 239
-
-
-
-
Vegetative protein 63
-
-
-
-
additional information
B3EY95
AarC is predicted to be a class I CoAtransferase
CAS REGISTRY NUMBER
COMMENTARY
9080-33-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strains 1023 and DSM 2002, aarABC region, gene aarC
UniProt
Manually annotated by BRENDA team
alpha-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
beta-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
subunit alpha; i.e. Tetrathiobacter mimigardefordensis, gene SucCDAm
UniProt
Manually annotated by BRENDA team
subunit beta; i.e. Tetrathiobacter mimigardefordensis, gene SucCDAm
UniProt
Manually annotated by BRENDA team
alpha-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
beta-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
alpha-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
beta-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
alpha-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
beta-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
human isolate, strain DMP/02-328, ATCC 50177
-
-
Manually annotated by BRENDA team
blowfly
-
-
Manually annotated by BRENDA team
gene CG11963
-
-
Manually annotated by BRENDA team
His246alpha to Asp mutant
-
-
Manually annotated by BRENDA team
mutant W76F and W43,76,248F and wild type
-
-
Manually annotated by BRENDA team
wild type and Cys325Glu mutant
-
-
Manually annotated by BRENDA team
wild type and mutant H142N
-
-
Manually annotated by BRENDA team
alpha-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
beta-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
Escherichia coli K-12 BL21
alpha-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
Escherichia coli K-12 BL21
beta-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
alpha-subunit
SwissProt
Manually annotated by BRENDA team
beta-subunit
UniProt
Manually annotated by BRENDA team
gene SUCLA1 encodes the alpha-subunit and gene SUCLA2 encodes the catalytic beta-subunit
-
-
Manually annotated by BRENDA team
gene SUCLG2
-
-
Manually annotated by BRENDA team
strain ATCC 25978
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
enzyme forms a complex with nucleoside-diphosphate kinase
-
-
Manually annotated by BRENDA team
B1Y9F9: subunit beta, B1Y9G0: subunit alpha
B1Y9F9 and B1Y9G0
UniProt
Manually annotated by BRENDA team
Pyrobaculum neutrophilum DSDM 2338
B1Y9F9: subunit beta, B1Y9G0: subunit alpha
B1Y9F9 and B1Y9G0
UniProt
Manually annotated by BRENDA team
strain DSM639
-
-
Manually annotated by BRENDA team
strain AT-62
-
-
Manually annotated by BRENDA team
Thermus thermophilus AT-62
strain AT-62
-
-
Manually annotated by BRENDA team
gene scsB
UniProt
Manually annotated by BRENDA team
additional information
organisms with a very high Km-value for ADP and a low Km value for GDP are listed at EC 6.2.1.4
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
malate-CoA ligases and succinate-CoA ligases might have the same evolutionary origin
evolution
Escherichia coli K-12 BL21
-
malate-CoA ligases and succinate-CoA ligases might have the same evolutionary origin
-
malfunction
-
knockdown of SUCLG2 by shRNA in both SUCLA2-related mitochondrial DNA depletion syndrome patient and control fibroblasts results in a significant decrease in mtDNA amount, decreased NDPK and cytochrome c oxidase activities, and a marked growth impairment, phenotype, overview
malfunction
-
in patients with enzyme mutations, muscle histology shows severe lipid accumulation, and a marked type I fibre predominance is found, with an increased variability in fibre diameter. mtDNA depletion in succinate-CoA ligase deficiency
malfunction
-
inhibition of the enzyme might influence the activity of nucleoside diphosphate kinase inducing an imbalance of nucleotides in the mitochondria and eventually mitochondrial DNA depletion. This may account for the potential liver failure associated with valproate therapy, reported in patients with deficiencies within the mitochondrial DNA replicase system such as polymerase gamma 1
physiological function
-
SUCLG2, to a higher degree than SUCLA2, EC 6.2.1.4, is crucial for mtDNA maintenance involving mitochondrial NDPK
physiological function
-
probable role of an aminolevulinic acid synthase ALAS2-succinyl-CoA synthetase complex in the regulation of erythroid heme biosynthesis
physiological function
-
the enzme is bound to the nucleoside diphosphate kinase, which is responsible for the mitochondrial (deoxy)nucleotide synthesis
physiological function
B1Y9F9 and B1Y9G0
the enzyjme is involved in autotrophic CO2 fixation
physiological function
Pyrobaculum neutrophilum DSDM 2338
-
the enzyjme is involved in autotrophic CO2 fixation
-
metabolism
-
key role of the enzyme in the Krebs cycle
additional information
-
the GDP-dependent isozyme SUCLG2 can complement the SUCLA2-related mitochondrial DNA depletion syndrome, a result of mutations in the beta subunit of the ADP-dependent isoform SUCLA2, EC 6.2.1.4
additional information
-
C-terminal mutations in the erythroid-specific aminolevulinic acid synthase gene ALAS2 cause loss of binding to the beta-subunit of succinyl-CoA synthetase, SUCLA2, resulting in reduced mitochondrial enzymatic activity and X-linked sideroblastic anemia
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
-
-
-
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
generation of ATP is critical for the beta-cell mitochondrial metabolism
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
the enzyme carries out the substrate-level phosphorylation in the citric acid cycle
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
the enzyme carries out the substrate-level phosphorylation in the citric acid cycle
-
?
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
-
-
-
-
-
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
-
the enzyme plays an essential role in the citric acid cycle, where the conversion of succinyl-CoA into succinate represents an important site of substrate level phosphorylation
-
-
-
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
-
catalyzes the formation of ATP via substrate-level phosphorylation
-
-
-
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
Escherichia coli K12
-
the enzyme plays an essential role in the citric acid cycle, where the conversion of succinyl-CoA into succinate represents an important site of substrate level phosphorylation
-
-
-
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
show the reaction diagram
P0A836, P0AGE9
-
-
-
r
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
show the reaction diagram
-, W0PAN5, W0PFR9
-
-
-
r
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
show the reaction diagram
B3TZD8, B3TZD9
SucCDAm is unspecific regarding ATP or GTP
determination of 3-sulfinopropionyl-CoA structure by using liquid chromatography-electrospray ionization-mass spectrometry
-
?
