Mammalian l‐to‐d‐amino‐acid‐residue isomerase from platypus venom
Mammalian l‐to‐d‐amino‐acid‐residue isomerase from platypus venom
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来自鸭嘴兽毒液的哺乳动物 L-至-D-氨基酸残基异构酶
DOI：
10.1016/j.febslet.2006.01.089
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发表时间：
2006
期刊：
影响因子：
3.5
通讯作者：
P. Kuchel
中科院分区：
文献类型：
--
作者：
A. Torres;Maria Tsampazi;Chryssanthi Tsampazi;E. Kennett;K. Belov;D. Geraghty;P. Bansal;P. Alewood;P. Kuchel
在鸭嘴兽毒中发现含有d-氨基酸的多肽--防御素样肽-2和鸟胸蛇毒C型利钠肽b，提示存在一种哺乳动物的d-氨基酸残基异构酶(S)，负责修饰全L氨基酸前体。我们在这里证明了这种酶(S)存在于毒腺提取物中，并负责从DLP-4产生DLP-2和从OvCNPA产生OvCNPB。异构化反应是自由可逆的，在明确的实验室条件下，催化DLP之间的相互转化达到完全平衡。该异构酶大小为∼50-60 kDa，可被甲醇和肽酶抑制剂阿司他丁抑制。这是已知的哺乳动物中第一个L氨基酸残基异构酶。
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 ∼50–60kDa 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.