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Structural Determination of Ancovenin, a Peptide Inhibitor of Angiotensin I Converting Enzyme

Authors :
Yoshinobu Motoki
Tateaki Wakamiya
Yasuyuki Ueki
Tetsuo Shiba
Yasuji Kido
Source :
Bulletin of the Chemical Society of Japan. 63:1032-1038
Publication Year :
1990
Publisher :
The Chemical Society of Japan, 1990.

Abstract

The structure of ancovenin, a new peptide inhibitor of angiotensin I converting enzyme was determined chemically. Ancovenin is composed of 16 amino acid residues including three lanthionine residues which form a complex tricyclic structure bridged by sulfide bonds. Moreover, this peptide includes dehydroalanine as one of its unusual amino acids. In the present study, plausible mechanisms of the Edman degradation of dehydroalanine and lanthionine-containing peptides were also elucidated.

Details

ISSN :
13480634 and 00092673
Volume :
63
Database :
OpenAIRE
Journal :
Bulletin of the Chemical Society of Japan
Accession number :
edsair.doi...........9e6e576c789e9638ab4d2d1ed9c0585b
Full Text :
https://doi.org/10.1246/bcsj.63.1032