Biosynthesis of a D-Amino Acid in Peptide Linkage by an Enzyme from Frog Skin Secretions

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 pep...

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Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 102; no. 12; pp. 4235 - 4239
Main Authors:	Jilek, Alexander, Mollay, Christa, Tippelt, Christa, Grassi, Jacques, Mignogna, Giuseppina, Müllegger, Johannes, Sander, Veronika, Fehrer, Christine, Barra, Donatella, Kreil, Günther, Steiner, Donald F.
Format:	Journal Article
Language:	English
Published:	United States National Academy of Sciences 22-03-2005 National Acad Sciences
Subjects:	Amino Acid Isomerases - genetics Amino Acid Isomerases - isolation & purification Amino Acid Isomerases - metabolism Amino Acid Sequence Amino acids Amino Acids - biosynthesis Amino Acids - chemistry Amphibian Proteins - chemistry Amphibian Proteins - metabolism Animals Anura - genetics Anura - metabolism Base Sequence Biochemistry Biological Sciences Body fluids Cloning, Molecular Complementary DNA DNA, Complementary - genetics Enzyme substrates Enzymes Female Freshwater Frogs Humans Hydrogen-Ion Concentration In Vitro Techniques Kinetics Molecular Sequence Data Oligopeptides - chemistry Oligopeptides - metabolism Oocytes Oocytes - enzymology Orientalism Peptides Proteins Recombinant Proteins - genetics Recombinant Proteins - metabolism Secretion Sequence Homology, Amino Acid Skin Skin - enzymology Species Specificity Stereoisomerism Xenopus laevis
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Summary:	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.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Data deposition: The sequences reported in this paper have been deposited in the GenBank database (accession nos. AY916557, AY916558, and AY916559). Communicated by Donald F. Steiner, University of Chicago, Chicago, IL, February 2, 2005 To whom correspondence may be addressed. E-mail: alexander.jilek@oeaw.ac.at or guenther.kreil@oeaw.ac.at. Abbreviation: d-aIle, d-allo-Ile.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.0500789102