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
show the reaction diagram
W0PAN5, W0PFR9
-
-
-
r
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
show the reaction diagram
Escherichia coli K-12 BL21
P0A836, P0AGE9
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
B3EY95
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
Blastocystis succinyl-CoA synthetase is a tricarboxylic acid cycle enzyme that conserves energy by substrate-level phosphorylation. In the absence of a classic mitochondrial electron transport chain, it is likely to be one of the main ATP producing enzymes in this parasite
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
Blastocystis SCS is ATP-specific, while both ATP and GTP fit into the Blastocystis SCS active site, GTP is destabilizes by electrostatic dipole interactions with Lys42 and Lys110, the side-chains of which lie outside the nucleotide-binding cavity, an electrostatic gatekeeper controls which ligands can enter the binding site, overview
three reaction steps in the reverse direction: 1. formation of a non-covalent enzyme-succinyl-phosphate complex and cocomitant release of CoA, 2. formation of a covalent phosphoryl-enzyme intermediate with the release of succinate, and 3. phosphorylation of ADP forming ATP
-
r
ATP + adipate + CoA
ADP + phosphate + adipyl-CoA
show the reaction diagram
-
59% activity compared to succinate
-
-
r
ATP + ATP
adenosine 5'-tetraphosphate + ADP
show the reaction diagram
-
-
-
-
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
-
48% activity compared to succinate
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
show the reaction diagram
P0A836, P0AGE9
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
show the reaction diagram
-, W0PAN5, W0PFR9
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
show the reaction diagram
W0PAN5, W0PFR9
-
-
-
r
ATP + glutarate + CoA
ADP + phosphate + glutaryl-CoA
show the reaction diagram
-
121% activity compared to succinate
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
P0A836, P0AGE9
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-, W0PAN5, W0PFR9
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
B3TZD8, B3TZD9
SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
W0PAN5, W0PFR9
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
Escherichia coli K-12 BL21
P0A836, P0AGE9
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
show the reaction diagram
P0A836, P0AGE9
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
show the reaction diagram
-, W0PAN5, W0PFR9
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + oxalate + CoA
ADP + phosphate + oxalyl-CoA
show the reaction diagram
-
9% activity compared to succinate
-
-
r
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
-
10% activity compared to succinate
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, P53597, Q9P2R7
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Pigeon
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Q7Z940, Q7Z941
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Q1KSE5
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
B3EY95
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, P53597, Q9P2R7
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, W0PAN5, W0PFR9
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
r
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
enzyme has a low Km value for ADP and for GDP
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
specific for ATP
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
specific for ATP
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
specific for ATP
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
specific for succinate
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
specific for succinate
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
during the reaction a His residue at the alpha-subunit is transiently phosphorylated. Glu208alpha and Glu197beta, are crucial for phosphorylation and dephosphorylation of the active-site His
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
B3EY95
AarC is succinyl-CoA:acetate CoA-transferase, which replaces succinyl-CoA synthetase in a variant CAC, this new bypass appears to reduce metabolic demand for free CoA, reliance upon nucleotide pools, and the likely effect of variable cytoplasmic pH upon CAC flux, the enzyme is required for the citric acid cycle, overview
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, P53597, Q9P2R7
the enzyme is part of the Krebs cycle
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
B3TZD8, B3TZD9
SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
B3TZD8, B3TZD9
succinate is the best substrate, SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
P0A836, P0AGE9
ATP is the preferred cosubstrate
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
no activity with GTP/GDP
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Thermus thermophilus AT-62
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
W0PAN5, W0PFR9
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Pseudomonas aeruginosa 8822
-
-
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Escherichia coli K12
-
r
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Escherichia coli K-12 BL21
P0A836, P0AGE9
ATP is the preferred cosubstrate
-
-
r
ATP + succinate + CoA
?
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
generation of succinyl-CoA from succinate for anabolic purposes when the route from 2-oxoglutarate is repressed, e.g. under anaerobic conditions
-
-
-
beta,gamma-Methylene adenosine triphosphate
Corresponding tetraphosphate + ?
show the reaction diagram
-
-
alpha,gamma-methylene adenosine tetraphosphate
-
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
P0A836, P0AGE9
-
-
-
r
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
Escherichia coli K-12 BL21
P0A836, P0AGE9
-
-
-
r
GTP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
GTP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
-
GTP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
enzyme has a low Km value for ADP and for GDP
-
-
-
GTP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
enzyme has no activity with GTP
-
-
-
UTP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
GTP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
no activity with GDP/GTP
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
catalyzes ATP-diphosphate exchange only when all the reactants necessary to establish the overall reaction are present
-
-
-
additional information
?
-
-
succinate-stimulated and CoA-stimulated ATP-diphosphate exchange is observed with ATP, GTP, UTP, ITP and CTP, enzyme has succinyl-CoA stimulated nucleoside diphosphate kinase activity
-
-
-
additional information
?
-
-
diglyceride kinase can use either ATP or the phosphorylated form of succinyl CoA synthetase as phosphate donor for the phosphorylation of diglyceride
-
-
-
additional information
?
-
-
enzyme is involved in the initial step of porphyrin biosynthesis
-
-
-
additional information
?
-
-
deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion
-
-
-
additional information
?
-
-
a Drosophila orthologue of succinyl-CoA synthetase beta-subunit is a modulator of Drosophila KCNQ channels responsible for slowly activating potassium currents in heart, brain, and other tissues, direct interaction with the intracellular C-terminal tail KCNQ channel, overview
-
-
-
additional information
?
