Enkephalinase: Difference between revisions

Latest revision as of 12:37, 31 December 2024

Enkephalinase

Enkephalinase is an enzyme that plays a crucial role in the metabolism of enkephalins, which are endogenous opioid peptides involved in regulating pain and emotion. Enkephalinase is also known as neutral endopeptidase (NEP) or CD10.

Function[edit]

Enkephalinase is a zinc-dependent metalloendopeptidase that cleaves peptide bonds on the amino side of hydrophobic residues. It is primarily responsible for the degradation of enkephalins, which are neurotransmitters that bind to opioid receptors in the central nervous system and peripheral nervous system. By breaking down enkephalins, enkephalinase regulates their activity and duration of action.

Structure[edit]

Enkephalinase is a membrane-bound enzyme that is anchored to the cell membrane via a single transmembrane domain. The active site of the enzyme contains a zinc ion, which is essential for its catalytic activity. The enzyme is composed of several domains, including a large extracellular domain where substrate binding and catalysis occur.

Biological Role[edit]

Enkephalinase is widely distributed in various tissues, including the brain, kidneys, and lungs. In the brain, it modulates the activity of enkephalins, thereby influencing pain perception, mood, and stress response. In the kidneys, enkephalinase is involved in the regulation of blood pressure and sodium balance.

Clinical Significance[edit]

Inhibition of enkephalinase has been explored as a therapeutic strategy for enhancing the effects of enkephalins, particularly in the management of pain and depression. Enkephalinase inhibitors, such as racecadotril, are used to treat diarrhea by reducing the breakdown of enkephalins in the gastrointestinal tract, thereby decreasing intestinal secretion.

Research and Development[edit]

Ongoing research is focused on developing selective enkephalinase inhibitors that can be used to treat various conditions, including chronic pain, hypertension, and heart failure. Understanding the structure and function of enkephalinase is crucial for the design of these inhibitors.

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-Enkephalinase, also known as neutral endopeptidase (NEP), is an enzyme that plays a crucial role in the regulation of various physiological processes in the human body. This article will provide an overview of enkephalinase, its functions, and its significance in different systems.
+{{Infobox enzyme
+| name = Enkephalinase
+| image = <!-- Image of the enzyme, if available -->
+| width = <!-- Width of the image -->
+| caption = <!-- Caption for the image -->
+| EC_number = 3.4.24.11
+| CAS_number = 9079-20-9
+| IUBMB_EC_number = 3/4/24/11
+| GO_code = 0004252
+}}
-== Overview ==
+'''Enkephalinase''' is an enzyme that plays a crucial role in the [[metabolism]] of [[enkephalins]], which are endogenous [[opioid peptides]] involved in regulating [[pain]] and [[emotion]]. Enkephalinase is also known as [[neutral endopeptidase]] (NEP) or [[CD10]].
-Enkephalinase is a type of peptidase enzyme that belongs to the metalloprotease family. It is primarily found in the central nervous system (CNS), as well as in peripheral tissues such as the kidneys, lungs, and intestines. Enkephalinase is responsible for the degradation of enkephalins, which are endogenous opioid peptides involved in pain modulation, mood regulation, and other physiological functions.
-== Functions ==
+==Function==
-Enkephalinase plays a crucial role in the regulation of pain perception. Enkephalins, which are produced in response to painful stimuli, bind to opioid receptors in the CNS, leading to analgesic effects. However, the activity of enkephalinase limits the duration of these effects by breaking down enkephalins into inactive fragments. By regulating the levels of enkephalins, enkephalinase helps maintain the balance between pain relief and pain sensitivity.
+Enkephalinase is a [[zinc]]-dependent [[metalloendopeptidase]] that cleaves peptide bonds on the amino side of hydrophobic residues. It is primarily responsible for the degradation of enkephalins, which are [[neurotransmitters]] that bind to [[opioid receptors]] in the [[central nervous system]] and [[peripheral nervous system]]. By breaking down enkephalins, enkephalinase regulates their activity and duration of action.
-In addition to pain modulation, enkephalinase is involved in various other physiological processes. It is known to regulate blood pressure by degrading vasoactive peptides such as bradykinin and substance P. Enkephalinase also plays a role in the regulation of mood and emotions, as enkephalins are involved in the reward system and the modulation of stress responses.
+==Structure==
+Enkephalinase is a membrane-bound enzyme that is anchored to the [[cell membrane]] via a single transmembrane domain. The active site of the enzyme contains a zinc ion, which is essential for its catalytic activity. The enzyme is composed of several domains, including a large extracellular domain where substrate binding and catalysis occur.
-== Clinical Significance ==
+==Biological Role==
-The activity of enkephalinase has been implicated in several medical conditions. Inhibitors of enkephalinase, such as thiorphan and racecadotril, have been used as therapeutic agents for the treatment of pain and hypertension. These inhibitors increase the levels of enkephalins, leading to prolonged analgesic effects and vasodilation.
+Enkephalinase is widely distributed in various tissues, including the [[brain]], [[kidneys]], and [[lungs]]. In the brain, it modulates the activity of enkephalins, thereby influencing [[pain perception]], [[mood]], and [[stress response]]. In the kidneys, enkephalinase is involved in the regulation of [[blood pressure]] and [[sodium]] balance.
-Enkephalinase inhibitors have also shown potential in the treatment of mood disorders, such as depression and anxiety. By preventing the degradation of enkephalins, these inhibitors enhance the activity of the endogenous opioid system, which is involved in mood regulation.
+==Clinical Significance==
+Inhibition of enkephalinase has been explored as a therapeutic strategy for enhancing the effects of enkephalins, particularly in the management of [[pain]] and [[depression]]. Enkephalinase inhibitors, such as [[racecadotril]], are used to treat [[diarrhea]] by reducing the breakdown of enkephalins in the [[gastrointestinal tract]], thereby decreasing intestinal secretion.
-== References ==
+==Research and Development==
-<references>
+Ongoing research is focused on developing selective enkephalinase inhibitors that can be used to treat various conditions, including [[chronic pain]], [[hypertension]], and [[heart failure]]. Understanding the structure and function of enkephalinase is crucial for the design of these inhibitors.
-  <ref>Smith A, Smith G. Enkephalinase inhibitors: potential therapeutic agents in the treatment of pain. Drugs. 1996;52(3):327-338. doi:10.2165/00003495-199652030-00001</ref>
-  <ref>Roques BP, Noble F, Dauge V, Fournie-Zaluski MC, Beaumont A. Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology. Pharmacol Rev. 1993;45(1):87-146.</ref>
-</references>
-== See Also ==
+==See Also==
-* [[Opioid receptors]]
+* [[Opioid receptor]]
-* [[Endogenous opioids]]
+* [[Endorphin]]
-* [[Pain modulation]]
+* [[Neurotransmitter]]
-* [[Metalloprotease]]
+* [[Metalloendopeptidase]]
+{{Enzymes}}
+{{Opioid system}}
 [[Category:Enzymes]]
-[[Category:Neurochemistry]]
+[[Category:Opioid peptides]]
-[[Category:Physiology]]
+[[Category:Neurotransmitters]]
-[[Category:Pharmacology]]
+[[Category:Metalloenzymes]]
-[[Category:Medical treatments]]