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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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2005-03, Vol.102 (12), p.4235-4239 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Jilek, Alexander Mollay, Christa Tippelt, Christa Grassi, Jacques Mignogna, Giuseppina Müllegger, Johannes Sander, Veronika Fehrer, Christine Barra, Donatella Kreil, Günther Steiner, Donald F. |
| description | 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. |
| doi_str_mv | 10.1073/pnas.0500789102 |
| format | Article |
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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.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0500789102</identifier><identifier>PMID: 15758070</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>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</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2005-03, Vol.102 (12), p.4235-4239</ispartof><rights>Copyright 1993/2005 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Mar 22, 2005</rights><rights>Copyright © 2005, The National Academy of Sciences 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c592t-c63b07cfa68b1100d35a761c60d16bbd2b30dae2f18fe465189fe0b31c9e43303</citedby><cites>FETCH-LOGICAL-c592t-c63b07cfa68b1100d35a761c60d16bbd2b30dae2f18fe465189fe0b31c9e43303</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/102/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3374965$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3374965$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,724,777,781,800,882,27906,27907,53773,53775,57999,58232</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15758070$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jilek, Alexander</creatorcontrib><creatorcontrib>Mollay, Christa</creatorcontrib><creatorcontrib>Tippelt, Christa</creatorcontrib><creatorcontrib>Grassi, Jacques</creatorcontrib><creatorcontrib>Mignogna, Giuseppina</creatorcontrib><creatorcontrib>Müllegger, Johannes</creatorcontrib><creatorcontrib>Sander, Veronika</creatorcontrib><creatorcontrib>Fehrer, Christine</creatorcontrib><creatorcontrib>Barra, Donatella</creatorcontrib><creatorcontrib>Kreil, Günther</creatorcontrib><creatorcontrib>Steiner, Donald F.</creatorcontrib><title>Biosynthesis of a D-Amino Acid in Peptide Linkage by an Enzyme from Frog Skin Secretions</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>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.</description><subject>Amino Acid Isomerases - genetics</subject><subject>Amino Acid Isomerases - isolation & purification</subject><subject>Amino Acid Isomerases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Amino Acids - biosynthesis</subject><subject>Amino Acids - chemistry</subject><subject>Amphibian Proteins - chemistry</subject><subject>Amphibian Proteins - metabolism</subject><subject>Animals</subject><subject>Anura - genetics</subject><subject>Anura - metabolism</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Body fluids</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>DNA, Complementary - genetics</subject><subject>Enzyme substrates</subject><subject>Enzymes</subject><subject>Female</subject><subject>Freshwater</subject><subject>Frogs</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - metabolism</subject><subject>Oocytes</subject><subject>Oocytes - enzymology</subject><subject>Orientalism</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Secretion</subject><subject>Sequence Homology, Amino Acid</subject><subject>Skin</subject><subject>Skin - enzymology</subject><subject>Species Specificity</subject><subject>Stereoisomerism</subject><subject>Xenopus laevis</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0UFvFCEYBuCJ0di1evZilHgwXqb9gAGGg4e1tmqyiSbVxBthGGbLdga2MNN0_fWy2U1XPSgXSHheArxF8RzDCQZBT9depxNgAKKWGMiDYoZB4pJXEh4WMwAiyroi1VHxJKUVAEhWw-PiCDORFwJmxY_3LqSNH69scgmFDmn0oZwPzgc0N65FzqOvdj261qKF89d6aVGzQdqjc_9zM1jUxTCgixiW6PI620troh1d8Olp8ajTfbLP9vNx8f3i_NvZp3Lx5ePns_miNEySsTScNiBMp3ndYAzQUqYFx4ZDi3nTtKSh0GpLOlx3tuIM17Kz0FBspK0oBXpcvNudu56awbbG-jHqXq2jG3TcqKCd-nPHuyu1DLeK5UFEzr_Z52O4mWwa1eCSsX2vvQ1TUlywiklG_wux4AS4rDN8_RdchSn6_AmKAK4w45hkdLpDJoaUou3ub4xBbatV22rVodqcePn7Qw9-32UGb_dgmzwcRxQmqiKUqW7q-9HejZm--jfN4sVOrNIY4j2hVFSSM_oLQc3AUA</recordid><startdate>20050322</startdate><enddate>20050322</enddate><creator>Jilek, Alexander</creator><creator>Mollay, Christa</creator><creator>Tippelt, Christa</creator><creator>Grassi, Jacques</creator><creator>Mignogna, Giuseppina</creator><creator>Müllegger, Johannes</creator><creator>Sander, Veronika</creator><creator>Fehrer, Christine</creator><creator>Barra, Donatella</creator><creator>Kreil, Günther</creator><creator>Steiner, Donald F.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20050322</creationdate><title>Biosynthesis of a D-Amino Acid in Peptide Linkage by an Enzyme from Frog Skin Secretions</title><author>Jilek, Alexander ; Mollay, Christa ; Tippelt, Christa ; Grassi, Jacques ; Mignogna, Giuseppina ; Müllegger, Johannes ; Sander, Veronika ; Fehrer, Christine ; Barra, Donatella ; Kreil, Günther ; Steiner, Donald F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c592t-c63b07cfa68b1100d35a761c60d16bbd2b30dae2f18fe465189fe0b31c9e43303</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Isomerases - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jilek, Alexander</au><au>Mollay, Christa</au><au>Tippelt, Christa</au><au>Grassi, Jacques</au><au>Mignogna, Giuseppina</au><au>Müllegger, Johannes</au><au>Sander, Veronika</au><au>Fehrer, Christine</au><au>Barra, Donatella</au><au>Kreil, Günther</au><au>Steiner, Donald F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biosynthesis of a D-Amino Acid in Peptide Linkage by an Enzyme from Frog Skin Secretions</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2005-03-22</date><risdate>2005</risdate><volume>102</volume><issue>12</issue><spage>4235</spage><epage>4239</epage><pages>4235-4239</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><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.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>15758070</pmid><doi>10.1073/pnas.0500789102</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2005-03, Vol.102 (12), p.4235-4239 |
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| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| 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 |
| title | Biosynthesis of a D-Amino Acid in Peptide Linkage by an Enzyme from Frog Skin Secretions |
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