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Literature summary extracted from

  • Soupene, E.; Dinh, N.P.; Siliakus, M.; Kuypers, F.A.
    Activity of the acyl-CoA synthetase ACSL6 isoforms: role of the fatty acid Gate-domains (2010), BMC Biochem., 11, 18.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.2.1.3 additional information specific Gate-domain residues are essential for activity, detailed overview Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.3 ACSL6 isoforms and truncated constructs, splicing variants, sequence organization, overview, expression of His-tagged full-length ACSL6 isoform 2 (F-Gate) and DELTAN-truncated version of isoform 1 (DELTAN-(Y-Gate)) in Escherichia coli strain BL21(DE3) membranes Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
6.2.1.3 F319A site-directed mutagenesis Homo sapiens
6.2.1.3 F319W site-directed mutagenesis Homo sapiens
6.2.1.3 F319Y site-directed mutagenesis Homo sapiens
6.2.1.3 H316L site-directed mutagenesis Homo sapiens
6.2.1.3 L316H site-directed mutagenesis Homo sapiens
6.2.1.3 additional information mutants of full-length ACSL6 isoform 2 (F-Gate) and DELTAN-truncated version of isoform 1 (DELTAN-(Y-Gate)) are obtained by site-directed mutagenesis of the H/L residue pair at position 316 and of the F/Y residue pair at position 319. An ACSL6 construct with a tag at its C-terminus has a far lower activity than a construct with a tag fused to its N-terminus Homo sapiens
6.2.1.3 Y319A site-directed mutagenesis Homo sapiens
6.2.1.3 Y319F site-directed mutagenesis Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.2.1.3 additional information an ACSL6 construct with a tag at its C-terminus has a far lower activity than a construct with a tag fused to its N-terminus Homo sapiens
6.2.1.3 Triton X-100 Inhibition of acyl-CoA formation, inhibits ACSL6 isoform 2 (F-Gate) and its N-terminus truncated version, DELTAN-(F-Gate) Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.2.1.3 plasma membrane isozyme ACSL6 Homo sapiens 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.3 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.3 ATP + acylate + CoA Homo sapiens
-
 AMP + diphosphate + acyl-CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.3 Homo sapiens
-
 isozyme ACSL6
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.3 ATP + acylate + CoA
-
 Homo sapiens AMP + diphosphate + acyl-CoA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.2.1.3 ACSL6
-
 Homo sapiens
6.2.1.3 Acyl-CoA synthetase
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.2.1.3 30
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.3 8
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.3 ATP
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
6.2.1.3 additional information long-chain acyl-CoA synthetase member 6, ASCL6, is a form present in the plasma membrane of cells. Splicing events affecting the N-terminus and alternative motifs near the ATP-binding site generate different isoforms of ACSL6. Alternative fatty acid Gate-domain motifs are essential determinants for the activity of the human ACSL6 isoforms, which appear to act as homodimeric enzyme as well as in complex with other spliced forms. The diversity of these enzyme species can produce the variety of acyl-CoA synthetase activities that are necessary to generate and repair the hundreds of lipid species present in membranes. Oligomeric complex fomations and interactions between isoforms, overview. The N-terminal domain is not essential for oligomer formation Homo sapiens