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Mammalian l ‐to‐ d ‐amino‐acid‐residue isomerase from platypus venom
Author(s) -
Torres Allan M.,
Tsampazi Maria,
Tsampazi Chryssanthi,
Kennett Eleanor C.,
Belov Katherine,
Geraghty Dominic P.,
Bansal Paramjit S.,
Alewood Paul F.,
Kuchel Philip W.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.01.089
Subject(s) - isomerase , venom , residue (chemistry) , peptide , biochemistry , chemistry , amino acid , peptide sequence , enzyme , stereochemistry , gene
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 ∼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.