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ADP + phosphate + succinyl-CoA
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
ATP + adipate + CoA
ADP + phosphate + adipyl-CoA
-
59% activity compared to succinate
-
-
r
ATP + ATP
adenosine 5'-tetraphosphate + ADP
-
-
-
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
-
48% activity compared to succinate
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
ATP + glutarate + CoA
ADP + phosphate + glutaryl-CoA
-
121% activity compared to succinate
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
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
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
beta,gamma-methylene-adenosine 5'-triphosphate
beta,gamma-methylene-adenosine 5'-tetraphosphate + ?
-
-
alpha,gamma-methylene adenosine tetraphosphate
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
UTP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
additional information
?
-
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
?
-
-
-
-
?
ADP + phosphate + succinyl-CoA
?
-
catalyzes the formation of ATP via substrate-level phosphorylation
-
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
-
-
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
-
-
-
?
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
-
-
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
-
-
-
r
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
-
-
r
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
-
-
r
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
generation of ATP is critical for the beta-cell mitochondrial metabolism
-
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
-
-
?
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
-
-
-
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 + acetate + CoA
ADP + phosphate + acetyl-CoA
-
-
-
-
?
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
-
-
-
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
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
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
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
802, 804, 806, 807, 809, 810, 811, 812, 813, 815, 820, 821, 823, 824 -
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
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 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
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
specific for ATP
-
-
?
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
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
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
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
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
-
-
-
-
?
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
Pigeon
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
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 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
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
specific for ATP
-
-
?
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
-
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
-
-
-
-
?
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
-
no activity with GTP/GDP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
?
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
-
-
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
-
-
-
r
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
?
-
-
-
-
-
?
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
?
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
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
?
-
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
?
-
-
catalyzes ATP-diphosphate exchange only when all the reactants necessary to establish the overall reaction are present
-
-
?
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C123ALPHAA
-
lower catalytic efficiency compared to the wild type enzyme
C123ALPHAS
-
lower catalytic efficiency compared to the wild type enzyme
C123ALPHAT
-
lower catalytic efficiency compared to the wild type enzyme
C123ALPHAV
-
lower catalytic efficiency compared to the wild type enzyme
C325E
-
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
-
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
-
the Km-values and turnover numbers are comparable to those of the wild-type enzyme
E197betaQ
-
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
-
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
-
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
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
E231betaW
-
strong decrease in activity
E231betaW/Q247betaW/E249betaW
-
strong decrease in activity
E29betaD/E33betaA/S36betaA
-
activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
E33betaA/S36betaA
-
activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
E33betaA/S36betaA/K66betaA
-
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
-
strong decrease in activity
E74betaK
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
H246D
-
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
-
activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
M156betaD/Y1258betaD/R161betaE/E162betaR
-
mutant enzyme with alphabeta-dimer subunit structure
N142N
-
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
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD/E231betA
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD/R70betaG/E74betaK
-
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
-
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
-
strong decrease in activity
R29betaD
-
activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
R70betaG
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R70betaG/E74betaK
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R70betaG/E74betaK/Q247betaK
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
W43F/W76F/W248F
-
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
W76F
-
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
A103D
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
A307V
the mutation is associated with succinyl-CoA ligase (ATP-forming) or succinyl-CoA synthetase (ADP-forming) deficiency
G424D
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
I402Y
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
M329V
the mutation is associated with succinyl-CoA ligase (ATP-forming) or succinyl-CoA synthetase (ADP-forming) deficiency
R284C
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
R40T
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
V370E
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
additional information
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
additional information
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
additional information
-
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
additional information
-
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
-
additional information
-
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
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
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
-
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
-
naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
additional information
naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
additional information
naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
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Weitzman, P.D.J.; Jaskowska-Hodges, H.
Pattern of nucleotide utilization in bacterial succinate thiokinases
FEBS Lett.
143
237-240
1982
Alcaligenes faecalis, Brevibacterium linens, Cereibacter sphaeroides, Escherichia coli, Geobacillus stearothermophilus, Klebsiella aerogenes, Kurthia zopfii, More, Paracoccus denitrificans, Pimelobacter simplex, Priestia megaterium, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas stutzeri, Salmonella enterica subsp. arizonae, Serratia marcescens, Thermus aquaticus
brenda
Buck, D.; Spencer, M.E.; Guest, J.R.
Cloning and expression of the succinyl-CoA synthetase genes of Escherichia coli K12
J. Gen. Microbiol.
132
1753-1762
1986
Escherichia coli
brenda
Allen, D.A.; Ottaway, J.H.
Succinate thiokinase in pigeon breast muscle mitochondria
FEBS Lett.
194
171-175
1986
Pigeon
brenda
Buck, D.; Spencer, M.E.; Guest, J.R.
Primary structure of the succinyl-CoA synthetase of Escherichi coli
Biochemistry
24
6245-6252
1985
Escherichia coli
brenda
Danson, M.J.; Black, S.C.; Woodland, D.L.; Wood, P.A.
Citric acid cycle enzymes of the archaebacteria: citrate synthase and succinate thiokinase
FEBS Lett.
179
120-124
1985
Escherichia coli, Haloarcula vallismortis, Halobacterium salinarum, Haloferax volcanii, Natronobacterium gregoryi, Natronococcus occultus, Natronomonas pharaonis, Priestia megaterium, Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639, Sus scrofa, Thermoplasma acidophilum
-
brenda
Wolodko, W.T.; James, M.N.G.; Bridger, W.A.
Crystallization of succinyl-CoA synthetase from Escherichia coli
J. Biol. Chem.
259
5316-5320
1984
Escherichia coli
brenda
Weitzman, P.D.J.; Kinghorn, H.A.
