Information on EC 6.2.1.5 - succinate-CoA ligase (ADP-forming) and Organism(s) Homo sapiens and UniProt Accession P53597

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This record set is specific for:
Homo sapiens
UNIPROT: P53597


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
6.2.1.5
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RECOMMENDED NAME
GeneOntology No.
succinate-CoA ligase (ADP-forming)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
anaerobic energy metabolism (invertebrates, mitochondrial)
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incomplete reductive TCA cycle
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methylaspartate cycle
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partial TCA cycle (obligate autotrophs)
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pyruvate fermentation to acetate V
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pyruvate fermentation to acetate VI
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reductive TCA cycle I
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reductive TCA cycle II
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TCA cycle I (prokaryotic)
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TCA cycle II (plants and fungi)
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TCA cycle III (animals)
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TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
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citric acid cycle
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Citrate cycle (TCA cycle)
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Propanoate metabolism
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C5-Branched dibasic acid metabolism
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Carbon fixation pathways in prokaryotes
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
succinate:CoA ligase (ADP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9080-33-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha-subunit
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
in patients with enzyme mutations, muscle histology shows severe lipid accumulation, and a marked type I fibre predominance is found, with an increased variability in fibre diameter. mtDNA depletion in succinate-CoA ligase deficiency
malfunction
metabolism
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key role of the enzyme in the Krebs cycle
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
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-
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r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
P53597, Q9P2R7
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r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
valproyl-CoA
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45-55% inhibition at 1 mM
zinc chloride
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additional information
-
no inhibition by valproic acid
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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
PDB
SCOP
CATH
ORGANISM
UNIPROT
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SUBUNITS
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, from Escherichia coli strain Top10 by amylose affinity chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, in Escherichia coli strain Top10
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gene SUCLG2, DNA and amino acid sequence determination and analysis, semi quantitative RT-PCR expression analysis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
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the maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, bound to an amylose resin, is used as an affinity ligand to bind FPLC-purified wild-type and some mutant erythroid-specific aminolevulinic acid synthases, ALAS2