Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/38833
Title: Characterization of angiotensin I-converting enzyme from anterior gills of the mangrove crab Ucides cordatus
Authors: Bersanetti, Patricia A. [UNIFESP]
Nogueira, Regina F. [UNIFESP]
Marcondes, Marcelo F. [UNIFESP]
Paiva, Paulo B. [UNIFESP]
Juliano, Maria A. [UNIFESP]
Juliano, Luiz [UNIFESP]
Carmona, Adriana K. [UNIFESP]
Zanotto, Flavia P.
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Keywords: Crab gill
ACE isoform
Characterization
FRET peptides
Issue Date: 1-Mar-2015
Publisher: Elsevier B.V.
Citation: International Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 74, p. 304-309, 2015.
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.
URI: http://repositorio.unifesp.br/handle/11600/38833
ISSN: 0141-8130
Other Identifiers: http://dx.doi.org/10.1016/j.ijbiomac.2014.12.036
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