Biosynthesis of a D-amino acid in peptide linkage by an enzyme from frog skin secretions

被引:68
作者
Jilek, A
Mollay, C
Tippelt, C
Grassi, J
Mignogna, G
Müllegger, J
Sander, V
Fehrer, C
Barra, D
Kreil, G
机构
[1] Austrian Acad Sci, Inst Mol Biol, A-5020 Salzburg, Austria
[2] Austrian Acad Sci, Inst Biophys & Xray Struct Res, A-8042 Graz, Austria
[3] CEA Saclay, Serv Pharmacol & Immunol, F-91191 Gif Sur Yvette, France
[4] Univ Roma La Sapienza, Dipartimento Sci Biochim, I-00185 Rome, Italy
关键词
amphibia; bombinin H; isomerase; chirality;
D O I
10.1073/pnas.0500789102
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
D-amino acids are present in some peptides from amphibian skin. These residues are derived from the corresponding L-amino acids present in the respective precursors. From skin secretions of Bombinae, we have isolated an enzyme that catalyzes the isomerization of an L-Ile in position 2 of a model peptide to D-allo-Ile. In the course of this reaction, which proceeds without the addition of a cofactor, radioactivity from tritiated water is incorporated into the second position of the product. The amino acid sequence of this isomerase could be deduced from cloned cDNA and genomic DNA. After expression of this cDNA in oocytes of Xenopus laevis, isomerase activity could be detected. Polypeptides related to the frog skin enzyme are present in several vertebrate species, including humans.
引用
收藏
页码:4235 / 4239
页数:5
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