Circulating Angiotensin Open Access Journals

Angiotensin-converting enzyme (EC 3.4.15.1), or ACE, may be a central component of the renin–angiotensin system (RAS), which controls vital sign by regulating the quantity of fluids within the body. It converts the hormone angiotensin I to the active vasoconstrictor angiotensin II . Therefore, ACE indirectly increases vital sign by causing blood vessels to constrict. ACE inhibitors are widely used as pharmaceutical drugs for treatment of cardiovascular diseases. The enzyme was discovered by Leonard T. Skeggs Jr. in 1956. The primary crystal structure of human testis ACE was solved within the year 2002 by R. Natesh within the lab of K. Ravi Acharya and therefore the work was published within the journal Nature within the January 2003. It's located mainly within the capillaries of the lungs but also can be found in endothelial and kidney epithelial cells. The function of the chloride ion is extremely complex and is very debated. The anion activation by chloride may be a characteristic feature of ACE. It had been experimentally determined that the activation of hydrolysis by chloride is very hooked in to the substrate. While it increases hydrolysis rates for e.g. Hip-His-Leu it inhibits hydrolysis of other substrates like Hip-Ala-Pro. Under physiological conditions the enzyme reaches about 60% of its maximal activity toward angiotensin I while it reaches its full activity toward bradykinin. it's therefore assumed that the function of the anion activation in ACE provides high substrate specificity. Other theories say that the chloride might simply stabilize the general structure of the enzyme.      

High Impact List of Articles

Relevant Topics in