Determination of the sequence of the arylacetyl acyl-CoA:amino acid N-acyltransferase from bovine liver mitochondria and its homology to the aralkyl acyl-CoA:amino acid N-acyltransferase
| العنوان: | Determination of the sequence of the arylacetyl acyl-CoA:amino acid N-acyltransferase from bovine liver mitochondria and its homology to the aralkyl acyl-CoA:amino acid N-acyltransferase |
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| المؤلفون: | Donald A. Vessey, Eva Lau |
| المصدر: | Journal of Biochemical and Molecular Toxicology. 12:275-279 |
| بيانات النشر: | Wiley, 1998. |
| سنة النشر: | 1998 |
| مصطلحات موضوعية: | Untranslated region, chemistry.chemical_classification, cDNA library, Health, Toxicology and Mutagenesis, General Medicine, Biology, Toxicology, Biochemistry, Homology (biology), Amino acid, chemistry.chemical_compound, chemistry, Complementary DNA, Acyltransferase, Molecular Medicine, Coding region, Cyanogen bromide, Molecular Biology |
| الوصف: | The arylacetyl acyl-CoA:amino acid N-acyltransferase was previously purified to homogeneity from bovine liver mitochondria, and partial sequences were obtained for peptides generated by cyanogen bromide cleavage of the enzyme. One of these sequences was used to design an oligonucleotide probe that was utilized to screen a bovine liver cDNA library. Several clones were isolated and sequenced, and the sequence is given. The cDNA contains 346 bases of 5'-untranslated region and 439 bases of 3' untranslated region. The cDNA codes for an enzyme containing 295 amino acid residues. The sequence gives a molecular weight for the enzyme of 38,937, which is larger than that previously estimated for the functional enzyme, which suggests the existence of ca. 5 kDA of signal peptide. The molecular weight of the enzyme was slightly lower than that of the aralkyltransferase, which was previously determined to be 39,229. Comparison of this sequence with that which we previously obtained for the aralkyltransferase indicated that the coding regions were of identical length and that the sequences were 78% homologous. However, the 5' and 3' untranslated regions had less than 29% homology. The derived amino acid sequences were 71% homologous. This high homology indicates a common origin for the two enzymes. There are, however, significant differences in amino acid compositions, and these are discussed. |
| تدمد: | 1099-0461 1095-6670 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_________::b713822b868351bea9ac5dd93941ce05Test https://doi.org/10.1002Test/(sici)1099-0461(1998)12:5<275::aid-jbt3>3.0.co;2-i |
| حقوق: | CLOSED |
| رقم الانضمام: | edsair.doi...........b713822b868351bea9ac5dd93941ce05 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10990461 10956670 |
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