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


Torres, AM and Tsampazi, M and Kennett, EC and Belov, K and Geraghty, DP and Bansal, PS and Alewood, PF and Kuchel, PW, Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom, Amino Acids, 32, (1) pp. 63-68. ISSN 0939-4451 (2007) [Refereed Article]

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DOI: doi:10.1007/s00726-006-0346-6


Platypus venom contains an isomerase that reversibly interconverts the second amino-acid residue in some peptides between the L-form and the D-form. The enzyme acts on the natriuretic peptides OvCNPa and OvCNPb, and on the defensin-like peptides DLP-2 and DLP-4, but it does not act on DLP-1. While the isomerization of DLP-2 to DLP-4 is inhibited by the amino-peptidase inhibitor amastatin, it is not affected by the leucine amino-peptidase inhibitor bestatin. The enzyme, that is only present in minute quantities in an extract of the venom gland, is thermally stable up to 55 C, and it was found by anion-exchange chromatography to be acidic. Isolation of the isomerase was carried out by combined ion-exchange chromatography and reverse-phase high performance liquid chromatography (HPLC).

Item Details

Item Type:Refereed Article
Keywords:DLP Peptide isomerase Platypus venom peptides
Research Division:Biomedical and Clinical Sciences
Research Group:Medical biochemistry and metabolomics
Research Field:Medical biochemistry - proteins and peptides (incl. medical proteomics)
Objective Division:Environmental Management
Objective Group:Terrestrial systems and management
Objective Field:Terrestrial biodiversity
UTAS Author:Geraghty, DP (Professor Dominic Geraghty)
ID Code:39387
Year Published:2007
Web of Science® Times Cited:30
Deposited By:Health Sciences A
Deposited On:2007-08-01
Last Modified:2012-04-20

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