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Mammalian L-to-D amino-acid-residue isomerase from platypus venom

Citation

Torres, Am and Tsampazi, M and Tsampazi, C and Kennett, EC and Belov, K and Geraghty, DP and Bansal, PS and Alewood, PF and Kuchel, PW, Mammalian L-to-D amino-acid-residue isomerase from platypus venom, FEBS Letters, 580, (6) pp. 1587-1591. ISSN 0014-5793 (2006) [Refereed Article]

DOI: doi:10.1016/j.febslet.2006.01.089

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 ∼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. © 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Item Details

Item Type:Refereed Article
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:39386
Year Published:2006
Web of Science® Times Cited:42
Deposited By:Health Sciences A
Deposited On:2006-08-01
Last Modified:2007-04-04
Downloads:0

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