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

Citation

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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The original publication is available at www.springerlink.com

Official URL: http://www.springerlink.com

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

Abstract

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
Downloads:0

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