The endopeptidase activity and the activation by Cl− of angiotensin-converting enzyme is evolutionarily conserved: purification and properties of an an angiotensin-converting enzyme from the housefly, Musca domestica
| Autor: | R. E. Isaac, Mohammed Sajid, N S Lamango |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
animal structures
Molecular Sequence Data Bradykinin Angiotensin-Converting Enzyme Inhibitors Peptidyl-Dipeptidase A Sodium Chloride Biochemistry Tripeptidase activity Chromatography Affinity Gonadotropin-Releasing Hormone chemistry.chemical_compound Enzyme activator Endopeptidase activity Houseflies Endopeptidases Fosinoprilat medicine Animals Amino Acid Sequence Molecular Biology Conserved Sequence biology Hydrolysis Captopril Angiotensin-converting enzyme Cell Biology Biological Evolution Endopeptidase Enzyme Activation chemistry biology.protein Peptides Research Article medicine.drug |
| Zdroj: | Biochemical Journal. 314:639-646 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj3140639 |
| Popis: | A soluble 67 kDa angiotensin-converting enzyme (ACE) has been purified by lisinopril-Sepharose affinity column chromatography from adult houseflies, Musca domestica. The dipeptidyl carboxypeptidase activity towards benzoyl-Gly-His-Leu was inhibited by captopril (IC50 50 nM) and fosinoprilat (IC50 251 nM), two inhibitors of mammalian ACE, and was activated by Cl- (optimal Cl- concentration 600 mM). Musca ACE removed C-terminal dipeptides from angiotensin I, bradykinin, [Leu5]enkephalin and [Met5]enkephalin and also functioned as an endopeptidase by hydrolysing dipeptideamides from [Leu5]enkephalinamide and [Met5]enkephalinamide, and a dipeptideamide and a tripeptideamide from substance P. Musca ACE was also able to cleave a tripeptide from both the N-terminus and C-terminus of luteinizing hormone-releasing hormone, with C-terminal hydrolysis predominating. Maximal N-terminal tripeptidase activity occurred at 150 mM NaCl, whereas the C-terminal tripeptidase activity continued to rise with increasing concentration of Cl- (0–0.5 M). Musca ACE displays properties of both the N- and C-domains of human ACE, indicating a high degree of conservation during evolution of the substrate specificity of ACE and its response to Cl-. |
| Databáze: | OpenAIRE |
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