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- W4238355399 abstract "Summary: Endothelin (ET) is a 21 amino acid peptide produced following the cleavage of its precursor, big ET, by a metalloprotease, the endothelin-converting enzyme (ECE). In the study reported here we determined the minimal peptide sequence of big ET necessary for enzyme recognition and cleavage at the P1-P1' site. Furthermore, we have explored the role of the amino acids found at the boundaries of the cleavage site. To reach these goals, we synthesized a series of fragments, all containing the P1-P1' cleavage site, Trp21-Val22. Following the incubation of peptide fragments with a partly purified bovine ECE preparation and after analyzing the cleavage pattern by high-performance liquid chromatography (HPLC), we were able to identify big ET18-23 amide as the minimal peptide core recognized and cleaved by the enzyme. This hydrolysis was inhibited by phosphoramidon but not by thiorphan, a characteristic of the ECE metalloprotease. However, none of the shorter peptides was able to inhibit the cleavage of big ET-1 by ECE, suggesting that they are not recognized by the enzyme. Particularly, it appears that aspartic acid 18 is a key residue for the recognition phenomenon. The delineation of the minimal structure will be a useful tool to further characterize ECE." @default.
- W4238355399 created "2022-05-12" @default.
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- W4238355399 date "2000-01-01" @default.
- W4238355399 modified "2023-10-16" @default.
- W4238355399 title "New Short Peptide Substrates of Endothelin-Converting Enzyme and Characterization of the Enzyme" @default.
- W4238355399 doi "https://doi.org/10.1097/00005344-200036001-00011" @default.
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