scholarly journals Homology Modeling and Site-Directed Mutagenesis To Identify Selective Inhibitors of Endothelin-Converting Enzyme-2

2008 ◽  
Vol 51 (12) ◽  
pp. 3378-3387 ◽  
Author(s):  
Khatuna Gagnidze ◽  
Sachchidanand ◽  
Raphael Rozenfeld ◽  
Mihaly Mezei ◽  
Ming-Ming Zhou ◽  
...  
Keyword(s):  
Homology Modeling ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Converting Enzyme ◽  
Selective Inhibitors ◽  
Endothelin Converting Enzyme

Design and Synthesis of Potent, Selective Inhibitors of Endothelin-Converting Enzyme

1998 ◽  
Vol 41 (9) ◽  
pp. 1513-1523 ◽  
Author(s):  
Eli M. Wallace ◽  
John A. Moliterni ◽  
Michael A. Moskal ◽  
Alan D. Neubert ◽  
Nicholas Marcopulos ◽  
...  
Keyword(s):  
Converting Enzyme ◽  
Selective Inhibitors ◽  
Design And Synthesis ◽  
Endothelin Converting Enzyme

Site-directed mutagenesis and homology modeling indicate an important role of cysteine 439 in the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa

Biochimie ◽  
2005 ◽  
Vol 87 (12) ◽  
pp. 1056-1064 ◽  
Author(s):  
Lilian González-Segura ◽  
Roberto Velasco-García ◽  
Enrique Rudiño-Piñera ◽  
Carlos Mújica-Jiménez ◽  
Rosario A. Muñoz-Clares
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Homology Modeling ◽  
Aldehyde Dehydrogenase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Betaine Aldehyde Dehydrogenase ◽  
Betaine Aldehyde ◽  
The Stability

Active site analysis of cis-epoxysuccinate hydrolase from Nocardia tartaricans using homology modeling and site-directed mutagenesis

2011 ◽  
Vol 93 (6) ◽  
pp. 2377-2386 ◽  
Author(s):  
Vinayagam Vasu ◽  
Jayaraman Kumaresan ◽  
Manoharan Ganesh Babu ◽  
Sankaranarayanan Meenakshisundaram
Keyword(s):  
Homology Modeling ◽  
Active Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Site Analysis

scholarly journals The N-terminal segment of endothelin-converting enzyme (ECE)-1b contains a di-leucine motif that can redirect neprilysin to an intracellular compartment in Madin–Darby canine kidney (MDCK) cells

1999 ◽  
Vol 341 (1) ◽  
pp. 119-126 ◽  
Author(s):  
Françoise CAILLER ◽  
Jacques P. ZAPPULLA ◽  
Guy BOILEAU ◽  
Philippe CRINE
Keyword(s):  
Cell Surface ◽  
Mdck Cells ◽  
Intracellular Localization ◽  
Site Directed Mutagenesis ◽  
Converting Enzyme ◽  
Madin Darby Canine Kidney ◽  
Intracellular Compartment ◽  
Endothelin Converting Enzyme ◽  
Darby Canine Kidney ◽  
Canine Kidney

Endothelin-converting enzyme (ECE)-1 is a membrane-bound metallopeptidase of the neprilysin (NEP) family. ECE-1 is responsible for the conversion of inactive big-endothelins into active endothelins. Three different isoforms of human ECE-1 (ECE-1a, ECE-1b and ECE-1c) have been identified. They differ in their N-terminal cytosolic regions, have distinct tissue distribution and intracellular localization. ECE-1a and ECE-1c are both located at the cell surface whereas ECE-1b is targeted to an intracellular compartment. To better understand the nature of the signal responsible for the targeting of ECE-1b to the intracellular compartment, we have constructed several ECE/NEP chimaeric proteins and expressed them by transfection into Madin-Darby canine kidney (MDCK) cells. This allowed us to identify a nine amino acid segment in the cytosolic tail of ECE-1b that is sufficient to relocate NEP from the cell surface to an intracellular compartment. Site-directed mutagenesis on these chimaeras led to the identification of two leucine residues as part of the intracellular retention signal.

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