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Activity of the acyl-CoA synthetase ACSL6 isoforms: role of the fatty acid Gate-domains by Eric Soupene; Nghi Phuong Dinh; Melvin Siliakus; Frans A Kuypers is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Activity of the acyl-CoA synthetase ACSL6 isoforms: role of the fatty acid Gate-domains about?

Background: Activation of fatty acids by acyl-CoA synthetase enzymes is required for de novo lipid synthesis, fatty acid catabolism, and remodeling of biological membranes. Human long-chain acyl-CoA synthetase member 6, ASCL6, is a form present in the plasma membrane of cells. Splicing events affecting the amino-terminus and alternative motifs near the ATP-binding site generate different isoforms of ACSL6. Results: Isoforms with different fatty acid Gate-domain motifs have different activity and the form lacking this domain, isoform 3, showed no detectable activity. Enzymes truncated of the first 40 residues generate acyl-CoAs at a faster rate than the full-length protein. The gating residue, which prevents entry of the fatty acid substrate unless one molecule of ATP has already accessed the catalytic site, was identified as a tyrosine for isoform 1 and a phenylalanine for isoform 2 at position 319. All isoforms, with or without a fatty acid Gate-domain, as well as recombinant protein truncated of the Nterminus, can interact to form enzymatic complexes with identical or different isoforms. ## Conclusion: The alternative fatty acid Gate-domain motifs are essential determinants for t

Who reads Activity of the acyl-CoA synthetase ACSL6 isoforms: role of the fatty acid Gate-domains?

Author

Eric Soupene; Nghi Phuong Dinh; Melvin Siliakus; Frans A Kuypers

Publisher

BioMed Central; Springer (Biomed Central Ltd.); London: BioMed Central; Springer Science and Business Media LLC (ISSN 1471-2091)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)