Proceedings of the National Academy of Sciences - PNAS, 2005-03, Vol.102 (12), p.4235-4239
2005
Details
- Autor(en) / Beteiligte
- Titel
- Biosynthesis of a D-Amino Acid in Peptide Linkage by an Enzyme from Frog Skin Secretions
- Ist Teil von
- Proceedings of the National Academy of Sciences - PNAS, 2005-03, Vol.102 (12), p.4235-4239
- Ort / Verlag
- United States: National Academy of Sciences
- Erscheinungsjahr
- 2005
- Link zum Volltext
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0027-8424eISSN: 1091-6490DOI: 10.1073/pnas.0500789102Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_555527
- Format
- –
- Schlagworte
- 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