-
-, P53597, Q9P2R7
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
-
-
-
additional information
?
-
-
the enzyme beta-subunit binds strongly to wild-type erythroid-specific aminolevulinic acid synthase, but not to the mutants M567V and S568G, aminolevulinic acid synthase mutant R452C shows binding to the succinyl-CoA synthetase, but with reduced affinity and positive cooperativity for succinyl-CoA
-
-
-
additional information
?
-
-, W0PAN5, W0PFR9
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, 3-sulfinopropionate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
-
additional information
?
-
-, Q0VPF7, Q0VPF8
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
-
additional information
?
-
P0A836, P0AGE9
the enzyme is able to use ATP as well as GTP as a cosubstrate, cf. EC 6.2.1.4, substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
-
additional information
?
-
P0A836, P0AGE9
the enzyme is able to use ATP as well as GTP as a cosubstrate, cf. EC 6.2.1.4. substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
-
additional information
?
-
-, Q0VPF7, Q0VPF8
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
-
additional information
?
-
W0PAN5, W0PFR9
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, 3-sulfinopropionate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
-
additional information
?
-
Escherichia coli K-12 BL21
P0A836, P0AGE9
the enzyme is able to use ATP as well as GTP as a cosubstrate, cf. EC 6.2.1.4. substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
-
additional information
?
-
Escherichia coli K-12 BL21
P0A836, P0AGE9
the enzyme is able to use ATP as well as GTP as a cosubstrate, cf. EC 6.2.1.4, substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
-
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
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
generation of ATP is critical for the beta-cell mitochondrial metabolism
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
the enzyme carries out the substrate-level phosphorylation in the citric acid cycle
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
the enzyme carries out the substrate-level phosphorylation in the citric acid cycle
-
?
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
-
-
-
-
-
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
-
the enzyme plays an essential role in the citric acid cycle, where the conversion of succinyl-CoA into succinate represents an important site of substrate level phosphorylation
-
-
-
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
-
catalyzes the formation of ATP via substrate-level phosphorylation
-
-
-
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
Escherichia coli K12
-
the enzyme plays an essential role in the citric acid cycle, where the conversion of succinyl-CoA into succinate represents an important site of substrate level phosphorylation
-
-
-
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
Blastocystis succinyl-CoA synthetase is a tricarboxylic acid cycle enzyme that conserves energy by substrate-level phosphorylation. In the absence of a classic mitochondrial electron transport chain, it is likely to be one of the main ATP producing enzymes in this parasite
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
P0A836, P0AGE9
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-, W0PAN5, W0PFR9
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
W0PAN5, W0PFR9
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
Escherichia coli K-12 BL21
P0A836, P0AGE9
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Q1KSE5
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, P53597, Q9P2R7
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, W0PAN5, W0PFR9
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
B3EY95
AarC is succinyl-CoA:acetate CoA-transferase, which replaces succinyl-CoA synthetase in a variant CAC, this new bypass appears to reduce metabolic demand for free CoA, reliance upon nucleotide pools, and the likely effect of variable cytoplasmic pH upon CAC flux, the enzyme is required for the citric acid cycle, overview
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, P53597, Q9P2R7
the enzyme is part of the Krebs cycle
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
B3TZD8, B3TZD9
SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
P0A836, P0AGE9
ATP is the preferred cosubstrate
-
-
r
ATP + succinate + CoA
?
show the reaction diagram
-
generation of succinyl-CoA from succinate for anabolic purposes when the route from 2-oxoglutarate is repressed, e.g. under anaerobic conditions
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-, Q0VPF7, Q0VPF8
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
W0PAN5, W0PFR9
-
-
-
r
ATP + succinate + CoA
?
show the reaction diagram
Escherichia coli K12
-
generation of succinyl-CoA from succinate for anabolic purposes when the route from 2-oxoglutarate is repressed, e.g. under anaerobic conditions
-
-
-
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Escherichia coli K-12 BL21
P0A836, P0AGE9
ATP is the preferred cosubstrate
-
-
r
additional information
?
-
-
diglyceride kinase can use either ATP or the phosphorylated form of succinyl CoA synthetase as phosphate donor for the phosphorylation of diglyceride
-
-
-
additional information
?
-
-
enzyme is involved in the initial step of porphyrin biosynthesis
-
-
-
additional information
?
-
-
deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion
-
-
-
additional information
?
-
-
a Drosophila orthologue of succinyl-CoA synthetase beta-subunit is a modulator of Drosophila KCNQ channels responsible for slowly activating potassium currents in heart, brain, and other tissues, direct interaction with the intracellular C-terminal tail KCNQ channel, overview
-
-
-
additional information
?
-
-, P53597, Q9P2R7
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
-
-
-
additional information
?
