Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.2.1.3 extracted from

  • Tuohetahuntila, M.; Spee, B.; Kruitwagen, H.S.; Wubbolts, R.; Brouwers, J.F.; van de Lest, C.H.; Molenaar, M.R.; Houweling, M.; Helms, J.B.; Vaandrager, A.B.
    Role of long-chain acyl-CoA synthetase 4 in formation of polyunsaturated lipid species in hepatic stellate cells (2015), Biochim. Biophys. Acta, 1851, 220-230 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
rosiglitazone
-
Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus O35547
-
-

Source Tissue

Source Tissue Comment Organism Textmining
hepatic stellate cell
-
Rattus norvegicus
-
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + arachidonate + CoA
-
Rattus norvegicus AMP + diphosphate + arachidonoyl-CoA
-
?

Subunits

Subunits Comment Organism
? x * 74000, SDS-PAGE Rattus norvegicus

Synonyms

Synonyms Comment Organism
ACSL4
-
Rattus norvegicus
long-chain acyl-CoA synthetase 4
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Rattus norvegicus

Expression

Organism Comment Expression
Rattus norvegicus isoform ACSL4 is upregulated in activated hepatic stellate cells up

General Information

General Information Comment Organism
physiological function upregulation of isoform ACSL4 is responsible for the increase in polyunsaturated fatty acid-triacylglycerol species during activation of hepatic stellate cells, which may serve to protect cells against a shortage of polyunsaturated fatty acids required for eicosanoid secretion Rattus norvegicus