6.2.1.5: succinate-CoA ligase (ADP-forming)
This is an abbreviated version!
For detailed information about succinate-CoA ligase (ADP-forming), go to the full flat file.
Word Map on EC 6.2.1.5
-
6.2.1.5
-
mtdna
-
suclg1
-
methylmalonic
-
aciduria
-
dguok
-
encephalomyopathic
-
c10orf2
-
mimigardefordensis
-
twinkle
-
c4-dicarboxylic
-
thiokinase
-
faroe
-
gtp-forming
-
hepatocerebral
-
3,3'-dithiodipropionic
-
molecular biology
- 6.2.1.5
- mtdna
- suclg1
-
methylmalonic
-
aciduria
- dguok
-
encephalomyopathic
- c10orf2
- mimigardefordensis
- twinkle
-
c4-dicarboxylic
- thiokinase
-
faroe
-
gtp-forming
-
hepatocerebral
-
3,3'-dithiodipropionic
- molecular biology
Reaction
Synonyms
A-SCS, A-STK, A-SUCL, AarC, ADP-forming succinyl-CoA synthase, ADP-forming succinyl-CoA synthetase, ADP-forming SUCL, ATP-dependent succinate:CoA ligase, ATP-forming SUCL, ATP-SCS, ATP-specific succinate:CoA ligase, ATP-specific SUCL, ATP-succinyl-CoA synthetase, CG11963, More, SCACT, SCS, SCS A-beta, SCS ADP-forming beta subunit, SCS-alpha, SCS-beta, SCS-betaA, ScsB, STK, SucCD, SucCDAm, succinate coenzyme A ligase, Succinate thiokinase, succinate-CoA ligase, Succinic thiokinase, Succinyl coenzyme A synthetase, Succinyl coenzyme A synthetase (adenosine diphosphate-forming), succinyl-CoA ligase (ATP-forming), succinyl-CoA synthase, succinyl-CoA synthase ADP-forming beta subunit, Succinyl-CoA synthetase, Succinyl-CoA synthetase (ADP-forming), succinyl-CoA synthetase subunit alpha, succinyl-CoA-synthetase (ATP), succinyl-CoA:acetate CoA-transferase, succinyl-coenzyme A:acetate CoA-transferase, SUCL, SUCLA2, Synthetase, succinyl coenzyme A (adenosine diphosphate-forming), Tneu_1463, Tneu_1464, VEG239, VEG63, Vegetative protein 239, Vegetative protein 63
ECTree
6.2.1.5 succinate-CoA ligase (ADP-forming)Advanced search results
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results (Substrates Products
Substrates Products on EC 6.2.1.5 - succinate-CoA ligase (ADP-forming)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + adipate + CoA
ADP + phosphate + adipyl-CoA
-
59% activity compared to succinate
-
-
r
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
-
48% activity compared to succinate
-
-
r
ATP + glutarate + CoA
ADP + phosphate + glutaryl-CoA
-
121% activity compared to succinate
-
-
r
ATP + oxalate + CoA
ADP + phosphate + oxalyl-CoA
-
9% activity compared to succinate
-
-
r
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
-
10% activity compared to succinate
-
-
r
ATP + succinate + CoA
?
-
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 5'-triphosphate
beta,gamma-methylene-adenosine 5'-tetraphosphate + ?
-
-
alpha,gamma-methylene adenosine tetraphosphate
?
ADP + phosphate + succinyl-CoA
?
-
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
?
-
catalyzes the formation of ATP via substrate-level phosphorylation
-
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
the enzyme carries out the substrate-level phosphorylation in the citric acid cycle
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
the enzyme carries out the substrate-level phosphorylation in the citric acid cycle
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
generation of ATP is critical for the beta-cell mitochondrial metabolism
-
?
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
-
-
-
r
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
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
-
-
-
r
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
-
-
-
r
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
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
-
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 + D-malate + CoA
ADP + phosphate + D-malyl-CoA
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
succinate is the best substrate, SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
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
ATP is the preferred cosubstrate
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
ATP is the preferred cosubstrate
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
the enzyme is part of the Krebs cycle
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
specific for ATP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
specific for succinate
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has no activity with GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
-
-
r
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
-
-
r
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has no activity with GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has no activity with GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has no activity with GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km value for ADP and for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
enzyme has a low Km-value for ADP and a high Km-value for GDP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
no activity with GDP/GTP
-
-
?
additional information
?
-
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
?
-
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
?
-
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
-
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
?
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
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
?
-
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
?
-
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
?
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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enzyme is involved in the initial step of porphyrin biosynthesis
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additional information
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deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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catalyzes ATP-diphosphate exchange only when all the reactants necessary to establish the overall reaction are present
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