-
-
the enzyme beta-subunit binds strongly to wild-type erythroid-specific aminolevulinic acid synthase, but not to the mutants M567V and S568G, aminolevulinic acid synthase mutant R452C shows binding to the succinyl-CoA synthetase, but with reduced affinity and positive cooperativity for succinyl-CoA
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-, P53597
;
ADP
-, Q0VPF7, Q0VPF8
;
ADP
P0A836, P0AGE9
;
ATP
-
specific for, while both ATP and GTP fit into the Blastocystis SCS active site, GTP is destabilized by electrostatic dipole interactions with Lys42 and Lys110, the side-chains of which lie outside the nucleotide-binding cavity, flexible docking and molecular dynamics simulations, overview
ATP
B3TZD8, B3TZD9
SucCDAm is unspecific regarding ATP or GTP; SucCDAm is unspecific regarding ATP or GTP
ATP
-, Q0VPF7, Q0VPF8
;
ATP
P0A836, P0AGE9
;
GDP
P0A836, P0AGE9
;
GTP
P0A836, P0AGE9
;
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
required, the true substrate is the MgADP-complex
Mg2+
-
required for activity
Mg2+
Q1KSE5
-
Mg2+
B3EY95
-
Mg2+
-, P53597
-
Mg2+
B3TZD8, B3TZD9
SucCDAm is Mg2+- or Mn2+-dependent; SucCDAm is Mg2+- or Mn2+-dependent
Mg2+
-
absolute requirement for either Mg2+ or Mn2+, optimal concentration of Mg2+ is 5 mM; Km: 1.5 mM, soluble enzyme
Mg2+
-
Km: 3.5 mM
Mg2+
-
Km: 0.1 mM, immobilized enzyme
Mg2+
-
1-100 mM activates
Mn2+
-
can replace Mg2+ as a cofactor
Mn2+
B3TZD8, B3TZD9
SucCDAm is Mg2+- or Mn2+-dependent; SucCDAm is Mg2+- or Mn2+-dependent
Mn2+
-
absolute requirement for either Mg2+ or Mn2+, Km: 3.5 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
no inhibition
2-oxoglutarate
-
no inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
acetate
-
-
ADP
-
adenosine 5-tetraphosphate formation
ATP
-
above 10 mM
Borohydride
B3EY95
inactivation, in the presence of acetyl-CoA causes near-complete loss of enzyme activity consistent with the reduction of the glutamyl-CoA thioester intermediate to 5-hydroxynorvaline, in absence of acetyl-CoA only partial inactivation, 71% activity relative to a control, occurs
Butyrate
-
-
Ca2+
-
10 mM, 75% inhibition
Co2+
-
up to 1 mM complete inhibition
CoA plus succinate
-
presence of succinate plus CoA inhibits adenosine 5'-tetraphosphate formation
-
Cu2+
-
up to 10 mM complete inhibition
cystine
-
-
Hg2+
-
up to 1 mM complete inhibition
iodoacetamide
-
-
Iodosobenzoate
-
-
malonate
-
-
Pb2+
-
up to 10 mM complete inhibibition
Propionate
-
-
protoporphyrin IX
-
-
Sodium arsenite
-
-
succinate
-
above 0.2 M
succinate
-
presence of succinate plus CoA inhibits adenosine 5'-tetraphosphate formation
valproyl-CoA
-
45-55% inhibition at 1 mM
zinc chloride
-
-
Zn2+
-
up to 1 mM complete inhibition
MnO4-
-
significant protection is obtained by: 1. MgATP2- and succinate, 51% 2. desulfo-CoA alone, 53% 3. MgATP2-, succinate, desulfo-CoA, 93%
additional information
-
no inhibition by valproic acid
-
additional information
-
mechanism of regulation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8-hydroxyquinoline
-
5 mM, enhances activity
glutathione
-
activates
NaCN
-
10 mM , enhances activity
phosphate
-
binds the porcine heart SCS alpha-subunit in a noncovalent manner and enhances its enzymatic activity. The ability of SCS alpha-subunit to retain its phosphate in SDS-PAGE is unique over the entire mitochondrial proteome. Phosphate in millimolar concentrations induces activation of SCS by more than 2fold
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
2
3-sulfinopropionate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
2.964
-
3-sulfinopropionate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
70
-
acetate
B3EY95
pH 8.0, 25C
0.0223
-
acetyl-CoA
B3EY95
pH 8.0, 25C
0.0077
-
ADP
-
at 55C
0.12
-
ADP
-
-
0.25
-
ADP
-
pH 8.0, 30C
0.0145
-
ATP
-
adenosine 5-tetraphosphate formation
0.017
-
ATP
-
-
0.041
-
ATP
-
pH 7.4, 22C, mutant enzyme E208alphaQ
0.055
-
ATP
-
pH 8.0, 30C
0.055
-
ATP
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.07
-
ATP
-
wild type enzyme, apparent value
0.08
-
ATP
-
immobilized enzyme
0.083
-
ATP
B3TZD8, B3TZD9
pH 7.4, 30C, recombinant sucCD; pH 7.4, 30C, recombinant sucCD
0.09
-
ATP
-
mutant enzyme C123ALPHAV, apparent value
0.1
-
ATP
-
mutant enzyme C123ALPHAS, apparent value; mutant enzyme C123ALPHAT, apparent value
0.106
-
ATP
-
pH 7.4, 22C, mutant enzyme E197betaQ
0.116
-
ATP
-
pH 7.4, 22C, mutant enzyme E208alphaD
0.137
-
ATP
-
pH 7.4, 22C, mutant enzyme E197betaD
0.18
-
ATP
-
mutant enzyme C123ALPHAA, apparent value
0.201
-
ATP
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.241
-
ATP
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.29
-
ATP
-
-
1.6
-
ATP
-
soluble enzyme
1.6
-
ATP
-
succinate
0.0013
-
CoA
-
pH 7.4, 22C, mutant enzyme E208alphaQ
0.0018
-
CoA
-
pH 7.4, 22C, mutant enzyme E197betaQ
0.002
-
CoA
-
pH 7.4, 22C, mutant enzyme E208alphaD
0.0027
-
CoA
-
pH 7.4, 22C, mutant enzyme E197betaD
0.004
-
CoA
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.032
-
CoA
-
pH 8.0, 30C
0.037
-
CoA
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.045
-
CoA
B3TZD8, B3TZD9
pH 7.4, 30C, recombinant sucCD; pH 7.4, 30C, recombinant sucCD
0.056
-
CoA
-
-
0.058
-
CoA
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
4
-
CoA
-
wild type enzyme, apparent value
11
-
CoA
-
mutant enzyme C123ALPHAS, apparent value
17
-
CoA
-
mutant enzyme C123ALPHAA, apparent value
20
-
CoA
-
mutant enzyme C123ALPHAV, apparent value
29
-
