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Literature summary for 6.2.1.3 extracted from

  • Richards, M.R.; Harp, J.D.; Ory, D.S.; Schaffer, J.E.
    Fatty acid transport protein 1 and long chain acyl CoA synthetase 1 interact in adipocytes (2005), J. Lipid Res., 47, 665-672.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Triacsin C 90% inhibition at 0.02 mM Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus inhibition of ACSL1 activity in adipocytes impairs fatty acid uptake, suggesting that esterification is essential for fatty acid transport. A constitutive interaction between the fatty acid transport protein FATP1 and ACSL1 contributes to efficient cellular uptake of long chain fatty acids in adipocytes through vectorial acylation ?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
3T3-L1 cell
-
Mus musculus
-
adipocyte
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + oleate + CoA
-
Mus musculus AMP + diphosphate + oleoyl-CoA
-
?
additional information inhibition of ACSL1 activity in adipocytes impairs fatty acid uptake, suggesting that esterification is essential for fatty acid transport. A constitutive interaction between the fatty acid transport protein FATP1 and ACSL1 contributes to efficient cellular uptake of long chain fatty acids in adipocytes through vectorial acylation Mus musculus ?
-
?

Subunits

Subunits Comment Organism
More fatty acid transport protein FATP1 and ACSL1 participate in an oligomeric complex in 3T3-L1 adipocytes. The interaction between ACSL1 and FATP1 is constitutive Mus musculus

Synonyms

Synonyms Comment Organism
ACSL
-
Mus musculus
ACSL1
-
Mus musculus
long-chain acyl coenzyme A synthetase 1
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Mus musculus