The Hemoregulatory Peptide N-Acetyl-Ser-Asp-Lys-Pro Is a Natural and Specific Substrate of the N-terminal Active Site of Human Angiotensin-converting Enzyme
TL;DR: This is the first report of a highly specific substrate for the N-active site of ACE, with kinetic constants in the range of physiological substrates suggesting that ACE might be involved via its N-terminal active site in the in vivo regulation of the local concentration of this hemoregulatory peptide.
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About: This article is published in Journal of Biological Chemistry. The article was published on 24 Feb 1995. and is currently open access. The article focuses on the topics: Active site & Carboxypeptidase.
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Citations
The angiotensin–converting enzyme gene family: genomics and pharmacology
TL;DR: The gene that encodes collectrin, a homologue of ACEH, is upregulated in response to renal injury, which indicates that there is more to ACE-like function than simple peptide hydrolysis.
422
Acute angiotensin-converting enzyme inhibition increases the plasma level of the natural stem cell regulator N-acetyl-seryl-aspartyl-lysyl-proline.
Michel Azizi,A Rousseau,Eric Ezan,Thanh-Tam Guyene,S Michelet,J M Grognet,M Lenfant,Pierre Corvol,Joël Ménard +8 more
TL;DR: It is demonstrated that Ac-SDKP is the first natural peptide hydrolyzed by the NH2-terminal domain of ACE not only in vitro but also in vivo, confirming that both catalytic sites of ACE are physiologically active.
The renin-angiotensin-aldosterone system and its suppression.
TL;DR: This review focuses on updates in the understanding of the RAAS and the pathophysiology of AngII and aldosterone excess, reviewing what is known about its suppression in cardiovascular and renal diseases, especially in the cat and dog.
Peptidyl dipeptidase A : Angiotensin I-converting enzyme
TL;DR: The tissue distribution and the substrate specificity of peptidyl-dipeptidase A/angiotensin I-converting enzyme is discussed, which belongs to the gluzincin family of metalloproteases of which thermolysin is the prototype.
326
A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme
Kenneth E. Bernstein,Frank S Ong,Wendell-Lamar B. Blackwell,Kandarp H. Shah,Jorge F. Giani,Romer A. Gonzalez-Villalobos,Xiao Z. Shen,Sebastien Fuchs +7 more
TL;DR: Knowing the structural differences between the two ACE domains should allow clinicians to envision new therapies for diseases not currently treated with ACE inhibitors, and these reagents will undoubtedly be powerful tools for probing the physiologic actions of each ACE domain.
310
References
Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung
David W. Cushman,H.S. Cheung +1 more
TL;DR: A sensitive, fixed-time, spectrophotometric assay for angiotensin-converting enzyme measures the rate of production of hippuric acid from hippuryl-L -histidyl- L -leucine (HHL).
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Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning.
Florent Soubrier,François Alhenc-Gelas,Christine Hubert,Jacqueline Allegrini,Marie John,Geoffrey W. Tregear,Pierre Corvol +6 more
TL;DR: The sequence of ACE reveals a high degree of internal homology between two large domains, suggesting that the molecule resulted from a gene duplication, and is consistent with the presence of a single gene for ACE in the haploid human genome.
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A dipeptidyl carboxypeptidase that converts angiotensin i and inactivates bradykinin.
TL;DR: While studying the inactivation of bradykinin, it was noticed that in addition to carboxypeptidase N, a second enzyme, kininase II, cleaved the peptide and liberated the C-terminal phenylalanylarginine dipeptide.
556
Angiotensin I-converting enzyme in human circulating mononuclear cells: genetic polymorphism of expression in T-lymphocytes.
TL;DR: The results show that ACE is expressed in T-lymphocytes and indicate that the level of ACE expression in cells synthesizing the enzyme is genetically determined, which is highly reproducible and influenced by the polymorphism of the ACE gene.
Angiotensin I converting enzyme and the changes in our concepts through the years. Lewis K. Dahl memorial lecture.
TL;DR: The recent molecular cloning of the human enzyme confirmed the existence of a hydrophobic C-terminal peptide that forms the short transmembrane domain of this plasma membrane-bound enzyme.
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