| First Author | Abe T | Year | 1992 |
| Journal | J Biochem | Volume | 111 |
| Issue | 1 | Pages | 123-8 |
| PubMed ID | 1607358 | Mgi Jnum | J:549 |
| Mgi Id | MGI:49086 | Doi | 10.1093/oxfordjournals.jbchem.a123707 |
| Citation | Abe T, et al. (1992) Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem 111(1):123-8 |
| abstractText | A complementary DNA clone encoding the entire human long-chain acyl-CoA synthetase was isolated and the total 698-amino acid sequence was deduced. The amino acid sequence of human long-chain acyl-CoA synthetase shows 84.9% identity to that of rat long-chain acyl-CoA synthetase. The nucleotide sequences of the protein coding regions between human and rat long-chain acyl-CoA synthetase mRNAs are highly conserved (85.6%), whereas those of the 3' untranslated regions are less conserved (72%). The location of the human long-chain acyl-CoA synthetase gene was identified on chromosome 4 by spot hybridization of flow-sorted chromosomes. Computer-assisted homology search revealed a significant similarity of the enzyme with the enzymes of the luciferase family. Based on this similarity, the structure of human long-chain acyl-CoA synthetase can be divided into five domains: the N-terminus, two domains similar to those in enzymes of the luciferase family, a long gap region between the similar domains and the C-terminus. |
