Critical lysine residue at the chloride binding site of angiotensin converting enzyme

Biochemistry ◽  
1983 ◽  
Vol 22 (23) ◽  
pp. 5315-5321 ◽  
Author(s):  
Robert Shapiro ◽  
James F. Riordan
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Binding Site ◽  
Lysine Residue ◽  
Chloride Binding ◽  
Converting Enzyme

scholarly journals The Potential Role of 6-gingerol and 6-shogaol as ACE Inhibitors in Silico Study

2020 ◽  
Vol 8 (2) ◽  
pp. 210
Author(s):  
Yohanes Bare ◽  
Maria Helvina ◽  
Gabriella Chandrakirana Krisnamurti ◽  
Mansur S
Keyword(s):  
Amino Acid ◽  
Angiotensin Converting Enzyme ◽  
Binding Site ◽  
Potential Role ◽  
Enzyme Inhibitor ◽  
Renin Angiotensin System ◽  
Data Bank ◽  
Amino Acid Residues ◽  
Converting Enzyme

Hypertension has become the third highest cause of death in Indonesia. The condition is correlated with angiotensin-converting enzyme (ACE), and possibly managed with the use of drugs. In addition, some natural compounds, including 6-shogaol and 6-gingerol from ginger, are used to decrease blood pressure. However, the mechanism and binding site of these compounds to ACE protein is currently unclear. This study, therefore, aims to investigate the potential role of these compounds as an angiotensin-converting enzyme inhibitor. The ACE protein was downloaded from Protein Data Bank (PDB) database with the ID: 3bkk, while the 6-shogaol (CID: 5281794) and 6-gingerol (CID: 44559528) ligands were obtained from the PubChem database. Meanwhile, molecular docking was established using HEX 8.0.0 software. The analysis examined the amino acid residues and the bonds formed from these interactions. According to the results, fourteen amino acid residues were formed by the interaction between 6-shogaol and ACE, while the interaction between 6-gingerol and ACE formed eight amino acids. Also, thirteen amino acid residues in the novelty binding site of ACE were discovered to be blocked by the ligands from ginger. Therefore, the compounds have potential roles as inhibitors, and this possibly helps to prevent regulation of the renin-angiotensin system. These interactions also formed hydrogen bonds, as well as electrostatic, unfavorable, and hydrophobic sites, making the binding stronger than others. 

Metal binding to angiotensin converting enzyme: implications for the metal binding site

1986 ◽  
Vol 26 (2) ◽  
pp. 93-106 ◽  
Author(s):  
Stephan G. Kleemann ◽  
Wing Ming Keung ◽  
James F. Riordan
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Binding Site ◽  
Metal Binding ◽  
Converting Enzyme ◽  
Metal Binding Site

Role of Two Chloride-Binding Sites in Functioning of Testicular Angiotensin-Converting Enzyme

2005 ◽  
Vol 70 (10) ◽  
pp. 1167-1172 ◽  
Author(s):  
N. A. Moiseeva ◽  
P. V. Binevski ◽  
I. I. Baskin ◽  
V. A. Palyulin ◽  
O. A. Kost
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Binding Sites ◽  
Chloride Binding ◽  
Converting Enzyme
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