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Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom
journal contribution
posted on 2023-05-16, 17:48 authored by Torres, AM, Tsampazi, M, Kennett, EC, Belov, K, Dominic Geraghty, Bansal, PS, Alewood, PF, Kuchel, PWPlatypus 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).
History
Publication title
Amino AcidsVolume
32Pagination
63-68ISSN
0939-4451Department/School
School of Health SciencesPublisher
SpringerPlace of publication
NewYork, USARights statement
The original publication is available at www.springerlink.comRepository Status
- Restricted