Characterization of angiotensin I-converting enzyme from anterior gills of the mangrove crab Ucides cordatus

Characterization of angiotensin I-converting enzyme from anterior gills of the mangrove crab Ucides cordatus

Author Bersanetti, Patricia A. Autor UNIFESP Google Scholar
Nogueira, Regina F. Autor UNIFESP Google Scholar
Marcondes, Marcelo F. Autor UNIFESP Google Scholar
Paiva, Paulo B. Autor UNIFESP Google Scholar
Juliano, Maria A. Autor UNIFESP Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Carmona, Adriana K. Autor UNIFESP Google Scholar
Zanotto, Flavia P. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Abstract Angiotensin I-converting enzyme (ACE) is a well-known metallopeptidase that is found in vertebrates, invertebrates and bacteria. We isolated from the anterior gill of the crab Ucides cordatus an isoform of ACE, here named crab-ACE, which presented catalytic properties closely resembling to those of mammalian ACE. the enzyme was purified on Sepharose-lisinopril affinity chromatography to apparent homogeneity and a band of about 72 kDa could be visualized after silver staining and Western blotting. Assays performed with fluorescence resonance energy transfer (FRET) selective ACE substrates Abz-FRK(Dnp)P-OH, Abz-SDK(Dnp)P-OH and Abz-LFK(Dnp)-OH, allowed us to verify that crab-ACE has hydrolytic profile very similar to that of the ACE C-domain. in addition, we observed that crab-ACE can hydrolyze the ACE substrates, angiotensin I and bradykinin. the enzyme was strongly inhibited by the specific ACE inhibitor lisinopril (K-1 of 1.26 nM). However, in contrast to other ACE isoforms, crab-ACE presented a very particular optimum pH, being the substrate Abz-FRK(Dnp)-P-OH hydrolyzed efficiently at pH 9.5. Other interesting characteristic of crab-ACE was that the maximum hydrolytic activity was reached at around 45 degrees C. the description of an ACE isoform in Ucides cordatus is challenging and may contribute to a better understanding of the biochemical function of this enzyme in invertebrates. (C) 2014 Elsevier B.V. All rights reserved.
Keywords Crab gill
ACE isoform
FRET peptides
Language English
Sponsor Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Date 2015-03-01
Published in International Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 74, p. 304-309, 2015.
ISSN 0141-8130 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 304-309
Access rights Closed access
Type Article
Web of Science ID WOS:000351248600040

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