Cloning of cDNA encoding a new peptide C-terminal alpha-amidating enzyme having a putative membrane-spanning domain from Xenopus laevis skin
| Autor: | Kayoko Fuchimura, Kazuhiro Ohsuye, Yayoi Wada, Shoji Tanaka, Katsuhiko Kitano, Kensaku Mizuno, Hisayuki Matsuo |
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| Rok vydání: | 1988 |
| Předmět: |
clone (Java method)
Molecular Sequence Data Biophysics DNA Recombinant Peptide Biology Biochemistry Restriction fragment Mixed Function Oxygenases Xenopus laevis Multienzyme Complexes Complementary DNA Sequence Homology Nucleic Acid Animals Amino Acid Sequence RNA Messenger Deoxyribonucleases Type II Site-Specific Molecular Biology Skin Cloning chemistry.chemical_classification Enzyme Precursors Oxidoreductases Acting on CH-NH Group Donors Base Sequence Hybridization probe Cell Membrane Nucleic Acid Hybridization Cell Biology DNA DNA Restriction Enzymes Molecular biology Peptide amidation chemistry biology.protein Peptidylglycine alpha-amidating monooxygenase |
| Zdroj: | Biochemical and biophysical research communications. 150(3) |
| ISSN: | 0006-291X |
| Popis: | A cDNA clone encoding a precursor of a peptide C-terminal alpha-amidating enzyme (AE-I) from Xenopus laevis skin was recently isolated and sequenced in our laboratory. In this study, by using the restriction fragment of this clone as a hybridization probe, we have identified the cDNA encoding another new peptide C-terminal alpha-amidating enzyme (tentatively named AE-II) distinct from AE-I. The cDNA encodes a polypeptide of 875 amino acid residues, which contains a region extensively homologous to AE-I precursor at N-terminus. The encoded protein characteristically has a putative membrane-spanning domain near C-terminus. Our results indicate that C-terminal alpha-amide formation of peptides in Xenopus skin is regulated by at least two distinct alpha-amidating enzymes. |
| Databáze: | OpenAIRE |
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