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

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Summary.

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).

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Torres, A., Tsampazi, M., Kennett, E. et al. Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom. Amino Acids 32, 63–68 (2007). https://doi.org/10.1007/s00726-006-0346-6

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  • DOI: https://doi.org/10.1007/s00726-006-0346-6

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