Title |
Mammalian l‐to‐d‐amino‐acid‐residue isomerase from platypus venom
|
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Published in |
Febs Letters, February 2006
|
DOI | 10.1016/j.febslet.2006.01.089 |
Pubmed ID | |
Authors |
Allan M. Torres, Maria Tsampazi, Chryssanthi Tsampazi, Eleanor C. Kennett, Katherine Belov, Dominic P. Geraghty, Paramjit S. Bansal, Paul F. Alewood, Philip W. Kuchel |
Abstract |
The presence of d-amino-acid-containing polypeptides, defensin-like peptide (DLP)-2 and Ornithorhyncus venom C-type natriuretic peptide (OvCNP)b, in platypus venom suggested the existence of a mammalian d-amino-acid-residue isomerase(s) responsible for the modification of the all-l-amino acid precursors. We show here that this enzyme(s) is present in the venom gland extract and is responsible for the creation of DLP-2 from DLP-4 and OvCNPb from OvCNPa. The isomerisation reaction is freely reversible and under well defined laboratory conditions catalyses the interconversion of the DLPs to full equilibration. The isomerase is approximately 50-60 kDa and is inhibited by methanol and the peptidase inhibitor amastatin. This is the first known l-to-d-amino-acid-residue isomerase in a mammal. |
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