Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
GoGreen Membership

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 9 October 1987:
Vol. 238. no. 4824, pp. 200 - 202
DOI: 10.1126/science.3659910

Articles

Science, Vol 238, Issue 4824, 200-202
Copyright © 1987 by American Association for the Advancement of Science


articles

D-alanine in the frog skin peptide dermorphin is derived from L-alanine in the precursor

K Richter, R Egger, and G Kreil

Molecular Biology Institute, Austrian Academy of Sciences, Salzburg.

A D-alanine-containing peptide termed dermorphin, with potent opiate-like activity, has been isolated from skin of the frog Phyllomedusa sauvagei. Complementary DNA (cDNA) libraries were constructed from frog skin messenger RNA and screened with a mixture of oligonucleotides that contained the codons complementary to five amino acids of dermorphin. Clones were detected with inserts coding for different dermorphin precursors. The predicted amino acid sequences of these precursors contained homologous repeats of 35 amino acids that included one copy of the heptapeptide dermorphin. In these cloned cDNAs, the alanine codon GCG occurred at the position where D-alanine is present in the end product. This suggests the existence of a novel post-translational reaction for the conversion of an L-amino acid to its D-isomer.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Substrate Specificity of Platypus Venom L-to-D-Peptide Isomerase.
P. S. Bansal, A. M. Torres, B. Crossett, K. K. Y. Wong, J. M. S. Koh, D. P. Geraghty, J. I. Vandenberg, and P. W. Kuchel (2008)
J. Biol. Chem. 283, 8969-8975
   Abstract »    Full Text »    PDF »
Biosynthesis of a D-amino acid in peptide linkage by an enzyme from frog skin secretions.
A. Jilek, C. Mollay, C. Tippelt, J. Grassi, G. Mignogna, J. Mullegger, V. Sander, C. Fehrer, D. Barra, and G. Kreil (2005)
PNAS 102, 4235-4239
   Abstract »    Full Text »    PDF »
Post-translational Amino Acid Isomerization: A FUNCTIONALLY IMPORTANT D-AMINO ACID IN AN EXCITATORY PEPTIDE.
O. Buczek, D. Yoshikami, G. Bulaj, E. C. Jimenez, and B. M. Olivera (2005)
J. Biol. Chem. 280, 4247-4253
   Abstract »    Full Text »    PDF »
Cloning and Characterization of Xen-dorphin Prohormone from Xenopus laevis: A NEW OPIOID-LIKE PROHORMONE DISTINCT FROM PROENKEPHALIN AND PRODYNORPHIN.
P. Pattee, A.-E. Ilie, S. Benyhe, G. Toth, A. Borsodi, and S. R. Nagalla (2003)
J. Biol. Chem. 278, 53098-53104
   Abstract »    Full Text »    PDF »
Structure, Synthesis, and Molecular Cloning of Dermaseptins B, a Family of Skin Peptide Antibiotics.
S. Charpentier, M. Amiche, J. Mester, V. Vouille, J.-P. Le Caer, P. Nicolas, and A. Delfour (1998)
J. Biol. Chem. 273, 14690-14697
   Abstract »    Full Text »    PDF »
Contryphan Is a D-Tryptophan-containing Conus Peptide.
E. C. Jimenez, B. M. Olivera, W. R. Gray, and L. J. Cruz (1996)
J. Biol. Chem. 271, 28002-28005
   Abstract »    Full Text »    PDF »
Conversion of L- to D-amino acids: a posttranslational reaction.
G Kreil (1994)
Science 266, 996-997
   PDF »
Functional consequences of posttranslational isomerization of Ser46 in a calcium channel toxin.
S. Heck, C. Siok, K. Krapcho, P. Kelbaugh, P. Thadeio, M. Welch, R. Williams, A. Ganong, M. Kelly, A. Lanzetti, et al. (1994)
Science 266, 1065-1068
   Abstract »    PDF »



ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)