Post-translational modifications of lantibiotics
Several newly reported post-translational modification reactions are involved in lantibiotic biosynthesis. A short overview of the present knowledge on the post-translational modifications and on the enzymes involved in lantibiotic biosynthesis is given. The oxidative decarboxylation of the epidermi...
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Veröffentlicht in: | Antonie van Leeuwenhoek 1996-02, Vol.69 (2), p.139-150 |
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description | Several newly reported post-translational modification reactions are involved in lantibiotic biosynthesis. A short overview of the present knowledge on the post-translational modifications and on the enzymes involved in lantibiotic biosynthesis is given. The oxidative decarboxylation of the epidermin precursor peptide EpiA is described in detail. The FMN-containing oxidoreductase EpiD is involved in the formation of the C-terminal S-[(Z)-2-aminovinyl]-D-cysteine residue of epidermin: under reducing conditions the side chain of the C-terminal cysteine residue of EpiA is converted to an enethiol. EpiD has no absolute substrate specificity and can be used for modification of peptides having the C-terminal consensus motif [V/I/L/(M)/F/Y/W]-[A/S/V/T/C/(I/L)]-C. |
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A short overview of the present knowledge on the post-translational modifications and on the enzymes involved in lantibiotic biosynthesis is given. The oxidative decarboxylation of the epidermin precursor peptide EpiA is described in detail. The FMN-containing oxidoreductase EpiD is involved in the formation of the C-terminal S-[(Z)-2-aminovinyl]-D-cysteine residue of epidermin: under reducing conditions the side chain of the C-terminal cysteine residue of EpiA is converted to an enethiol. 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Psychology</topic><topic>Genetics</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Oxidoreductases - isolation & purification</topic><topic>Oxidoreductases - metabolism</topic><topic>Peptide Chain Termination, Translational</topic><topic>Peptides</topic><topic>Protein Processing, Post-Translational</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KUPKE, T</creatorcontrib><creatorcontrib>GÖTZ, F</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Antonie van Leeuwenhoek</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KUPKE, T</au><au>GÖTZ, F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Post-translational modifications of lantibiotics</atitle><jtitle>Antonie van Leeuwenhoek</jtitle><addtitle>Antonie Van Leeuwenhoek</addtitle><date>1996-02-01</date><risdate>1996</risdate><volume>69</volume><issue>2</issue><spage>139</spage><epage>150</epage><pages>139-150</pages><issn>0003-6072</issn><eissn>1572-9699</eissn><coden>ANLEDR</coden><abstract>Several newly reported post-translational modification reactions are involved in lantibiotic biosynthesis. 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subjects | Amino Acid Sequence Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - metabolism Bacteriocins Bacteriology Biological and medical sciences Carboxy-Lyases Decarboxylation Flavoproteins - metabolism Fundamental and applied biological sciences. Psychology Genetics Microbiology Molecular Sequence Data Oxidoreductases - isolation & purification Oxidoreductases - metabolism Peptide Chain Termination, Translational Peptides Protein Processing, Post-Translational |
title | Post-translational modifications of lantibiotics |
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