World Library  
Flag as Inappropriate
Email this Article


Article Id: WHEBN0035581735
Reproduction Date:

Title: Leumorphin  
Author: World Heritage Encyclopedia
Language: English
Subject: Neoendorphin, DADLE, Amidorphin, Valorphin, Hemorphin-4
Collection: Kappa Agonists, Opioid Peptides
Publisher: World Heritage Encyclopedia


CAS number
Molecular formula C161H236N42O48
Molar mass 3527.85 g/mol
Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)

Leumorphin, also called dynorphin B-29, is a naturally occurring, endogenous opioid peptide.[1][2] Derived as a proteolytic cleavage product of residues 226-254 of prodynorphin (preproenkephalin B),[3][4] leumorphin is a nonacosapeptide (29 amino acids in length) and has the sequence Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr-Arg-Ser-Gln-Glu-Asp-Pro-Asn-Ala-Tyr-Ser-Gly-Glu-Leu-Phe-Asp-Ala. It can be further reduced to dynorphin B (dynorphin B-13) and dynorphin B-14 by pitrilysin metallopeptidase 1 (formerly referred to as "dynorphin-converting enzyme"), an enzyme of the endopeptidase family.[5][6][7] Leumorphin behaves as a potent and selective κ-opioid receptor agonist, similarly to other endogenous opioid peptide derivatives of prodynorphin.[8][9]

See also


  1. ^ Nakao K, Suda M, Sakamoto M, et al. (December 1983). "Leumorphin is a novel endogenous opioid peptide derived from preproenkephalin B". Biochemical and Biophysical Research Communications 117 (3): 695–701.  
  2. ^ Suda M, Nakao K, Sakamoto M, et al. (August 1984). "Leumorphin is a novel endogenous opioid peptide in man". Biochemical and Biophysical Research Communications 123 (1): 148–55.  
  3. ^ Leon F. Tseng (1 September 1995). Pharmacology of Opioid Peptides. CRC Press. p. 171.  
  4. ^ Nock B, Giordano AL, Cicero TJ, O'Connor LH (August 1990). "Affinity of drugs and peptides for U-69,593-sensitive and -insensitive kappa opiate binding sites: the U-69,593-insensitive site appears to be the beta endorphin-specific epsilon receptor". The Journal of Pharmacology and Experimental Therapeutics 254 (2): 412–9.  
  5. ^ Devi L, Gupta P, Fricker LD (January 1991). "Subcellular localization, partial purification, and characterization of a dynorphin processing endopeptidase from bovine pituitary". Journal of Neurochemistry 56 (1): 320–9.  
  6. ^ Berman YL, Juliano L, Devi LA (October 1995). "Purification and characterization of a dynorphin-processing endopeptidase". The Journal of Biological Chemistry 270 (40): 23845–50.  
  7. ^ Mzhavia N, Berman YL, Qian Y, Yan L, Devi LA (May 1999). "Cloning, expression, and characterization of human metalloprotease 1: a novel member of the pitrilysin family of metalloendoproteases". DNA and Cell Biology 18 (5): 369–80.  
  8. ^ Suda M, Nakao K, Yoshimasa T, et al. (September 1984). "Human leumorphin is a potent, kappa opioid receptor agonist". Neuroscience Letters 50 (1-3): 49–52.  
  9. ^ Inenaga K, Nagatomo T, Nakao K, Yanaihara N, Yamashita H (January 1994). "Kappa-selective agonists decrease postsynaptic potentials and calcium components of action potentials in the supraoptic nucleus of rat hypothalamus in vitro". Neuroscience 58 (2): 331–40.  

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.