CoA
-
mutant enzyme C123ALPHAT, apparent value
0.01
-
coenzyme A
-
-
3.588
-
D-malate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
3.635
-
D-malate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
4.243
-
D-malate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.011
-
GTP
-
pH 7.4, 22C, mutant enzyme E208alphaQ
0.02
-
GTP
-
pH 7.4, 22C, mutant enzyme E197betaQ
0.063
-
GTP
-
pH 7.4, 22C, mutant enzyme E208alphaD
0.311
-
GTP
-
pH 7.4, 22C, mutant enzyme E197betaD
0.351
-
Itaconate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.448
-
Itaconate
B3TZD8, B3TZD9
pH 7.4, 30C, recombinant sucCD; pH 7.4, 30C, recombinant sucCD
0.475
-
Itaconate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.818
-
Itaconate
B3TZD8, B3TZD9
pH 7.4, 30C, recombinant sucCD; pH 7.4, 30C, recombinant sucCD
1.509
-
Itaconate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
2.558
-
L-Malate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
3.095
-
L-Malate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.72
-
phosphate
-
pH 8.0, 30C
1.4
-
phosphate
-
at 55C
0.141
-
succinate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.143
-
succinate
B3TZD8, B3TZD9
pH 7.4, 30C, recombinant sucCD; pH 7.4, 30C, recombinant sucCD
0.157
-
succinate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.182
-
succinate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.25
-
succinate
-
wild type enzyme, apparent value
0.26
-
succinate
-
pH 7.4, 22C, mutant enzyme E208alphaD
0.27
-
succinate
-
pH 7.4, 22C, mutant enzyme E208alphaQ
0.4
-
succinate
-
pH 7.4, 22C, mutant enzyme E197betaQ
0.71
-
succinate
-
mutant enzyme C123ALPHAA, apparent value
0.8
-
succinate
-
mutant enzyme C123ALPHAS, apparent value
0.87
-
succinate
-
pH 7.4, 22C, mutant enzyme E197betaD
0.9
-
succinate
B3EY95
pH 8.0, 25C
1.3
-
succinate
-
mutant enzyme C123ALPHAV, apparent value
1.5
-
succinate
-
-
2.8
-
succinate
-
at 55C
3.3
-
succinate
-
mutant enzyme C123ALPHAT, apparent value
5
-
succinate
-
immobilized enzyme
5
-
succinate
-
succinate
5.1
-
succinate
-
pH 8.0, 30C
14
-
succinate
-
soluble enzyme
0.0221
-
succinyl-CoA
B3EY95
pH 8.0, 25C
0.024
-
succinyl-CoA
-
-
0.041
-
succinyl-CoA
-
pH 8.0, 30C
3.27
-
L-Malate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
additional information
-
additional information
B3EY95
kinetic analysis, parameters at different conditions, overview
-
additional information
-
additional information
Pigeon
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.2
-
3-sulfinopropionate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.2
-
3-sulfinopropionate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
280
-
acetate
B3EY95
pH 8.0, 25C
75.2
-
acetyl-CoA
B3EY95
pH 8.0, 25C
0.57
-
ATP
-
pH 7.4, 22C, mutant enzyme E208alphaQ
0.85
-
ATP
-
pH 7.4, 22C, mutant enzyme E197betaQ
3.6
-
ATP
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
6.08
-
ATP
-
pH 7.4, 22C, mutant enzyme E208alphaQ
19.6
-
ATP
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
58.8
-
ATP
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1775
-
ATP
-
pH 7.4, 22C, mutant enzyme E197betaD
1780
-
ATP
-
pH 7.4, 22C, mutant enzyme E197betaD
2340
-
ATP
-
pH 7.4, 22C, mutant enzyme E208alphaD
2343
-
ATP
-
pH 7.4, 22C, mutant enzyme E208alphaD
1.6
-
CoA
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
26.7
-
CoA
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
40.3
-
CoA
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1.2
-
D-malate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1.7
-
D-malate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
2.1
-
D-malate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
0.21
-
GTP
-
pH 7.4, 22C, mutant enzyme E197betaQ
0.28
-
GTP
-
pH 7.4, 22C, mutant enzyme E208alphaQ
302
-
GTP
-
pH 7.4, 22C, mutant enzyme E208alphaD
1775
-
GTP
-
pH 7.4, 22C, mutant enzyme E197betaD
1780
-
GTP
-
pH 7.4, 22C, mutant enzyme E197betaD
0.5
-
Itaconate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1.5
-
Itaconate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
5.3
-
Itaconate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1.1
-
L-Malate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1.8
-
L-Malate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
20
-
phosphate
-
at 55C
0.3
-
succinate
-
mutant enzyme C123ALPHAA, apparent value
2.7
-
succinate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
14.3
-
succinate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
15.3
-
succinate
-
mutant enzyme C123ALPHAV, apparent value
29
-
succinate
-
at 55C
29.25
-
succinate
-
mutant enzyme C123ALPHAS, apparent value
31
-
succinate
-
mutant enzyme C123ALPHAT, apparent value
31.1
-
succinate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
35.38
-
succinate
-
mutant enzyme C123ALPHAA, apparent value
44.73
-
succinate
-
wild type enzyme, apparent value
70.9
-
succinate
B3EY95
pH 8.0, 25C
201
-
succinyl-CoA
B3EY95
pH 8.0, 25C
2.6
-
L-Malate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
3-sulfinopropionate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
85598
1
-
3-sulfinopropionate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
85598
14.8
-
ATP
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
4
292.5
-
ATP
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
4
354.4
-
ATP
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
4
372.3
-
CoA
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
18
