Journal
BIOPOLYMERS
Volume 69, Issue 2, Pages 244-252Publisher
WILEY
DOI: 10.1002/bip.10362
Keywords
angiotensin-I converting enzyme; renin-angiotensin system; zinc binding motifs; NMR; chemical shift index
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We report the design and synthesis through solid phase 9-flourenylmethoxycarbonyl (Fmoc) chemistry of the two angiotensin-I converting enzyme active sites possessing the general sequence HEMGHX(23)EAIGDX(3). Their zinc-binding properties were monitored in solution through high-resolution H-1-NMR. The obtained data were analyzed in terms of chemical shift differences. The results indicate that zinc binds to the HEMGH and the EAIGD characteristic motifs, and suggest possible coordination modes of zinc in the native enzyme. (C) 2003 Wiley Periodicals, Inc.
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