Search by BoMiProt ID - Bomi75


Primary Information

BoMiProt ID Bomi75
Protein Name Acyl-CoA synthetase long-chain family member 1
Organism Bos taurus
Uniprot IdQ0VCZ8
Milk FractionMFGM, Exosome
Ref Sequence Id NP_001069553.1
Amino Acid Lenth 699
Molecular Weight 78281
Fasta Sequence https://www.uniprot.org/uniprot/Q0VCZ8.fasta
Gene Name ACSL1
Gene Id 537161
Protein Existence Status Unreviewed: Experimental evidence at protein level

Secondry Information

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
Linking IDs Bomi2612
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.