461.3
-
CoA
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
18
1100
-
CoA
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
18
0.3
-
D-malate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1139
0.4
-
D-malate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1139
0.6
-
D-malate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1139
3.1
-
Itaconate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1978
3.3
-
Itaconate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1978
15.1
-
Itaconate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
1978
0.3
-
L-Malate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
247
0.7
-
L-Malate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
247
0.8
-
L-Malate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
247
17.2
-
succinate
-, Q0VPF7, Q0VPF8
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
58
101.4
-
succinate
P0A836, P0AGE9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
58
171.1
-
succinate
-, W0PAN5, W0PFR9
recombinant enzyme, pH 7.4, 30C; recombinant enzyme, pH 7.4, 30C
58
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.053
-
B3EY95
strain 2002, reverse reaction
0.083
-
B3EY95
strain 1023, reverse reaction
0.1
-
Pigeon
-
-
0.114
-
B3EY95
strain 2002, forward reaction
0.17
-
B3EY95
strain 1023, forward reaction
0.18
-
-
cell extract
1
2
-, W0PAN5, W0PFR9
purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation; purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation
4.14
-
-, Q0VPF7, Q0VPF8
purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation; purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation
6.61
-
-
-
10
-
-
-
18.6
-
P0A836, P0AGE9
purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation; purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation
39.4
-
-
after 221fold purification
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8
-
immobilized enzyme
7.4
-
-
assay at
7.4
-
-
assay at; assay at
7.4
-
-, Q0VPF7, Q0VPF8
assay at; assay at
7.4
-
P0A836, P0AGE9
assay at; assay at
7.9
8.3
-
-
8
-
B3EY95
assay at
8
-
-
free enzyme
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9.6
-
6.0: about 50% of maximal activity, 9.5: about 30% of maximal activity
7
9
-
about 50% of maximal activity at pH 7.0 and pH 9.0
7.1
9
-
pH 7.1: about 75% of maximal activity, pH 9.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
B3EY95
assay at
30
-
-
assay at
30
-
B3TZD8, B3TZD9
assay at; assay at
30
-
-, W0PAN5, W0PFR9
assay at; assay at
30
-
-, Q0VPF7, Q0VPF8
assay at; assay at
30
-
P0A836, P0AGE9
assay at; assay at
32
40
-
immobilized enzyme
35
-
-
free enzyme
38
-
-
-
65
-
B1Y9F9 and B1Y9G0
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
60
-
about 50% of maximal activity at 15C and 60C
25
45
-
about 50% of maximal activity at 25C and 45C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.9
-
-
isoelectric focusing
8.47
-
-
beta-subunit, sequence calculation
8.7
-
Q7Z940, Q7Z941
subunit beta, theoretical value
9.34
-
-
alpha-subunit, sequence calculation
9.6
-
Q7Z940, Q7Z941
subunit alpha, theoretical value
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Pigeon
-
-
Manually annotated by BRENDA team
Pyrobaculum neutrophilum DSDM 2338
-
-
-
Manually annotated by BRENDA team
Pyrobaculum neutrophilum DSDM 2338
-
-
-
Manually annotated by BRENDA team
Pyrobaculum neutrophilum DSDM 2338
-
-
-
Manually annotated by BRENDA team
Pyrobaculum neutrophilum DSDM 2338
-
-
-
Manually annotated by BRENDA team
Pyrobaculum neutrophilum DSDM 2338
-
-
-
Manually annotated by BRENDA team
-
low activity, muscle
Manually annotated by BRENDA team
Pigeon
-
-
Manually annotated by BRENDA team
-
two distinct ATP-specific and GTP-specific succinyl-CoA synthetases
Manually annotated by BRENDA team
-
two distinct ATP-specific and GTP-specific succinyl-CoA synthetases
Manually annotated by BRENDA team
Pigeon
-
-
Manually annotated by BRENDA team
Pigeon
-
-
Manually annotated by BRENDA team
additional information
Q1KSE5
quantitative expression analysis in in tachyzoites and in vitro bradyzoites, overview
Manually annotated by BRENDA team
additional information
-, P53597
the enzyme is preferably expressed in catabolic tissues
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
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)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27000
-
-
SDS-PAGE, beta subunit
35000
-
-
alpha-subunit, SDS-PAGE
35500
-
Q7Z940, Q7Z941
subunit alpha, theoretical value
47100
-
Q7Z940, Q7Z941
subunit beta, theoretical value
50000
-
-
SDS-PAGE, alpha subunit
68000
-
-
gel filtration
75000
-
-
gel filtration
80000
100000
Pigeon
-
-
130000
-
-
gel filtration
136000
-
-
gel filtration
141000
-
-
tertameric form, sedimentation equilibrium measurement
150000
-
-
about, gel filtration
160000
-
-
circa 160000 Da, gel filtration
160000
-
-
gel filtration
170000
-
-
gel filtration
171000
-
-
gel filtration
184000
-
-
gel filtration
330000
-
-
native gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Pigeon
-
x * 40000 + x * 48000
?
-
x * 31000 (alpha) + x * 41000 (beta), SDS-PAGE
?
-
x * 29644 (alpha) + x * 41390 (beta), calculation from nucleotide sequence
?
-
alphaxbetay, x * 35000 + y * 42500, ATP-specific succinyl-CoA synthetase and GTP-specific succinyl-CoA synthetase incorporate the same alpha-subunit, SDS-PAGE
?
B3EY95
x * 55846, recombinant enzyme, x * 55832, recombinant, borohydride-treated enzyme
?
