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Related Concept Videos

Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors01:30

Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors

Angiotensin-converting enzyme (ACE), a vital component of the renin-angiotensin-aldosterone system, is abundant in lung endothelial cells. ACE converts the inactive decapeptide, angiotensin I, into the active octapeptide, angiotensin II. This potent vasoconstrictor narrows blood vessels, increasing resistance to blood flow and elevating blood pressure. Angiotensin II also stimulates aldosterone production, encouraging kidney cells to reabsorb more sodium and water from urine, thereby increasing...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Antihypertensive Drugs: Direct Renin Inhibitors01:25

Antihypertensive Drugs: Direct Renin Inhibitors

The renin-angiotensin-aldosterone system (RAAS) is an intricate physiological pathway involving numerous enzymes and hormones, including renin, angiotensin-converting enzyme (ACE), angiotensin I and II, and aldosterone. Imbalances within this system increase the production of angiotensin II and aldosterone. Increased angiotensin II levels promote vasoconstriction and blood pressure elevation. Concurrently, higher aldosterone levels stimulate sodium and water reabsorption in the kidneys,...
Hormonal Regulation01:33

Hormonal Regulation

The renin-aldosterone system is an endocrine system which guides the renal absorption of water and electrolytes, thus managing blood pressure and osmoregulation. Activation of the system begins in the kidneys with a small cluster of cells adjacent to the afferent and efferent blood vessels of the renal corpuscle. As the nephrons are filtering blood, juxtaglomerular cells monitor blood pressure. If they detect a decrease in pressure, they release the hormone renin into the bloodstream.
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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Related Experiment Video

Updated: Jun 16, 2026

Receptor Autoradiography Protocol for the Localized Visualization of Angiotensin II Receptors
12:03

Receptor Autoradiography Protocol for the Localized Visualization of Angiotensin II Receptors

Published on: June 7, 2016

[Angiotensin-converting enzyme: a protein conserved during evolution].

Guillaume Rivière1

  • 1UMR M100 IFREMER/UCBN Physiologie et Ecophysiologie des Mollusques Marins, Université de Caen Basse-Normandie, Bâtiment Sciences C, Campus I, Esplanade de la Paix, 14000 Caen, France. Guillaume.riviere@unicaen.fr

Journal De La Societe De Biologie
|February 4, 2010
PubMed
Summary

Angiotensin-Converting Enzyme (ACE) is ancient, present in bacteria to mammals, suggesting early evolution. Its conserved features across diverse species hint at a long evolutionary specialization from an ancestral protease.

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Nitropeptide Profiling and Identification Illustrated by Angiotensin II
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Nitropeptide Profiling and Identification Illustrated by Angiotensin II

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Live Cell Imaging and 3D Analysis of Angiotensin Receptor Type 1a Trafficking in Transfected Human Embryonic Kidney Cells Using Confocal Microscopy
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Live Cell Imaging and 3D Analysis of Angiotensin Receptor Type 1a Trafficking in Transfected Human Embryonic Kidney Cells Using Confocal Microscopy

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Related Experiment Videos

Last Updated: Jun 16, 2026

Receptor Autoradiography Protocol for the Localized Visualization of Angiotensin II Receptors
12:03

Receptor Autoradiography Protocol for the Localized Visualization of Angiotensin II Receptors

Published on: June 7, 2016

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
07:31

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

Live Cell Imaging and 3D Analysis of Angiotensin Receptor Type 1a Trafficking in Transfected Human Embryonic Kidney Cells Using Confocal Microscopy
09:51

Live Cell Imaging and 3D Analysis of Angiotensin Receptor Type 1a Trafficking in Transfected Human Embryonic Kidney Cells Using Confocal Microscopy

Published on: March 27, 2017

Area of Science:

  • Evolutionary biology
  • Biochemistry
  • Enzymology

Context:

  • Angiotensin-Converting Enzyme (ACE) plays a vital role in mammalian vascular homeostasis.
  • Human ACE has somatic (sACE) and testicular (tACE) isoforms with distinct functions.
  • ACE2, though related, has an antagonistic role.

Purpose:

  • To investigate the evolutionary origins and conserved functions of Angiotensin-Converting Enzyme (ACE).
  • To explore the presence and potential roles of ACE across a wide range of organisms, from bacteria to mammals.

Summary:

  • ACE is found from bacteria to mammals, exhibiting conserved molecular and biochemical features.
  • Its presence in diverse phyla, including invertebrates like leeches, suggests an ancient origin.
  • The enzyme's absence in some eukaryotes might be due to secondary loss, indicating early evolutionary appearance.

Impact:

  • Suggests that mammalian ACE features are a result of long evolutionary specialization of an ancient protease.
  • Highlights the conserved nature of ACE across vast evolutionary distances.
  • Opens avenues for elucidating the original physiological functions of this ancient enzyme.