| Fondo | Angiotensin-converting enzyme (CD143/ACE) is a ~149 kDa protein. Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates. Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins. 1. Naqvi, N. et al. (2005) The Journal of biological chemistry 280, 6669-75. PMID: 156156922. Anthony, CS. et al. (2010) The Journal of biological chemistry 285, 35685-93. PMID: 208268233. Takeuchi, K. et al. (1989) Journal of biochemistry 106, 442-5. PMID: 25581094. Yang, HY. et al. (1970) Biochimica et biophysica acta 214, 374-6. PMID: 43227425. Danilov, S. et al. (1994) The Journal of biological chemistry 269, 26806-14. PMID: 75234126. Jaspard, E. et al. (1993) The Journal of biological chemistry 268, 9496-503. PMID: 76836548. Wei, L. et al. (1992) The Journal of biological chemistry 267, 13398-405. PMID: 13200199. Wei, L. et al. (1991) The Journal of biological chemistry 266, 9002-8. PMID: 185116010. Zou, K. et al. (2009) The Journal of biological chemistry 284, 31914-20. PMID: 19773553 |
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