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

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

doi:10.1016/j.febslet.2006.01.089

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

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

Research output: Contribution to journal › Article › peer-review

48 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1587-1591
Number of pages	5
Journal	FEBS Letters
Volume	580
Issue number	6
DOIs	https://doi.org/10.1016/j.febslet.2006.01.089
Publication status	Published - 6 Mar 2006
Externally published	Yes

Keywords

DLP
Peptide isomerase
Platypus venom peptide

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10.1016/j.febslet.2006.01.089

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title = "Mammalian L-to-D-amino-acid-residue isomerase from platypus venom",

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.",

keywords = "DLP, Peptide isomerase, Platypus venom peptide",

author = "Torres, {Allan M.} and Maria Tsampazi and Chryssanthi 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 = "2006",

month = mar,

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doi = "10.1016/j.febslet.2006.01.089",

language = "English",

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T1 - Mammalian L-to-D-amino-acid-residue isomerase from platypus venom

AU - Torres, Allan M.

AU - Tsampazi, Maria

AU - Tsampazi, Chryssanthi

AU - Kennett, Eleanor C.

AU - Belov, Katherine

AU - Geraghty, Dominic P.

AU - Bansal, Paramjit S.

AU - Alewood, Paul F.

AU - Kuchel, Philip W.

PY - 2006/3/6

Y1 - 2006/3/6

N2 - 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.

AB - 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.

KW - DLP

KW - Peptide isomerase

KW - Platypus venom peptide

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DO - 10.1016/j.febslet.2006.01.089

M3 - Article

C2 - 16480722

AN - SCOPUS:33344470537

SN - 0014-5793

VL - 580

SP - 1587

EP - 1591

JO - FEBS Letters

JF - FEBS Letters

IS - 6

ER -

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

Abstract

Keywords

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