Angiotensin I-converting enzyme (ACE) gene structure and polymorphism: Relation to enzyme function and gene expression

Florent Soubrier, Lei Wei, Christine Hubert, Eric Clauser, François Alhenc-Gelas, Pierre Corvol

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Angiotensin I-converting enzyme (ACE; Kininase II, dipeptidyl-carboxy-peptidase I; EC 3.4.15.1) acts primarily as a dipeptidyl carboxypeptidase and is involved in the metabolism of two major vasoactive peptides, angiotensin II and bradykinin. ACE generates the potent vasopressor angiotensin II (AII) by cleaving the C-terminal dipeptide from angiotensin I (AI) and inactivates the vasodepressor bradykinin (BK), by the sequential removal of two C-terminal dipeptides. 1 The most favorable ACE substrate is BK (Km: 0.2 μM) for which the Km is approximately 80 times lower than for AI (Km: 16 μM).

Original languageEnglish (US)
Title of host publicationCellular and Molecular Biology of the Renin-Angiotensin System
PublisherCRC Press
Pages221-242
Number of pages22
ISBN (Electronic)9781351078948
ISBN (Print)9781315891392
DOIs
StatePublished - Jan 1 2018
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Soubrier, F., Wei, L., Hubert, C., Clauser, E., Alhenc-Gelas, F., & Corvol, P. (2018). Angiotensin I-converting enzyme (ACE) gene structure and polymorphism: Relation to enzyme function and gene expression. In Cellular and Molecular Biology of the Renin-Angiotensin System (pp. 221-242). CRC Press. https://doi.org/10.1201/9781351070492