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Information on EC 6.2.1.4 - succinate-CoA ligase (GDP-forming) and Organism(s) Homo sapiens and UniProt Accession Q96I99

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     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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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q96I99
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The taxonomic range for the selected organisms is: Homo sapiens
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G-STK
-
-
-
-
G-SUCL
GDP-forming SUCL
301393, 301394
-
GTP-dependent succinate:CoA ligase
247
-
GTP-specific succinate:CoA ligase
247
-
GTP-specific SUCL
247
-
SCS-alpha
-
-
-
-
SCS-beta
-
-
-
-
SCS-betaG
-
-
-
-
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
247
-
Succinyl-CoA synthetase (GDP-forming)
-
-
-
-
SUCL
247
-
SUCLG1
301393
-
SUCLG2
301394
-
Synthetase, succinyl coenzyme A (guanosine diphosphate-forming)
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
GDP + phosphate + succinyl-CoA
GTP + succinate + CoA
show the reaction diagram
-
-
-
-
r
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
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
Q96I99
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
Q96I99
-
-
-
r
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
P53597, Q96I99
-
-
-
r
GDP + phosphate + succinyl-CoA
GTP + succinate + CoA
show the reaction diagram
-
-
-
-
r
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
valproyl-CoA
zinc chloride
-
-
ZnCl2
-
complete inhibition at 1mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63
GTP
-
at pH 8.0 and 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high level
Manually annotated by BRENDA team
high level
Manually annotated by BRENDA team
high level
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a patient with a SUCLG1 mutation shows steatosis in liver histology and severe lactic acidosis, one patient shows combined deficiency of respiratory chain complexes I, III and IV in liver. The accumulated succinyl-CoA inhibits the reaction catalysed by methylmalonyl-CoA mutase or causes an equilibrium shift. mtDNA depletion in succinate-CoA ligase deficiency
malfunction
metabolism
-
key role of the enzyme in the Krebs cycle
physiological function
-
SUCLG2, EC 6.2.1.5, to a higher degree than SUCLA2, is crucial for mtDNA maintenance involving mitochondrial NDPK
additional information
-
the GDP-dependent isozyme SUCLG2, EC 6.2.1.5, can complement the SUCLA2-related mitochondrial DNA depletion syndrome
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
SUCB2_HUMAN
432
0
46511
Swiss-Prot
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
the enzyme is composed of an alpha subunit, encoded by SUCLG1, and a beta subunit, encoded by either SUCLA2 or SUCLG2. The alpha-subunit forms a heterodimer with either of its beta-subunits, resulting in an ADP-forming succinate-CoA ligase, EC 6.2.1.5, and a GDP-forming succinate-CoA ligase, EC 6.2.1.4, respectively
heterodimer
the enzyme is composed of an alpha subunit, encoded by SUCLG1, and a beta subunit, encoded by either SUCLA2 or SUCLG2. The alpha-subunit forms a heterodimer with either of its beta-subunits, resulting in an ADP-forming succinate-CoA ligase, EC 6.2.1.5, and a GDP-forming succinate-CoA ligase, EC 6.2.1.4, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A209E
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
E263K
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
H71R
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
additional information
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
gene SUCLA2, DNA and amino acid sequence determination and analysis, semi quantitative RT-PCR expression analysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ostergaard, E.
Disorders caused by deficiency of succinate-CoA ligase
J. Inherit. Metab. Dis.
31
226-229
2008
Homo sapiens, Homo sapiens (P53597), Homo sapiens (Q96I99)
Manually annotated by BRENDA team
Miller, C.; Wang, L.; Ostergaard, E.; Dan, P.; Saada, A.
The interplay between SUCLA2, SUCLG2, and mitochondrial DNA depletion
Biochim. Biophys. Acta
1812
625-629
2011
Homo sapiens
Manually annotated by BRENDA team
Luis, P.B.; Ruiter, J.; Ijlst, L.; de Almeida, I.T.; Duran, M.; Wanders, R.J.; Silva, M.F.
Valproyl-CoA inhibits the activity of ATP- and GTP-dependent succinate:CoA ligases
J. Inherit. Metab. Dis.
37
353-357
2013
Homo sapiens
Manually annotated by BRENDA team
Dobolyi, A.; Bago, A.G.; Gal, A.; Molnar, M.J.; Palkovits, M.; Adam-Vizi, V.; Chinopoulos, C.
Localization of SUCLA2 and SUCLG2 subunits of succinyl CoA ligase within the cerebral cortex suggests the absence of matrix substrate-level phosphorylation in glial cells of the human brain
J. Bioenerg. Biomembr.
47
33-41
2015
Homo sapiens, Homo sapiens (Q96I99)
Manually annotated by BRENDA team
Luis, P.; Ruiter, J.; IJlst, L.; De Almeida, I.; Duran, M.; Wanders, R.; Silva, M.
Valproyl-CoA inhibits the activity of ATP- and GTP-dependent succinateCoA ligases
J. Inherit. Metab. Dis.
37
353-357
2014
Homo sapiens
Manually annotated by BRENDA team
Carrozzo, R.; Verrigni, D.; Rasmussen, M.; de Coo, R.; Amartino, H.; Bianchi, M.; Buhas, D.; Mesli, S.; Naess, K.; Born, A.P.; Woldseth, B.; Prontera, P.; Batbayli, M.; Ravn, K.; Joensen, F.; Cordelli, D.M.; Santorelli, F.M.; Tulinius, M.; Darin, N.; Duno, M.; Jouvencel, P.; Burlina, A.; Stangoni, G.; , B.
Succinate-CoA ligase deficiency due to mutations in SUCLA2 and SUCLG1 phenotype and genotype correlations in 71 patients
J. Inherit. Metab. Dis.
39
243-252
2016
Homo sapiens, Homo sapiens (P53597)
Manually annotated by BRENDA team
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