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Met-enkephalin, also known as metenkefalin (INN), sometimes referred to as opioid growth factor (OGF), is a naturally occurring, endogenous opioid peptide that has opioid effects of a relatively short duration. It is one of the two forms of enkephalin, the other being leu-enkephalin. The enkephalins are considered to be the primary endogenous ligands of the δ-opioid receptor, due to their high potency and selectivity for the site over the other endogenous opioids.
Prolyl endopeptidase (PE) also known as prolyl oligopeptidase or post-proline cleaving enzyme is an enzyme that in humans is encoded by the PREP gene.
Neuromedin N is a neuropeptide derived from the same precursor polypeptide as neurotensin, and with similar but subtly distinct expression and effects. Composed of the amino acid sequence Lys-Ile-Pro-Tyr-Ile-Leu, neuromedin N is homologous to neurotensin, both of whose sequences are found on the pro neurotensin/neuromedin N precursor C-terminus. Both sequences of neuromedin N as well as neurotensin are flanked by Lys-Arg amino acids, which comprise a consensus sequence for the endoprotease proprotein convertase. Neuromedin N is primarily synthesized in the neural and intestinal tissues of mammals; in studies performed in mice, neuromedin N's physiological effects were shown to include hypothermia and analgesia, arising from the peptide's ligand association to and interaction with neurotensin type 2 (NTS2) G protein-coupled receptors.
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Gamma-D-glutamyl-meso-diaminopimelate peptidase is an enzyme. This enzyme catalyses the following chemical reaction
Caricain is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
Thimet oligopeptidases, also known as TOPs, are a type of M3 metallopeptidases. These enzymes can be found in animals and plants, showing distinctive functions. In animals and humans, they are involved in the degradation of peptides, such as bradykinin, neurotensin, angiotensin I, and Aβ peptide, helping to regulate physiological processes. In plants, their role is related to the degradation of targeting peptides and the immune response to pathogens through Salicylic Acid (SA)-dependent stress signaling. In Arabidopsis thaliana—recognized as a model plant for scientific studies—two thimet oligopeptidases, known as TOP1 and TOP2, have been identified as targets for salicylic acid binding in the plant. These TOP enzymes are key components to understand the SA-mediated signaling where interactions exist with different components and most of the pathways are unknown.
References
- ↑ Checler F, Vincent JP, Kitabgi P (August 1986). "Purification and characterization of a novel neurotensin-degrading peptidase from rat brain synaptic membranes". The Journal of Biological Chemistry. 261 (24): 11274–81. PMID 3525564.
- ↑ Barelli H, Vincent JP, Checler F (August 1988). "Peripheral inactivation of neurotensin. Isolation and characterization of a metallopeptidase from rat ileum". European Journal of Biochemistry. 175 (3): 481–9. doi: 10.1111/j.1432-1033.1988.tb14220.x . PMID 3409880.
- ↑ Checler F, Barelli H, Vincent JP (January 1989). "Tissue distribution of a novel neurotensin-degrading metallopeptidase. An immunological approach using monospecific polyclonal antibodies". The Biochemical Journal. 257 (2): 549–54. PMC 1135613 . PMID 2649078.
