Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Jilek A,Mollay C,Tippelt C,Grassi J,Mignogna G,Müllegger J,Sander V,Fehrer C,Barra D,Kreil Gdoi
10.1073/pnas.0500789102keywords:
subject
Has Abstractpub_date
2005-03-22 00:00:00pages
4235-9issue
12eissn
0027-8424issn
1091-6490pii
0500789102journal_volume
102pub_type
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