D‐Amino acid residue in the C‐type natriuretic peptide from the venom of the mammal, Ornithorhynchus anatinus, the Australian platypus

  title={D‐Amino acid residue in the C‐type natriuretic peptide from the venom of the mammal, Ornithorhynchus anatinus, the Australian platypus},
  author={Allan M Torres and Ian R. Menz and Paul F. Alewood and Paramjit S. Bansal and Jelle Lahnstein and Clifford H Gallagher and Philip W. Kuchel},
  journal={FEBS Letters},

D-amino acid residue in a defensin-like peptide from platypus venom: effect on structure and chromatographic properties.

It is shown that DLP-2 (defensin-like peptide-2), a 42-amino-acid residue polypeptide in the platypus venom, also contains a D-aminos acid residue, D-methionine, at position 2, while D LP-4, which has an identical amino acid sequence, has all amino acids in the L-form.

Mammalian l‐to‐d‐amino‐acid‐residue isomerase from platypus venom

Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom

Platypus venom contains an isomerase that reversibly interconverts the second amino-acid residue in some peptides between the L-form and the D-form, and it was found by anion-exchange chromatography to be acidic.

Biogenesis of d‐amino acid containing peptides/proteins: where, when and how?

The different pathways of biogenesis of DAACPs not only in bacteria but also in multicellular organisms are discussed, along with the description of the cellular specificity, the enzyme specificity and the substrate specificity of peptidyl aminoacyl l‐d isomerisation.

Biosynthesis of a D-amino acid in peptide linkage by an enzyme from frog skin secretions.

  • A. JilekC. Mollay G. Kreil
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 2005
From skin secretions of Bombinae, an enzyme is isolated that catalyzes the isomerization of an L-Ile in position 2 of a model peptide to D-allo- Ile, which proceeds without the addition of a cofactor.

Molecular and cellular specificity of post‐translational aminoacyl isomerization in the crustacean hyperglycaemic hormone family

Using antisera specifically recognizing the epimers of CHH and VIH reveals that aminoacyl isomerization occurs in specialized cells of the X’organ–sinus gland neurosecretory system and that the d‐forms of the two neuropeptides are not only present in the same cells, but, importantly, also are co‐packaged within the same secretory vesicles.

D-Amino Acids in Peptides from Animals, Including Human: Occurrence, Structure, Bioactivity and Pharmacology..

  • E. C. Jimenez
  • Biology, Chemistry
    Current protein & peptide science
  • 2020
D-amino acids have been identified in a variety of peptides synthesized by animal cells and the pharmacology and potential medical applications of some of the peptides are explored.

Characterization of D‐amino‐acid‐containing excitatory conotoxins and redefinition of the I‐conotoxin superfamily

Two related peptides are characterized, r11b and r11c, with d‐Phe and d‐Leu at the homologous position, with results indicate that neither the chemical nature of the side chain nor the precise vicinal sequence around the modified residue seem to be critical, but there may be favored loci for isomerization to a d‐amino acid.

Experimental strategies for the analysis of D-amino acid containing peptides in crustaceans: a review.

Aplysia allatotropin-related peptide and its newly identified d-amino acid–containing epimer both activate a receptor and a neuronal target

The results indicate that l- to d-residue isomerization can occur even in an all-l- Residue peptide with a known biological activity and that in some cases, this PTM may help modulate peptide signal lifetime in the extracellular space rather than activity at the cognate receptor.



Evidence for a conformational polymorphism of invertebrate neurohormones. D-amino acid residue in crustacean hyperglycemic peptides.

It is reported here that these isoforms differ by the configuration of a single amino acid residue, which is in either the L- or D-configuration of the lobster hyperglycemic hormones.

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

A D-alanine-containing peptide termed dermorphin, with potent opiate-like activity, has been isolated from skin of the frog Phyllomedusa sauvagei and the existence of a novel post-translational reaction for the conversion of an L-amino acid to its D-isomer is suggested.

Fulicin, a novel neuropeptide containing a D-amino acid residue isolated from the ganglia of Achatina fulica.

Amino acid composition and sequence of dermorphin, a novel opiate-like peptide from the skin of Phyllomedusa sauvagei.

Dermorphin presents striking differences from the known enkephalins; it offers a surprising example of a peptide from Vertebrata containing a D-amino acid residue in its sequence.

l to d Amino Acid Isomerization in a Peptide Hormone Is a Late Post-translational Event Occurring in Specialized Neurosecretory Cells*

For the first time, amino acid isomerization has been shown to occur in the perikarya of fully specialized neurosecretory cells, as a late step of the maturation of the hyperglycemic hormone precursor and after propeptide cleavage, indicating the existence of a new enzyme family involved in the biogenesis of peptide hormones.

d-Amino Acids in Animal Peptides

Summary.Secreted peptides from diverse sources have been found to contain a d-amino acid. From the sequence of cloned mRNAs coding for the precursors of such peptides it could be deduced that in all

Defensin-like peptide-2 from platypus venom: member of a class of peptides with a distinct structural fold.

The three-dimensional structure of DLP-2 was determined by NMR spectroscopy with the aim of gaining insights into the natural function of the DLPs in platypus venom, and the nature of the side chains in this group of peptides is likely to play an important role in defining the biological function(s).