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

Allan M. Torres; M. Tsampazi; Eleanor C. Kennett; Katherine Belov; Dominic P. Geraghty; Paramjit S. Bansal; Paul F. Alewood; Philip W. Kuchel

doi:10.1007/s00726-006-0346-6

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

Allan M. Torres, M. Tsampazi, Eleanor C. Kennett, Katherine Belov, Dominic P. Geraghty, Paramjit S. Bansal, Paul F. Alewood, Philip W. Kuchel

Research output: Contribution to journal › Article

36 Citations (Scopus)

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 degrees 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).

Original language	English
Pages (from-to)	63-68
Number of pages	6
Journal	Amino Acids
Volume	32
Issue number	1
DOIs	https://doi.org/10.1007/s00726-006-0346-6
Publication status	Published - 2007

Keywords

amino acids
isomerases
peptides
platypus
polypeptides
venom

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10.1007/s00726-006-0346-6

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title = "Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom",

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 degrees 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).",

keywords = "amino acids, isomerases, peptides, platypus, polypeptides, venom",

author = "Torres, {Allan M.} and M. Tsampazi and Kennett, {Eleanor C.} and Katherine Belov and Geraghty, {Dominic P.} and Bansal, {Paramjit S.} and Alewood, {Paul F.} and Kuchel, {Philip W.}",

year = "2007",

doi = "10.1007/s00726-006-0346-6",

language = "English",

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journal = "Amino Acids",

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T1 - Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom

AU - Torres, Allan M.

AU - Tsampazi, M.

AU - Kennett, Eleanor C.

AU - Belov, Katherine

AU - Geraghty, Dominic P.

AU - Bansal, Paramjit S.

AU - Alewood, Paul F.

AU - Kuchel, Philip W.

PY - 2007

Y1 - 2007

N2 - 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 degrees 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).

AB - 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 degrees 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).

KW - amino acids

KW - isomerases

KW - peptides

KW - platypus

KW - polypeptides

KW - venom

UR - http://handle.uws.edu.au:8081/1959.7/37364

U2 - 10.1007/s00726-006-0346-6

DO - 10.1007/s00726-006-0346-6

M3 - Article

SN - 0939-4451

VL - 32

SP - 63

EP - 68

JO - Amino Acids

JF - Amino Acids

IS - 1

ER -

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

Abstract

Keywords

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