Succinate thiokinase from Thermus aquaticus and Halobacterium salinarium
FEBS Lett.
154
369-372
1983
Escherichia coli, Halobacterium salinarum, Thermus aquaticus
-
brenda
Birney, M.; Um, H.D.; Klein, C.
Novel mechanism of Escherichia coli succinyl-coenzyme A synthetase regulation
J. Bacteriol.
178
2883-2889
1996
Escherichia coli
brenda
Hamilton, M.L.; Ottaway, J.H.
An ATP-dependent succinic thiokinase in birds and its relation to ketone-body utilization
FEBS Lett.
123
252-254
1981
Gallus gallus, Pigeon
brenda
Pearson, P.H.; Bridger, W.A.
Isolation of the alpha and beta subunits of Escherichia coli succinyl coenzyme A synthetase and their recombination into active enzyme
J. Biol. Chem.
250
4451-4455
1975
Escherichia coli
brenda
Wider, E.A.; Tigier, H.A.
Porphyrin biosynthesis in soybean callus tissue system. VIII. Isolation, purification and general properties of succinyl CoA synthetase
Enzymologia
41
217-231
1971
Glycine max
brenda
Thomas, E.L.
Studies on the metabolism of ATP by isolated bacterial membranes: role of succinyl CoA synthetase in diglyceride kinase activity
Arch. Biochem. Biophys.
163
530-536
1974
Escherichia coli
brenda
Krebs, A.; Bridger, W.A.
Some physical parameters of succinyl-coenzyme A synthetase of Eschericha coli
Can. J. Biochem.
52
594-598
1974
Escherichia coli
brenda
Hansford, R.G.
An adenine nucleotide-linked succinic thiokinase of animal origin
FEBS Lett.
31
317-320
1973
Calliphoridae
brenda
Moffet, F.J.; Wang, T.T.; Bridger, W.A
Succinyl coenzyme A synthetase of Escherichia coli. Effects of phosphoenzyme formation and substrate binding on the reactivity and stability of the enzyme
J. Biol. Chem.
247
8139-8144
1972
Escherichia coli
brenda
Murakami, K.; Mitchell, T.; Nishimura, J.S.
Nucleotide specificity of Escherichia coli succinic thiokinase
J. Biol. Chem.
247
6247-6252
1972
Escherichia coli
brenda
Hager, L.P.
Succinyl CoA synthetase
The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
6
387-399
1962
Escherichia coli, Spinacia oleracea, Sus scrofa
-
brenda
Mann, C.J.; Hardies, S.C.; Nishimura, J.S.
Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. beta-Cys325 is a nonessential active site residue
J. Biol. Chem.
264
1457-1460
1989
Escherichia coli
brenda
Khan, I.A.; Nishimura, J.S.
Native-like intermediate on the folding pathway of Escherichia coli succinyl-CoA synthetase
J. Biol. Chem.
263
2152-2158
1988
Escherichia coli
brenda
Wider de Xifra, E.A.; Del C.Batlle, A.M.
Porphyrin biosynthesis: immobilized enzymes and ligands. VI. Studies on succinyl CoA synthetase from cultured soya bean cells
Biochim. Biophys. Acta
523
245-249
1978
Glycine max
brenda
Nishimura, J.S.; Mitchell, T.; Matula, J.M.
Inactivation of Escherichia coli succinic thiokinase by selective oxidation of thiol groups by permanganate
Biochem. Biophys. Res. Commun.
69
1057-1064
1976
Escherichia coli
brenda
Kondo, H.; Ohmori, T.; Shibata, H.; Sase, K.; Takahashi, R.; Tokuyama, T.
Thermostable succinyl-coenzyme A synthetase from Nitrosomonas europaea ATCC 25978: purification and properties
J. Ferment. Bioeng.
79
499-502
1995
Nitrosomonas europaea
-
brenda
Kavanaugh-Black, A.; Connolly, D.M.; Chugani, S.A.; Chakrabarty, A.M.
Characterization of nucleoside-diphosphate kinase from Pseudomonas aeruginosa: Complex formation with succinyl-CoA synthetase
Proc. Natl. Acad. Sci. USA
91
5883-5887
1994
Pseudomonas aeruginosa
brenda
Krivanek, J.; Novakova, L.
A novel effect of vanadium ions: inhibition of succinyl-CoA synthetase
Gen. Physiol. Biophys.
10
71-82
1991
Rattus norvegicus
brenda
Krivanek, J.; Novakova, L.
Differential sensitivity of the brain ATP-dependent and GTP-dependent succinyl-CoA synthetase to vanadium ions. Developmental aspects
Physiol. Res.
41
345-350
1992
Rattus norvegicus
brenda
Fong, G.; Bridger, W.A.
Folding and assembly of the Escherichia coli succinyl-CoA synthetase heterotetramer without participation of molecular chaperones
Biochemistry
31
5661-5664
1992
Escherichia coli
brenda
Majumdar, R.; Guest, J.R.; Bridger, W.A.
Functional consequences of substitution of the active site (phospho)histidine residue of Escherichia coli succinyl-CoA synthetase
Biochim. Biophys. Acta
1076
86-90
1991
Escherichia coli
brenda
Lahti, C.J.; Bradley, P.J.; Johnson, P.J.
Molecular characterization of the alpha-subunit of Trichomonas vaginalis hydrogenosomal succinyl CoA synthetase
Mol. Biochem. Parasitol.
66
309-318
1994
Trichomonas vaginalis
brenda
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Adenosine 5-tetraphosphate is synthesized by the histidine alpha142-->asparagine mutant of Escherichia coli succinyl-CoA synthetase
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