|Protein Name||Acyl-CoA synthetase long-chain family member 1|
|Milk Fraction||MFGM, Exosome|
|Ref Sequence Id||NP_001069553.1|
|Amino Acid Lenth||699|
|Protein Existence Status||Unreviewed: Experimental evidence at protein level|
|Protein Function||activate the major long-chain fatty acids (FAs) of 16–22 carbons; regulate transcription by modulating the intracellular content of FA and acyl-CoA; required for complex lipid synthesis in rapidly growing cells; necessary for fatty acid degradation, phospholipid remodeling, and the production of long acyl-CoA esters that regulate many physiological processes|
|Biochemical Properties||membrane-bound enzymes act on non-polar hydrophobic substrates; as extracted from bovine mammary galnd, purified fatty acid synthetase has a specific activity of 875 _+ 82 (S.E.) units/mg; At 4 ºC, the isolated enzyme was unstable in a 0.25 M potassium phosphate buffer (pH 7.0) 10^-3 M with EDTA and dithiothreitol, but stable in the same buffer at - 95 ºC for at least 2 months; the enzyme was therefore stored at -95ºC; enzyme activity was found to be highly dependent on the presence of NADPH.;|
|Significance in milk||synthesized both long and short chain fatty acids present in milk|
|PTMs||As found in liver and brown adipose tissue of mice, universal Nterminal acetylation, 15 acetylated lysines, and 25 phosphorylation sites on ACSL1 was identified|
|Significance of PTMs||ACSL1 directs its acyl-CoA product towards both triacylglycerol synthesis and β-oxidation in liver, but only towards β-oxidation in adipocytes and heart , it is likely that some of the modifications, rather than altering enzyme activity, might affect ACSL1 protein stability or protein-protein interactions|
|Bibliography||1. Frahm, J. L., Li, L. O., Grevengoed, T. J., & Coleman, R. A. (2011). Phosphorylation and Acetylation of Acyl-Coa Synthetase-I. Journal of Proteomics and Bioinformatics, 4(7), 129–137. https://doi.org/10.4172/jpb.1000180. |
2. Knudsen, J. (1972). Fatty acid synthetase from cow mammary gland tissue cells. Biochimica et Biophysica Acta, 280(3), 408–414. https://doi.org/10.1016/0005-2760(72)90246-9.
3. Soupene, E., Dinh, N. P., Siliakus, M., & Kuypers, F. A. (2010). Activity of the acyl-CoA synthetase ACSL6 isoforms: role of the fatty acid Gate-domains. BMC Biochemistry, 11, 18. https://doi.org/10.1186/1471-2091-11-18.
4. Watkins, P. A., Maiguel, D., Jia, Z., & Pevsner, J. (2007). Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. Journal of Lipid Research, 48(12), 2736–2750. https://doi.org/10.1194/jlr.M700378-JLR200.