Angiotensin-converting enzyme

1O86, 1O8A, 1UZE, 1UZF, 2C6F, 2C6N, 2IUL, 2IUX, 2OC2, 2XY9, 2XYD, 2YDM, 3BKK, 3BKL, 3NXQ, 4APH, 4APJ, 3L3N, 4BXK, 4BZR, 4BZS, 4C2N, 4C2O, 4C2P, 4C2Q, 4C2R, 4CA5, 4CA6, 4UFA, 4UFB, 5AMB, 5AM9, 5AM8, 5AMC, 5AMA163611421ENSG00000159640ENSMUSG00000020681P12821P09470NM_000789NM_001178057NM_152830NM_152831NM_009598NM_207624NM_001281819NP_000780NP_001171528NP_690043NP_001268748NP_033728NP_997507Angiotensin-converting enzyme (EC 3.4.15.1), or ACE, is a central component of the renin–angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. It converts the hormone angiotensin I to the active vasoconstrictor angiotensin II. Therefore, ACE indirectly increases blood pressure by causing blood vessels to constrict. ACE inhibitors are widely used as pharmaceutical drugs for treatment of cardiovascular diseases.ACE is also known by the following names:1o86: CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH LISINOPRIL.1o8a: CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME (NATIVE).1uze: COMPLEX OF THE ANTI-HYPERTENSIVE DRUG ENALAPRILAT AND THE HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME1uzf: COMPLEX OF THE ANTI-HYPERTENSIVE DRUG CAPTOPRIL AN THE HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME2c6f: STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN2c6n: STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN WITH LISINOPRIL2iul: HUMAN TACE G13 MUTANT2iux: HUMAN TACE MUTANT G12342oc2: Structure of testis ACE with RXPA380 Angiotensin-converting enzyme (EC 3.4.15.1), or ACE, is a central component of the renin–angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. It converts the hormone angiotensin I to the active vasoconstrictor angiotensin II. Therefore, ACE indirectly increases blood pressure 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. It is located mainly in the capillaries of the lungs but can also be found in endothelial and kidney epithelial cells. Other less known functions of ACE are degradation of bradykinin and amyloid beta-protein. ACE hydrolyzes peptides by the removal of a dipeptide from the C-terminus. Likewise it converts the inactive decapeptide angiotensin I to the octapeptide angiotensin II by removing the dipeptide His-Leu. Angiotensin II is potent vasoconstrictor in a substrate concentration-dependent manner. Angiotensin II binds to the type 1 angiotensin II receptor (AT1), which sets off a number of actions that result in vasoconstriction and therefore increased blood pressure. ACE is also part of the kinin-kallikrein system where it degrades bradykinin, a potent vasodilator, and other vasoactive peptides. Kininase II is the same as angiotensin-converting enzyme. Thus, the same enzyme (ACE) that generates a vasoconstrictor (ANG II) also disposes of vasodilators (bradykinin). ACE is a zinc metalloenzyme. The zinc ion is essential to its activity, since it directly participates in the catalysis of the peptide hydrolysis. Therefore, ACE can be inhibited by metal-chelating agents. The E384 residue was found to have a dual function. First it acts as a general base to activate water as a nucleophile. Then it acts as a general acid to cleave the C-N bond.