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Information on EC 6.2.1.15 - arachidonate-CoA ligase and Organism(s) Homo sapiens and UniProt Accession O60488

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.15 arachidonate-CoA ligase
IUBMB Comments
Not identical with EC 6.2.1.3 long-chain-fatty-acid---CoA ligase. Icosa-8,11,14-trienoate, but not the other long-chain fatty acids, can act in place of arachidonate.
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This record set is specific for:
Homo sapiens
UNIPROT: O60488
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Word Map
  • 6.2.1.15
  • ferroptosis
  • arachidonic
  • acsls
  • erastin
  • ferroptosis-related
  • acid-coa
  • triacsin
  • ferrostatin-1
  • slc7a11
  • alport
  • col4a5
  • erastin-induced
  • liproxstatin-1
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
acsl4, facl4, arachidonoyl-coa synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACSL4
-
-
Acyl-CoA synthetase
-
-
Arachidonoyl-CoA synthetase
-
-
-
-
FACL4
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
arachidonate:CoA ligase (AMP-forming)
Not identical with EC 6.2.1.3 long-chain-fatty-acid---CoA ligase. Icosa-8,11,14-trienoate, but not the other long-chain fatty acids, can act in place of arachidonate.
CAS REGISTRY NUMBER
COMMENTARY hide
82047-87-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
show the reaction diagram
ATP + 8,11,14-eicosatrienoate + CoA
AMP + diphosphate + 8,11,14-eicosatrienoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + arachidonate + CoA
?
show the reaction diagram
-
enzyme may control the level of free arachidonate in platelets, limiting prostaglandin synthesis by the unstimulated cell and capturing free arachidonate from extracellular sources
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
show the reaction diagram
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
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
show the reaction diagram
arachidonic acid is a preferred substrate for ACSL4 variant 1 in intact human smooth muscle cells
-
-
?
ATP + arachidonate + CoA
?
show the reaction diagram
-
enzyme may control the level of free arachidonate in platelets, limiting prostaglandin synthesis by the unstimulated cell and capturing free arachidonate from extracellular sources
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8,11,14-Eicosatrienoate
-
-
arachidonate
-
unlabeled arachidonate inhibits arachidonate activation
eicosapentaenoate
-
slight
fatty acids
-
overview
H2O2
-
-
oleate
-
not
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
arachidonate
-
-
0.5
ATP
-
-
0.13
CoA
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ACSL4 variant 1
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
a breast cancer cell model, comprising different cell lines, expresses ACSL4 in all cell lines, high expression level
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
The alternative pathway, in which the rate-limiting enzyme is ACSL4, provides arachidonoyl-CoA to a mitochondrial acyl-CoA thioesterase that releases AA in mitochondria and directs this fatty acid to the lipooxygenase for its subsequent conversion to lipooxygenase metabolites
physiological function
-
the acyl-CoA synthetase, ACSL4, belongs to a five member family of enzymes that esterify mainly arachidonic acid into acyl-CoA. Role of ACSL4 and acyl-CoA thioesterase, ACOT2, in the production of lipooxygenase metabolites in breast cancer cells, regulation, overview. ACSL4 is the rate-limiting enzyme for intramitochondrial arachidonic acid generation and export, for the conversion to lipooxygenase metabolites
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACSL4_HUMAN
711
1
79188
Swiss-Prot
Secretory Pathway (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
heat inactivation does not distinguish between arachidonoyl-CoA synthetase and a palmitoyl-CoA synthetase
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stable for up to 6 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional overexpression of ACSL4 variant 1 in smooth muscle cells using a retroviral vector, semiquantitative and quantitative real-time PCR expression analysis
overexpression of ACSL4 in the MCF-7 Tet-off/ACSL4 cell line affects cell proliferation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bakken, A.M.; Farstad, M.
Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets
Biochem. J.
261
71-76
1989
Homo sapiens
Manually annotated by BRENDA team
Bakken, A.M.; Farstad, M.; Holmsen, H.
Identity between palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase in human platelets?
Biochem. J.
274
145-152
1991
Homo sapiens
Manually annotated by BRENDA team
Hornberger, W.; Patscheke, H.
Primary stimuli of icosanoid release inhibit arachidonoyl-CoA synthetase and lysophospholipid acyltransferase. Mechanism of action of hydrogen peroxide and methyl mercury in platelets
Eur. J. Biochem.
187
175-181
1990
Homo sapiens
Manually annotated by BRENDA team
Laposata, M.; Reich, E.L.; Majerus, P.W.
Arachidonoyl-CoA synthetase. Separation from nonspecific acyl-CoA synthetase and distribution in various cells and tissues
J. Biol. Chem.
260
11016-11020
1985
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Neufeld, E.J.; Sprecher, H.; Evans, R.W.; Majerus, P.W.
Fatty acid structural requirements for activity of arachidonoyl-CoA synthetase
J. Lipid Res.
25
288-293
1984
Homo sapiens
Manually annotated by BRENDA team
Wilson, D.B; Prescott, S.M.; Majerus, P.W.
Discovery of an arachidonoyl coenzyme A synthetase in human platelets
J. Biol. Chem.
257
3510-3515
1982
Homo sapiens
Manually annotated by BRENDA team
Laposata, M.
Solubilization of arachidonate-CoA ligase from cell membranes, chromatographic separation from nonspecific long-chain fatty acid CoA ligase, and isolation of mutant cell line defective in arachidonate-CoA ligase
Methods Enzymol.
187
237-242
1990
Bos taurus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Golej, D.L.; Askari, B.; Kramer, F.; Barnhart, S.; Vivekanandan-Giri, A.; Pennathur, S.; Bornfeldt, K.E.
Long-chain acyl-CoA synthetase 4 modulates prostaglandin E2 release from human arterial smooth muscle cells
J. Lipid Res.
52
782-793
2011
Homo sapiens (O60488), Homo sapiens
Manually annotated by BRENDA team
Maloberti, P.M.; Duarte, A.B.; Orlando, U.D.; Pasqualini, M.E.; Solano, A.R.; Lopez-Otin, C.; Podesta, E.J.
Functional interaction between acyl-CoA synthetase 4, lipooxygenases and cyclooxygenase-2 in the aggressive phenotype of breast cancer cells
PLoS ONE
5
e15540
2010
Homo sapiens
Manually annotated by BRENDA team