scholarly journals Erratum: Phan, T.T.V., et al. Spontaneous Hinge-Bending Motions of Angiotensin I Converting Enzyme: Role in Activation and Inhibition. Molecules 2020, 25, 1288

Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1508
Author(s):  
Thi Tuong Vy Phan ◽  
Seong-Yeong Heo ◽  
Won-Kyo Jung ◽  
Myunggi Yi
Keyword(s):  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Hinge Bending

The authors wish to make the following corrections to the paper [...]

scholarly journals Molecular and Thermodynamic Mechanisms of the Chloride-dependent Human Angiotensin-I-converting Enzyme (ACE)

2013 ◽  
Vol 289 (3) ◽  
pp. 1798-1814 ◽  
Author(s):  
Christopher J. Yates ◽  
Geoffrey Masuyer ◽  
Sylva L. U. Schwager ◽  
Mohd Akif ◽  
Edward D. Sturrock ◽  
...  
Keyword(s):  
Salt Bridge ◽  
Titration Calorimetry ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Site Analysis ◽  
Angiotensin I Converting Enzyme ◽  
Catalytically Active ◽  
Scissile Bond ◽  
Hinge Bending ◽  
S2 Subsite

Somatic angiotensin-converting enzyme (sACE), a key regulator of blood pressure and electrolyte fluid homeostasis, cleaves the vasoactive angiotensin-I, bradykinin, and a number of other physiologically relevant peptides. sACE consists of two homologous and catalytically active N- and C-domains, which display marked differences in substrate specificities and chloride activation. A series of single substitution mutants were generated and evaluated under varying chloride concentrations using isothermal titration calorimetry. The x-ray crystal structures of the mutants provided details on the chloride-dependent interactions with ACE. Chloride binding in the chloride 1 pocket of C-domain ACE was found to affect positioning of residues from the active site. Analysis of the chloride 2 pocket R522Q and R522K mutations revealed the key interactions with the catalytic site that are stabilized via chloride coordination of Arg522. Substrate interactions in the S2 subsite were shown to affect chloride affinity in the chloride 2 pocket. The Glu403-Lys118 salt bridge in C-domain ACE was shown to stabilize the hinge-bending region and reduce chloride affinity by constraining the chloride 2 pocket. This work demonstrated that substrate composition to the C-terminal side of the scissile bond as well as interactions of larger substrates in the S2 subsite moderate chloride affinity in the chloride 2 pocket of the ACE C-domain, providing a rationale for the substrate-selective nature of chloride dependence in ACE and how this varies between the N- and C-domains.

scholarly journals Spontaneous Hinge-Bending Motions of Angiotensin I Converting Enzyme: Role in Activation and Inhibition

Molecules ◽  
2020 ◽  
Vol 25 (6) ◽  
pp. 1288 ◽  
Author(s):  
Thi Tuong Vy ◽  
Seong-Yeong Heo ◽  
Won-Kyo Jung ◽  
Myunggi Yi
Keyword(s):  
Mechanistic Model ◽  
Enzyme Function ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Treatment Of Hypertension ◽  
Simulation Results ◽  
Dynamics Simulations ◽  
Open States ◽  
Hinge Bending

The inhibition of human angiotensin I converting enzyme (ACE) has been regarded as a promising approach for the treatment of hypertension. Despite research attempts over many years, our understanding the mechanisms of activation and inhibition of ACE is still far from complete. Here, we present results of all atom molecular dynamics simulations of ACE with and without ligands. Two types of inhibitors, competitive and mixed non-competitive, were used to model the ligand bound forms. In the absence of a ligand the simulation showed spontaneous large hinge-bending motions of multiple conversions between the closed and open states of ACE, while the ligand bound forms were stable in the closed state. Our simulation results imply that the equilibrium between pre-existing backbone conformations shifts in the presence of a ligand. The hinge-bending motion of ACE is considered as an essential to the enzyme function. A mechanistic model of activation and the inhibition may provide valuable information for novel inhibitors of ACE.

Relationships between angiotensin I converting enzyme gene polymorphism, plasma levels, and diabetic retinal and renal complications

Diabetes ◽  
1994 ◽  
Vol 43 (3) ◽  
pp. 384-388 ◽  
Author(s):  
M. Marre ◽  
P. Bernadet ◽  
Y. Gallois ◽  
F. Savagner ◽  
T. T. Guyene ◽  
...  
Keyword(s):  
Gene Polymorphism ◽  
Plasma Levels ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Enzyme Gene ◽  
Angiotensin I Converting Enzyme ◽  
Renal Complications

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

2005 ◽  
Vol 10 (3) ◽  
pp. 239-243 ◽  
Author(s):  
Rohan Karawita ◽  
Pyo-Jam park ◽  
Nalin Siriwardhana ◽  
Byong-Tae Jeon ◽  
Sang-Ho Moon ◽  
...  
Keyword(s):  
Cervus Elaphus ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Velvet Antler ◽  
Ace Inhibitory
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