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Information on EC 6.2.1.4 - succinate-CoA ligase (GDP-forming) and Organism(s) Sus scrofa and UniProt Accession O19069

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.4 succinate-CoA ligase (GDP-forming)
IUBMB Comments
Itaconate can act instead of succinate, and ITP instead of GTP.
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This record set is specific for:
Sus scrofa
UNIPROT: O19069
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The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
succinyl-coa synthetase, suclg1, suclg2, succinate-coa ligase, succinate thiokinase, succinyl coa synthetase, succinyl-coa synthase, succinic thiokinase, succinyl coenzyme a synthetase, g-scs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G-STK
-
-
-
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GTP-specific succinyl-CoA synthetase
SCS-alpha
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-
-
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SCS-beta
-
-
-
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SCS-betaG
-
-
-
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Succinate thiokinase
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-
-
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Succinic thiokinase
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-
-
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Succinyl CoA synthetase
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-
-
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Succinyl coenzyme A synthetase
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-
-
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Succinyl coenzyme A synthetase (GDP-forming)
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-
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Succinyl coenzyme A synthetase (guanosine diphosphate-forming)
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-
-
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Succinyl-CoA synthetase
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Succinyl-CoA synthetase (GDP-forming)
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-
-
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succinyl-coenzyme A synthetase
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Synthetase, succinyl coenzyme A (guanosine diphosphate-forming)
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
show the reaction diagram
catalytic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
succinate:CoA ligase (GDP-forming)
Itaconate can act instead of succinate, and ITP instead of GTP.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-36-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
?
GTP + L-malate + CoA
GDP + phosphate + L-malyl-CoA
show the reaction diagram
low activity
-
-
?
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 0.007
CoA
0.009 - 0.027
GTP
0.39 - 5.1
succinate
additional information
additional information
-
kinetic mechanism and thermodynamic parameter values, quasi-steady-state models, evaluation of five different proposed mechanisms, overview. The ordered ter-ter mechanism with dead-end product inhibition of succinate against succinyl-CoA effectively matches kinetic data on pig heart enzyme, thermodynamic-constrained kinetic model
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme participates in the tricarboxylic acid cycle, ketone body metabolism and haem biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUCA_PIG
346
0
36117
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74000
-
enzyme pI 6.0, at pI, gel filtration
77000
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enzyme form pI 5.9, at pH 8.0, gel filtration
78000
-
enzyme form pI 6.3, at pH 8.0 and at pI, gel filtration
79250
-
enzyme form pI 6.0, at pH 8.0, gel filtration
80000
-
enzyme form pI 6.4, at pI, gel filtration
82500
-
enzyme form pI 6.4, at pH 8.0, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method using a precipitant solution containing 10% (v/v) isopropanol, 100 mM ammonium sulfate, 20% (w/v) polyethylene glycol 4000, and 100 mM HEPES or Bicine, pH 7.5
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in complex with CoA, hanging drop vapor diffusion method, using 1.6 M ammonium sulfate, 1 mM 2-mercaptoethanol, 50 mM sodium/potassium phosphate pH 7.0
in complex with succinate, magnesium ions and CoA, hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 3350 and 0.2 M magnesium formate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V330M
the mutant exhibits an about 10fold higher Km value for succinate compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiTrap Blue column chromatography, and Sephadex G-25 gel filtration
at least 5 peaks of enzyme having isoelectric points of 6.4, 6.2, 6.0, 5.9 and 5.8
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G-Sephadex Coarse column chromatography, hydroxyapatite column chromatography, and Q-Sepharose Fast Flow column chromatography
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Ni-NTA column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
two mRNA transcripts arise from a single gene and are generated by mutually exclusive splicing
beta-subunit
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crystallization of the phosphorylated and of the dephosphorylated enzyme form, refined to 2.1 A resolution
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nishimura, J.S.; Ybarra J.; Mitchell, T.; Horowitz P.M.
Isolation, amino acid analysis and refolding of subunits of pig heart succinyl-CoA synthetase
Biochem. J.
250
429-434
1988
Sus scrofa
Manually annotated by BRENDA team
Baccanari, D.P.; Cha, S.
Succinate thiokinase. VI. Multiple interconvertible forms of the enzyme
J. Biol. Chem.
248
15-24
1973
Sus scrofa
Manually annotated by BRENDA team
Um H.D.; Klein, C.
Regulatory role of GDP in the phosphoenzyme formation of guanine nucleotide: specific form of succinyl coenzyme A synthetase
J. Protein Chem.
13
177-185
1994
Dictyostelium discoideum, Sus scrofa
Manually annotated by BRENDA team
Ryan D.G.; Lin, T.; Brownie, E.; Bridger, W.A.; Wolodko, W.T.
Mutually exclusive splicing generates two distinct isoforms of pig heart succinyl-CoA synthetase
J. Biol. Chem.
272
21151-21159
1997
Sus scrofa (O19069), Sus scrofa
Manually annotated by BRENDA team
Bailey, D.L.; Wolodko, W.T.; Bridger, W.A.
Cloning, characterization, and expression of the beta subunit of pig heart succinyl-CoA synthetase
Plant Sci.
2
1255-1262
1993
Sus scrofa
Manually annotated by BRENDA team
Fraser, M.E.; James, M.N.G.; Bridger, W.A.; Wolodko, W.T.
Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase
J. Mol. Biol.
299
1325-1339
2000
Sus scrofa
Manually annotated by BRENDA team
Fraser, M.E.; Hayakawa, K.; Hume, M.S.; Ryan, D.G.; Brownie, E.R.
Interactions of GTP with the ATP-grasp domain of GTP-specific succinyl-CoA synthetase
J. Biol. Chem.
281
11058-11065
2006
Sus scrofa
Manually annotated by BRENDA team
Li, X.; Wu, F.; Beard, D.A.
Identification of the kinetic mechanism of succinyl-CoA synthetase
Biosci. Rep.
33
145-163
2013
Sus scrofa
Manually annotated by BRENDA team
Huang, J.; Fraser, M.
Structural basis for the binding of succinate to succinyl-CoA synthetase
Acta Crystallogr. Sect. D
72
912-921
2016
Sus scrofa (P53590), Sus scrofa
Manually annotated by BRENDA team
Huang, J.; Malhi, M.; Deneke, J.; Fraser, M.E.
Structure of GTP-specific succinyl-CoA synthetase in complex with CoA
Acta Crystallogr. Sect. F
71
1067-1071
2015
Sus scrofa (P53590), Sus scrofa
Manually annotated by BRENDA team