Escherichia coli K12
-
x * 31000 (alpha) + x * 41000 (beta), SDS-PAGE
-
dimer
-
1 * 29600 (alpha) + 1 * 38700 (beta), at concentrations above 1 mg/ml the enzyme exists predominantly as an alpha2beta2 tetramer, at lower concentrations, a significant fraction of the enzyme dissociates to an alphabeta dimer, SDS-PAGE
dimer
-
2 * 32500, alphabeta, SDS-PAGE, 1 * 33400, alpha-subunit, + 1 * 45100, beta-subunit, sequence calculation
heterodimer
-
the enzyme is composed of an alpha subunit, encoded by SUCLG1, and a beta subunit, encoded by either SUCLA2 or SUCLG2. The alpha-subunit forms a heterodimer with either of its beta-subunits, resulting in an ADP-forming succinate-CoA ligase, EC 6.2.1.5, and a GDP-forming succinate-CoA ligase, EC 6.2.1.4, respectively
tetramer
-
2 * 29600 (alpha) + 2 * 38700 (beta), at concentrations above 1 mg/ml the enzyme exists predominantly as an alpha2beta2 tetramer, at lower concentrations, a significant fraction of the enzyme dissociates to an alphabeta dimer, SDS-PAGE
tetramer
-
alpha2beta2
tetramer
-
2 * 29000 (alpha) + 2 * 36000 (beta), SDS-PAGE
tetramer
-
2 * alpha + 2 * beta. The dimerization of the alphabeta-dimer is not a prerequisite for catalytic competency nor for alternating sites cooperativity in the tetramer
heterotetramer
-
2 * 50000 + 2 * 27000, gel filtration
additional information
-
homology modelling using pig SCS, PDB code 2fp4, induced-fit docking calculations and molecular dynamics simulations, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
the alpha-subunit of succinyl-CoA synthetase undergoes autophosphorylation at a histidine residue. Coprovision of exogenous succinate and CoA results in pronounced dephosphorylation of the phosphorylated alpha-subunit of succinyl-CoA synthetase
phosphoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by X-ray crystallography
-
detailed structural description
-
wild-type and mutant enzyme E197betaA, hanging drop vapour diffusion method
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
10
-
50C, 30 min stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
5 min, stable
40
-
-
5 min, about 20% loss of activity
40
-
-
5 min, stable
50
-
-
5 min, stable
50
-
-
pH 8.0-10.0, 30 min, stable
60
-
-
5 min, complete loss of activity
60
-
-
5 min, stable
70
-
-
pH 7.5, half-life: 60 min
80
-
-
5 min, about 10% loss of activity
90
-
-
5 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP or phosphate protects against trypsin inactivation
-
mutant W76F and mutant W43,76,248F are more sensitive to proteolysis by clostripain than the wild type enzyme or other Trp mutant proteins. ADP and ATP both protect the enzyme against inactivation by clostripain. Mutagenic replacement of Argbeta80, but not Argbeta14, with Lys results in an enzyme that is resistant to clostripain as wild type enzyme
-
phosphorylation of 1 active site histidine residue per oligomeric enzyme molecule results in a significant change in the three-dimensional structure of the enzyme to a tighter conformation, with concomittant stability
-
25% loss of activity after 3 months at 4C, immobilized enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable for several months in the frozen state
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli by ammonium sulfate fractionation and metal affinity chromatography
B3EY95
recombinant enzyme 1.07fold from Escherichia coli strain BL21(DE3)-pLysS by two different steps of anion exchange chromatography and affinity chromatography; recombinant enzyme 1.07fold from Escherichia coli strain BL21(DE3)-pLysS by two different steps of anion exchange chromatography and affinity chromatography
-, W0PAN5, W0PFR9
recombinant soluble enzyme from Escherichia coli strain BL21(DE3)/pLysS by anion exchange chromatography; recombinant soluble enzyme from Escherichia coli strain BL21(DE3)/pLysS by anion exchange chromatography
B3TZD8, B3TZD9
recombinant C-terminally His-tagged enzyme 1.55fold from Escherichia coli strain BL21(DE3)-pLysS by nickel affinity chromatography; recombinant C-terminally His-tagged enzyme 1.55fold from Escherichia coli strain BL21(DE3)-pLysS by nickel affinity chromatography
-, Q0VPF7, Q0VPF8
recombinant His-tagged proteins from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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recombinant enzyme 1.47fold from Escherichia coli strain BL21(DE3)-pLysS by anion exchange and affinity chromatography; recombinant enzyme 1.47fold from Escherichia coli strain BL21(DE3)-pLysS by anion exchange and affinity chromatography
P0A836, P0AGE9
recombinant maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, from Escherichia coli strain Top10 by amylose affinity chromatography and gel filtration
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-
Pigeon
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B1Y9F9 and B1Y9G0
Dyematrex Blue A column chromatography and DE-52 cellulose chromatography
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Resource Q column chromatography, Resource ISO column chromatography, and Superdex 200 HR 10/30 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene aarC, DNA and amino acid sequence determination and analysis, expression analysis, overexpression as soluble His6-tagged enzyme in Escherichia coli
B3EY95
gene sucCD, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)/pLysS; gene sucCD, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)/pLysS
B3TZD8, B3TZD9
gene sucCD, expression in Escherichia coli strain BL21(DE3)-pLysS; gene sucCD, expression in Escherichia coli strain BL21(DE3)-pLysS
-, W0PAN5, W0PFR9
gene sucCD, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)-pLysS; gene sucCD, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)-pLysS
-, Q0VPF7, Q0VPF8
alpha and beta subunits, expression of His-tagged proteins in Escherichia coli strain BL21(DE3), phylogenetic analysis of SCS subunits
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gene CG11963, expression as GST-tagged enzyme in Escherichia coli strain BL21(DE3), interaction analysis of Myc-tagged CG11963 and FLAG-tagged dKCNQ using the yeast two-hybrid system
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gene sucCD, expression in Escherichia coli strain BL21(DE3)-pLysS; gene sucCD, expression in Escherichia coli strain BL21(DE3)-pLysS
P0A836, P0AGE9
expression of the maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, in Escherichia coli strain Top10
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gene SUCLG2, DNA and amino acid sequence determination and analysis, semi quantitative RT-PCR expression analysis
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beta-subunit
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expression in Escherichia coli
B1Y9F9 and B1Y9G0
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
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expression in Escherichia coli
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gene scsB, DNA and amino acid sequence determination and analysis, quantitative expression analysis in in tachyzoites and in vitro bradyzoites, overview
Q1KSE5
isolation and amino terminal sequencing of 3 alpha-SCS proteins
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EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
approximately 10fold downregulated in presence of acetate, 4-hydroxybutyrate, succinate or pyruvate
B1Y9F9 and B1Y9G0
approximately 10fold downregulated in presence of acetate, 4-hydroxybutyrate, succinate or pyruvate
Pyrobaculum neutrophilum DSDM 2338
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C123ALPHAA
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lower catalytic efficiency compared to the wild type enzyme
