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Structure and regulation of rat long-chain acyl-CoA synthetase.
Open accessAbstract
Complementary DNAs encoding rat long-chain acyl-CoA synthetase have been isolated. The cDNAs were identified using synthetic oligonucleotide probes based on partial amino acid sequences of lysyl endopeptidase peptides of the purified enzyme. Rat long-chain acyl-CoA synthetase is predicted to contain 699 amino acid residues and to have a calculated molecular weight of 78,177. Significant sequence similarity was found between parts of long-chain acyl-CoA synthetase and firefly luciferase. Based on the similarity of the reaction mechanisms of the two enzymes, we propose a function for the similar region. The long-chain acyl-CoA synthetase mRNA is expressed in liver, heart, and epididymal adipose tissues and, to a much lesser extent, in brain, small intestine, and lung. The level of long-chain acyl-CoA synthetase mRNA is increased 7-8-fold in rat liver by feeding a diet high in carbohydrate or fat, consistent with the physiological significance of the enzyme in fatty acid metabolism.
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Cites
Rapid similarity searches of nucleic acid and protein data banks.
Wilbur, W. J., & Lipman, D. J. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.3.726 · Cited by 1,546
Cited by
Schoonjans, K., Staels, B., & Auwerx, J. (1996) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42003-6 · Cited by 1,216
Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters
Mosser, J., Douar, A.-M., Sarde, C.-O., Kioschis, P., Feil, R., Moser, H., Poustka, A.-M., Mandel, J.-L., & Aubourg, P. (1993) · Nature · doi:10.1038/361726a0 · Cited by 1,202
Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein
Schaffer, J. E., & Lodish, H. F. (1994) · Cell · doi:10.1016/0092-8674(94)90252-6 · Cited by 872
Kim, H.-J., Takahashi, M., & Ezaki, O. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25892 · Cited by 377
Role of the Gut in Lipid Homeostasis
Abumrad, N. A., & Davidson, N. O. (2012) · Physiological Reviews · doi:10.1152/physrev.00019.2011 · Cited by 355
Metadata
- Authors
- Suzuki, H., Kawarabayasi, Y., Kondo, J., Abe, T., Nishikawa, K., Kimura, S., Hashimoto, T., & Yamamoto, T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-05
- Volume
- 265
- Issue
- 15
- Pages
- 8681-8685
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1570662124
- Cited by
- 357
- References
- 1
- FWCI
- 7.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Suzuki, H., Kawarabayasi, Y., Kondo, J., Abe, T., Nishikawa, K., Kimura, S., Hashimoto, T., & Yamamoto, T. (1990). Structure and regulation of rat long-chain acyl-CoA synthetase. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)38942-2
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