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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)

Renatured

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

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
50-60% of the activity can be recovered following renaturation. ATP is required for reconstitution
-
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
-
purified bacterial chaperone GroEL has no effect on the folding and assembly of succinyl-CoA synthetase
-