C123ALPHAS
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lower catalytic efficiency compared to the wild type enzyme
C123ALPHAT
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lower catalytic efficiency compared to the wild type enzyme
C123ALPHAV
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lower catalytic efficiency compared to the wild type enzyme
C325E
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Cys325Glu mutant is 83% as active as the wild type enzyme. The mutant enzyme is refractory to chemical modification by CoA disulfide-S,S-dioxide and methyl methane thiosulfonate. It is less reactive with NEM
E197betaA
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mutant enzyme with very low activity. The mutant protein is crystallized in the same space group as the wild-type enzyme. Crystals of the mutant enzyme grew as plates rather than as cubes which are the usual crystal habit for the wild-type enzyme
E197betaD
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the Km-values and turnover numbers are comparable to those of the wild-type enzyme
E197betaQ
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the KM-value for each substrate is comparable to that of the wild-type enzyme, except for GTP, whose Km-value is reduced by a factor of 20. 3000fold decrease in turnover number for reaction with ATP, 7000fold decrease in turnover-number when using GTP
E208alphaD
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Km-values for succinate, CoA, GTP and ATP are comparable to those observed with wild-type enzyme. The turnover-numbers for ATP and GTP are comparable to the wild-type value
E208alphaQ
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Km-values for succinate, CoA and ATP are comparable to those observed with wild-type enzyme. The KM-value for GTP is 36times lower than that of the wild-type enzyme. The turnover-numbers for ATP and GTP are reduced approximately 5000fold compared to the wild-type enzyme
E231betaA
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
E231betaW
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strong decrease in activity
E231betaW/Q247betaW/E249betaW
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strong decrease in activity
E29betaD/E33betaA/S36betaA
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activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
E33betaA/S36betaA
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activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
E33betaA/S36betaA/K66betaA
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activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
E4betaK/R14betaD//R70betaG/E231betaW/Q247betaW/E24
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strong decrease in activity
E74betaK
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
H246D
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His246alpha to Asp mutant is indistinguishable from the native enzyme with respect to its subunit assembly, but has no ability to catalyze the overall reaction. The mutant enzyme is incapable of undergoing phosphorylation and is devoid of arsenolysis activity
K66betaA
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activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
M156betaD/Y1258betaD/R161betaE/E162betaR
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mutant enzyme with alphabeta-dimer subunit structure
N142N
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mutant H142N is devoid of the ability to catalyze the overall reaction but is able to catalyze the half-reactions at significant rates. Phosphorylation by ATP and dephosphorylation by ADP of the mutant enzyme occurs at rates that are at least 10times greater than those with wild type enzyme. Dephosphorylation by succinate plus CoA, succinyl-CoA formation, proceeds with a maximal velocity of 10% that of wild type enzyme
Q247betaK
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD/E231betA
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD/R70betaG/E74betaK
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD/R70betaG/E74betaK/E231betaA/Q247betaK
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R29betaA/E33betaA/S36betaA/K66betaA
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strong decrease in activity
R29betaD
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activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
R70betaG
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R70betaG/E74betaK
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R70betaG/E74betaK/Q247betaK
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activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
W43F/W76F/W248F
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mutant W76F and mutant W43,76,248F are more sensitive to proteolysis by clostripain than the wild type enzyme or other Trp mutant proteins. Mutagenic replacement of Argbeta80, but not Argbeta14, with Lys results in an enzyme that is resistant to clostripain as wild type enzyme
additional information
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transposon mutagenesis and deletion of gene sucCD, accumulation of 3SP during 3,3'-dithiodipropionic acid degradation occurs in Tn5::mob-induced mutants of Advenella mimigardefordensis strain DPN7T disrupted in sucCD and in the defined deletion mutant Advenella mimigardefordensis DELTAsucCD
W76F
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mutant W76F and mutant W43,76,248F are more sensitive to proteolysis by clostripain than the wild type enzyme or other Trp mutant proteins. Mutagenic replacement of Argbeta80, but not Argbeta14, with Lys results in an enzyme that is resistant to clostripain as wild type enzyme
additional information
-, P53597
patients with SUCLA2 mutations are expected to retain the activity of G-SUCL, and only the ATP production is expected to be compromised. In addition, in patients with SUCLA2 mutations, no liver symptoms are reported. The lactate level in patients with SUCLA2 mutations is normal or moderately elevated, phenotype, overview
additional information
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the GDP-dependent isozyme SUCLG2 can complement the SUCLA2-related mitochondrial DNA depletion syndrome, a result of mutations in the beta subunit of the ADP-dependent isoform SUCLA2, EC 6.2.1.4
additional information
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naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
50-60% of the activity can be recovered following renaturation. ATP is required for reconstitution
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enzyme that is completely inactivated by 0.6 M guanidine hydrochloride, but contains 90% residual native structure, can refold back to fully active enzyme. Enzyme denatured in 1.5 M and 6.0 M guanidine hydrochloride, that is catalytically inactive and devoid of a large fraction of the native enzyme structure, can also regain the native structure upon refolding, but the refolded structures are only 86% and 71% active, respectively
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purified bacterial chaperone GroEL has no effect on the folding and assembly of succinyl-CoA synthetase
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
molecular biology
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the maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, bound to an amylose resin, is used as an affinity ligand to bind FPLC-purified wild-type and some mutant erythroid-specific aminolevulinic acid synthases, ALAS2