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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

Reaction

ATP
+
succinate
 +
CoA
=
ADP
 +
phosphate
 +
succinyl-CoA

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 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.5 succinate-CoA ligase (ADP-forming)

Engineering

Engineering on EC 6.2.1.5 - succinate-CoA ligase (ADP-forming)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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