angiotensin-converting enzyme

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 (ACE) [an″je-o-ten´sin]
a vasoconstrictive substance formed in the blood when renin is released from the juxtaglomerular apparatus in the kidney. The enzymatic action of renin acts on angiotensinogen to form the decapeptide angiotensin I, which is relatively inactive. It in turn is acted upon by peptidases (converting enzymes), chiefly in the lungs, to form the octapeptide angiotensin II, a powerful vasopressor and a stimulator of aldosterone secretion by the adrenal cortex. By its vasopressor action, it raises blood pressure and diminishes fluid loss in the kidney by restricting blood flow. Angiotensin II is hydrolyzed in various tissues to form heptapeptide angiotensin III, which has less vasopressor activity but more effect on the adrenal cortex.
angiotensin-converting enzyme (ACE) an enzyme of the hydrolase class that catalyzes cleavage of a dipeptide from the C-terminal end of angiotensin I to form activated angiotensin II; called also peptidyl-dipeptidase A.
angiotensin-converting enzyme inhibitors competitive inhibitors of angiotensin-converting enzyme, which converts angiotensin I to angiotensin II and inactivates bradykinin. ACE inhibitors, such as captopril, are antagonists of the renin-angiotensin-aldosterone system and potentiators of the kinin system and are used for treatment of hypertension, usually in conjunction with a diuretic. They are also used as vasodilators in the treatment of congestive heart failure.

an·gi·o·ten·sin-con·vert·ing en·zyme (ACE),

A zinc-containing hydrolase cleaving C-terminal dipeptides from a variety of substrates, including angiotensin I, which is converted to angiotensin II and histidylleucine (an important step in the metabolism of certain vasopressor agents). Drugs that inhibit it are used to treat hypertension and congestive heart failure.

angiotensin-converting enzyme

/an·gio·ten·sin-con·vert·ing en·zyme/ (-ten´sin kon-vert´ing en´zīm) see peptidyl-dipeptidase A.

angiotensin-converting enzyme (ACE)

a glycoprotein (dipeptidyl carboxypeptidase) that catalyzes the conversion of angiotensin I to angiotensin II by splitting two terminal amino acids. ACE-inhibiting agents are used for controlling hypertension and for protecting the kidneys in diabetes mellitus.

angiotensin-converting enzyme

Peptidyl-dipeptidase A is the name recommended by the IUBMB for this enzyme (EC, though it is more popularly known as angiotensin I-converting enzyme (ACE).

angiotensin-converting enzyme

A key enzyme in the RAA system, which converts the inactive decapeptide angiotensin I to the octapeptide, angiotensin II, a potent vasoconstrictor that also stimulates aldosterone secretion; ACE is also involved in metabolizing bradykinin Ref range 18–67 U/L, > age 20; those < 20 have higher levels; ACE is ↑ in sarcoidosis, Gaucher disease, leprosy, histoplasmosis, cirrhosis, asbestosis, berylliosis, DM, Hodgkin's disease, hyperthyroidism, amyloidosis, PBC, idiopathic pulmonary fibrosis, PE, scleroderma, silicosis, TB; ACE ↓ in response to prednisone therapy for sarcoidosis. See Renin/angiotensin/aldosterone system.

an·gi·o·ten·sin-con·vert·ing en·zyme

(ACE) (an'jē-ō-ten'sin-kŏn-vĕrt'ing en'zīm)
A hydrolase responsible for the conversion of angiotensin I to the vasoactive angiotensin II by removal of a dipeptide (histidylleucine) from angiotensin I. Drugs that inhibit ACE are used to treat hypertension and congestive heart failure.

angiotensin-converting enzyme

The (ACE) enzyme that converts angiotensin I to the active form angiotensin II. The gene for this enzyme has two alleles, the I allele and the D allele. Research has shown that the I allele is associated with significantly better physical performance, endurance and response to physical training than the D allele. The difference is especially marked if the I allele is present at both loci and compared with people with the D allele at both loci.

angiotensin-converting enzyme (anˑ·jē·ō·ten·sin kon·verˑ·ting enˑ·zīm),

n glycoprotein that converts angiotensin I to angiotensin II by dividing two terminal amino acids.
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References in periodicals archive ?
Peptides with angiotensin I-converting enzyme (ACE) inhibitory activity from defibrinated, hydrolyzed bovine plasma.
Angiotensin I-converting enzyme inhibitory peptides in a hydrolyzed chicken breast muscle extract.
Production of novel angiotensin I-converting enzyme inhibitory peptides by fermentation of marine shrimp Acetes chinensis with Lactobacillus fermentum SM 605.
Bekasem as a potential source of angiotensin I-converting enzyme inhibitor.
Structure-function analysis of angiotensin I-converting enzyme using monoclonal antibodies.
Development of enzyme-linked immunoassays for human angiotensin I-converting enzyme suitable for large-scale studies.
Angiotensin I-converting enzyme inhibitory activities of porcine skeletal muscle proteins following enzyme digestion.
Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects.
A reliable radiometric assay for the determination of angiotensin I-converting enzyme activity in urines.
1) plan to screen a large number of samples for the angiotensin I-converting enzyme polymorphism by CGE, the use of a polyacrylamide-coated capillary and 0.
The aims of the present investigation were to study the effects of added MDCM hydrolysates on the gel properties, oxidative stability, and angiotensin I-converting enzymes (ACE) inhibitory activities of IFP made from Alaska Pollack and spend laying hen meat.

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