These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Biochemical properties of the angiotensin-converting-like enzyme from the leech Theromyzon tessulatum.
    Author: Laurent V, Salzet M.
    Journal: Peptides; 1996; 17(5):737-45. PubMed ID: 8844761.
    Abstract:
    This article reports the evidence and the biochemical properties of an angiotensin-converting (ACE)-like enzyme from head parts of the leech Theromyzon tessulatum. After solubilization from membranes with Triton X-114, the ACE-like enzyme was purified from the detergent-poor fraction. Four steps of purification including gel permeation and anion exchange chromatographies followed by a reversed-phase HPLC were needed. This poor glycosylated peptidyl dipeptidase (of ca. 120 kDa) hydrolyzes, at pH 8.4 and at 37 degrees C, the Phe8-His9 bond of angiotensin I with a high catalytic activity (i.e., K(m): 830 microM and Kcat/K(m): 153 s-1 mM-1). The hydrolysis of angiotensin I is inhibitable at 80% by captopril (IC50 = 175 nM) and lisinopril (IC50 = 35 nM). This activity is strictly dependent on the presence of NaCl and is increased by Zn2+. This zinc metallopeptidase also attacks peptides that have in their sequence either Gly-His, Gly-Phe, or Phe-His bond [e.g., enkephalins (Kcat/K(m): 12 s-1 mM-1) or bradykinin (Kcat/K(m): 2200 s-1 mM-1]. Taken together, these arguments are consistent with an ACE-like activity implicated in metabolism of angiotensins and bradykinin in leeches.
    [Abstract] [Full Text] [Related] [New Search]