Cloning and sequence of cDNA encoding a peptide C-terminal alpha-amidating enzyme from Xenopus laevis
| Autor: | Hisayuki Matsuo, Kayoko Fuchimura, Shoji Tanaka, Kazuhiro Ohsuye, Kensaku Mizuno, Yayoi Wada |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
PLCD4
Molecular Sequence Data Biophysics Xenopus Peptidylglycine monooxygenase Biology Biochemistry Mixed Function Oxygenases Xenopus laevis Multienzyme Complexes Complementary DNA Animals Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence Skin chemistry.chemical_classification Base Sequence Cell Biology DNA biology.organism_classification Molecular biology Enzyme Peptide amidation chemistry Oxygenases Peptidylglycine alpha-amidating monooxygenase |
| Zdroj: | Biochemical and biophysical research communications. 148(2) |
| ISSN: | 0006-291X |
| Popis: | The C-terminal alpha-amide formation of the peptides is one of the most important events of prohormone processing. We have recently isolated an alpha-amidating enzyme, AE-I, from Xenopus laevis skin, which is the only enzyme ever purified to homogeneity. In this study, we report cloning and sequence of cDNA encoding AE-I. Our results indicate that enzyme AE-I is initially synthesized as a precursor with 400 amino acid residues, which is further processed to the mature enzyme consisting of 344 residues. Preliminary expression in E. coli of the cDNA corresponding to AE-I was found to produce an enzyme with appreciable alpha-amidating activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|