Abstract
Many of the properties of angiotensin I converting enzyme or kininase II (ACE) have been discussed in extenso in the literature. The mode of action of ACE inhibitors has been studied in experimental animals and used clinically in millions of patients. The relatively few side effects have also been amply scrutinized. Nevertheless, some of the basic properties of this enzyme remain unexplained. For instance, although ACE was first considered to be a carboxypeptidase-type enzyme (peptidyl dipeptidase or dipeptidyl carboxypeptidase) (1,2) its actions go beyond cleaving dipep-tides from the free C-terminal end of peptide substrates. ACE inactivates substance P in spite of its blocked C-terminus, primarily by releasing the C-terminal tripeptide Gly-Leu-Met-NH2 (3). The blocked C-terminal tripep-tide, Arg-Pro-Gly-NH2, is also released from the luteinizing hormone releasing hormone (LHRH) (A). ACE, surprisingly, also cleaves the protected the N-terminal tripeptide <Glu -His -Trp from LHRH as well. A mechanism has been proposed (3) for the hydrolysis of C-terminal tripeptides from substrates with blocked C-terminal amino acids.
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© 1989 Plenum Press, New York
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Skidgel, R.A., Erdös, E.G. (1989). Angiotensin I Converting Enzyme. In: Abe, K., Moriya, H., Fujii, S. (eds) Kinins V. Advances in Experimental Medicine and Biology, vol 247 A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9543-4_4
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DOI: https://doi.org/10.1007/978-1-4615-9543-4_4
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