6.2.1.4: succinate-CoA ligase (GDP-forming)

This is an abbreviated version!
For detailed information about succinate-CoA ligase (GDP-forming), go to the full flat file.

Reaction

Synonyms

ATP-specific SCS, G-SCS, G-STK, G-SUCL, GDP-forming SUCL, GTP-dependent succinate:CoA ligase, GTP-forming SUCL, GTP-specific succinate:CoA ligase, GTP-specific succinyl-CoA synthetase, GTP-specific SUCL, GTPSCS, SCS, SCS-alpha, SCS-beta, SCS-betaG, ScsA, SCSalpha, SucCDAm, Succinate thiokinase, succinate-CoA ligase, Succinic thiokinase, Succinyl CoA synthetase, Succinyl coenzyme A synthetase, Succinyl coenzyme A synthetase (GDP-forming), Succinyl coenzyme A synthetase (guanosine diphosphate-forming), succinyl-CoA synthase, Succinyl-CoA synthetase, Succinyl-CoA synthetase (GDP-forming), succinyl-CoA synthetase subunit beta, succinyl-coenzyme A synthetase, SUCL, SUCLG1, SUCLG2, Synthetase, succinyl coenzyme A (guanosine diphosphate-forming)

ECTree

     6 Ligases

         6.2 Forming carbon-sulfur bonds

             6.2.1 Acid-thiol ligases

                6.2.1.4 succinate-CoA ligase (GDP-forming)

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
2363	AA Sequence
1	CAS Registry Number
12	Cloned(Commentary)
26	Cofactor
5	Crystallization (Commentary)
135	Disease/ Diagnostics
9	General Information
10	Inhibitors
5	kcat/KM [mM/s]
27	KM Value [mM]
14	Localization
8	Metals/Ions
9	Molecular Weight [Da]
28	Natural Substrates/ Products (Substrates)
59	Organism
9	Pathway
39	PDB ID
3	pH Optimum
1	pI Value
1	Posttranslational Modification
16	Protein Variants
8	Purification (Commentary)
2	Reaction
1	Reaction Type
59	Reference
2	Renatured (Commentary)
44	Source Tissue
2	Specific Activity [micromol/min/mg]
90	Substrates and Products (Substrate)
10	Subunits
72	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Stability [°C]
5	Turnover Number [1/s]

Renatured

print visible entries

print all entries

Renatured on EC 6.2.1.4 - succinate-CoA ligase (GDP-forming)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Renatured Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

denaturing of the enzyme in 6 M guanidinium chloride for 24 h and refolding by rapid dilution (1:20 v:v) into one of three solutions: benign buffer consisting of 50 mM KCl, 60 mM potassium phosphate pH 7.4, arginine buffer containing 0.67 M L-arginine-HCl, 60 mM potassium phosphate, pH 7.4, or arginine buffer containing 0.67 M L-arginine-HCl, 60 mM potassium phosphate, 50 mM Tris-HCl, pH 8.0, kinetics of refolding, overview. Enzyme refolding in arginine buffer, pH 7.4, is temperature-dependent, the rate of refolding follows apparent first-order kinetics. Omission of phosphate from the buffer does not affect the rate. The refolded enzyme form is much less thermostable than the native form

Thermus aquaticus

-

726583

refolded from its isolated subunit after denaturation. Refolding of enzyme denatured in 6 M guanidine hydrochloride or of alpha- and beta-subunits isolated in the solvent requires the presence of either ethylene glycol or glycerol, optimally at 20-25% (v/v). MgGTP2- does not stimulate reactivation of the enzyme. Yields of 60% and 40% are obtained in the refolding of denatured enzyme and isolated subunits respectively

Sus scrofa

-

785