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Information on EC 6.2.1.4 - succinate-CoA ligase (GDP-forming) and Organism(s) Homo sapiens and UniProt Accession P53597
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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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Word Map
- 6.2.1.4
-
tricarboxylic
- tca
- malate
- sucla2
-
citric
- mtdna
-
methylmalonic
-
krebs
- alpha-ketoglutarate
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adp-forming
-
substrate-level
- fumarase
-
aciduria
- hydrogenosomes
- dguok
-
phosphohistidine
-
coa-transferase
- phosphoenzyme
-
encephalomyopathic
-
nishimura
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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, succinic thiokinase, succinyl-coa synthase, succinyl coenzyme a synthetase, g-scs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G-STK
-
-
-
-
G-SUCL
SCS
SCS-alpha
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-
-
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SCS-beta
-
-
-
-
SCS-betaG
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-
-
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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 (GDP-forming)
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-
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Synthetase, succinyl coenzyme A (guanosine diphosphate-forming)
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-
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SCS
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
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-
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-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
succinate:CoA ligase (GDP-forming)
Itaconate can act instead of succinate, and ITP instead of GTP.
CAS REGISTRY NUMBER
COMMENTARY
9014-36-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. ATP-specific succinate:CoA ligase, EC 6.2.1.5
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the enzyme is preferably expressed in anabolic tissues
additional information
the enzyme is preferably expressed in anabolic tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
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
malfunction
a patient with a SUCLG1 mutation shows steatosis in liver hstology 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
enzyme mutations cause the encephalomyopathic mitochondrial DNA depletion syndrome with methylmalonic aciduria
malfunction
-
deficiency of SUCLA2 results in Leigh's or a Leigh-like syndrome with onset of severe hypotonia in early infancy, severemuscular atrophy, and sensorineural hearing impairment. SUCLA2-related mitochondrial DNA depletion syndrome is a result of mutations in the beta subunit of the ADP-dependent isoform of the Krebs cycle succinyl-CoA synthase, phenotype, overview
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUCA_HUMAN
346
0
36250
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
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
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
additional information
-
naturally occuring mutation c.113_114delAT causes succinate-CoA ligase deficiency
additional information
naturally occuring mutation c.113_114delAT causes succinate-CoA ligase deficiency
additional information
naturally occuring mutation c.113_114delAT causes succinate-CoA ligase deficiency
additional information
-
the severe disorder in patients with SUCLG1 mutations is likely caused by the absence of both ASUCL and G-SUCL, and thereby a compromised formation of both ATP and GTP. Severe lactic acidosis is found in patients with SUCLG1 mutations, phenotype, overview
additional information
the severe disorder in patients with SUCLG1 mutations is likely caused by the absence of both ASUCL and G-SUCL, and thereby a compromised formation of both ATP and GTP. Severe lactic acidosis is found in patients with SUCLG1 mutations, phenotype, overview
additional information
the severe disorder in patients with SUCLG1 mutations is likely caused by the absence of both ASUCL and G-SUCL, and thereby a compromised formation of both ATP and GTP. Severe lactic acidosis is found in patients with SUCLG1 mutations, phenotype, overview
additional information
-
the GDP-dependent isozyme SUCLG2, EC 6.2.1.5, can complement the SUCLA2-related mitochondrial DNA depletion syndrome, a result of mutations in the beta subunit of the ADP-dependent isoform SUCLA2, EC 6.2.1.4
additional information
-
naturally occuring mutation c.113_114delAT causes succinate-CoA ligase deficiency
additional information
naturally occuring mutation c.113_114delAT causes succinate-CoA ligase deficiency
additional information
naturally occuring mutation c.113_114delAT causes succinate-CoA ligase deficiency
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)
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
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
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 (Q96I99), Homo sapiens
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 succinate CoA ligases
J. Inherit. Metab. Dis.
37
353-357
2014
Homo sapiens
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 (P53597), Homo sapiens
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