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IUPAC name
Other names
Dynorphin B-29; Dynorphin B (1-29)
3D model (JSmol)
Molar mass 3527.85 g/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references

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[edit]


  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. PMID 6689399. doi:10.1016/0006-291X(83)91653-4. 
  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. PMID 6548137. doi:10.1016/0006-291X(84)90392-9. 
  3. ^ Leon F. Tseng (1 September 1995). Pharmacology of Opioid Peptides. CRC Press. p. 171. ISBN 978-3-7186-5632-5. Retrieved 22 April 2012. 
  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. PMID 2166790. 
  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. PMID 1670956. doi:10.1111/j.1471-4159.1991.tb02598.x. 
  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. PMID 7559562. doi:10.1074/jbc.270.40.23845. 
  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. PMID 10360838. doi:10.1089/104454999315268. 
  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. PMID 6149506. doi:10.1016/0304-3940(84)90460-9. 
  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. PMID 7908725. doi:10.1016/0306-4522(94)90039-6.