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  1. AU="Tietzmann, Marcel"
  2. AU="DeRenzo, Christopher"

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  1. Article: Total Synthesis and Biosynthesis of Cyclodepsipeptide Cochinmicin I

    Schnegotzki, Romina / Wiebach, Vincent / Sánchez-Hidalgo, Marina / Tietzmann, Marcel / zur Bonsen, Andreas B. / Genilloud, Olga / Süssmuth, Roderich D.

    Organic letters. 2022 Mar. 21, v. 24, no. 12

    2022  

    Abstract: Phenylglycines are building blocks of many non-ribosomally synthesized peptides. The dihydroxyphenylglycine-containing cyclodepsipeptide cochinmicin I exhibits endothelin receptor antagonist activity. Therefore, it represents an interesting and ... ...

    Abstract Phenylglycines are building blocks of many non-ribosomally synthesized peptides. The dihydroxyphenylglycine-containing cyclodepsipeptide cochinmicin I exhibits endothelin receptor antagonist activity. Therefore, it represents an interesting and synthetically challenging molecule because of the racemization-prone nature of dihydroxyphenylglycine. We present the total synthesis of cochinmicin I and the non-natural derivative cochinmicin VI and describe the identification and assignment of the cochinmicin (cmn) biosynthesis gene cluster, encoding a five-module non-ribosomal peptide synthetase for cochinmicin assembly.
    Keywords antagonists ; biosynthesis ; endothelin receptors ; multigene family ; nonribosomal peptides
    Language English
    Dates of publication 2022-0321
    Size p. 2344-2348.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1523-7052
    DOI 10.1021/acs.orglett.2c00525
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: Total Synthesis and Biosynthesis of Cyclodepsipeptide Cochinmicin I.

    Schnegotzki, Romina / Wiebach, Vincent / Sánchez-Hidalgo, Marina / Tietzmann, Marcel / Zur Bonsen, Andreas B / Genilloud, Olga / Süssmuth, Roderich D

    Organic letters

    2022  Volume 24, Issue 12, Page(s) 2344–2348

    Abstract: Phenylglycines are building blocks of many non-ribosomally synthesized peptides. The dihydroxyphenylglycine-containing cyclodepsipeptide cochinmicin I exhibits endothelin receptor antagonist activity. Therefore, it represents an interesting and ... ...

    Abstract Phenylglycines are building blocks of many non-ribosomally synthesized peptides. The dihydroxyphenylglycine-containing cyclodepsipeptide cochinmicin I exhibits endothelin receptor antagonist activity. Therefore, it represents an interesting and synthetically challenging molecule because of the racemization-prone nature of dihydroxyphenylglycine. We present the total synthesis of cochinmicin I and the non-natural derivative cochinmicin VI and describe the identification and assignment of the cochinmicin (
    MeSH term(s) Depsipeptides ; Multigene Family ; Peptides, Cyclic
    Chemical Substances Depsipeptides ; Peptides, Cyclic ; cochinmicin I (143728-97-6)
    Language English
    Publishing date 2022-03-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1523-7052
    ISSN (online) 1523-7052
    DOI 10.1021/acs.orglett.2c00525
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Dissecting Reactions of Nonlinear Precursor Peptide Processing of the Class III Lanthipeptide Curvopeptin

    Jungmann, Natalia A / Ensle Paul / Krawczyk Bartlomiej / Süssmuth Roderich D / Tietzmann Marcel

    Journal of the American Chemical Society. 2014 Oct. 29, v. 136, no. 43

    2014  

    Abstract: Lanthipeptides are ribosomally synthesized peptides which undergo extensive post-translational modifications. In addition to novel structural features and bioactivities, the in vitro study on the biosynthesis of the class III lanthipeptide ... ...

    Abstract Lanthipeptides are ribosomally synthesized peptides which undergo extensive post-translational modifications. In addition to novel structural features and bioactivities, the in vitro study on the biosynthesis of the class III lanthipeptide labyrinthopeptin revealed a unique C- to N-terminal directionality of biosynthetic processing. The recently described class III lanthipeptide curvopeptin allowed investigating the directionality aspect in much greater detail: Structural characterization of nine curvopeptin biosynthesis intermediates by high-resolution mass spectrometry combined with a deuterium-labeling approach enabled for the first time building a comprehensive biosynthesis model featuring all three post-translational modification reactions: phosphorylation, elimination, and cyclization. These results point to a nonlinear processing scheme with a predominant C → N-terminal directionality. Our data give important mechanistic insights into the concerted processing and directionality of the multifunctional class III modifying enzymes. The data are of significance in the light of obtaining a mechanistic understanding of the post-translational biosynthesis machinery of the growing variety of ribosomally synthesized and post-translationally modified peptides.
    Keywords bioactive properties ; biosynthesis ; enzymes ; in vitro studies ; mass spectrometry ; models ; peptides ; phosphorylation ; post-translational modification
    Language English
    Dates of publication 2014-1029
    Size p. 15222-15228.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021%2Fja5062054
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  4. Article ; Online: Biosynthesis of the Peptide Antibiotic Feglymycin by a Linear Nonribosomal Peptide Synthetase Mechanism.

    Gonsior, Melanie / Mühlenweg, Agnes / Tietzmann, Marcel / Rausch, Saskia / Poch, Annette / Süssmuth, Roderich D

    Chembiochem : a European journal of chemical biology

    2015  Volume 16, Issue 18, Page(s) 2610–2614

    Abstract: Feglymycin, a peptide antibiotic produced by Streptomyces sp. DSM 11171, consists mostly of nonproteinogenic phenylglycine-type amino acids. It possesses antibacterial activity against methicillin-resistant Staphylococcus aureus strains and antiviral ... ...

    Abstract Feglymycin, a peptide antibiotic produced by Streptomyces sp. DSM 11171, consists mostly of nonproteinogenic phenylglycine-type amino acids. It possesses antibacterial activity against methicillin-resistant Staphylococcus aureus strains and antiviral activity against HIV. Inhibition of the early steps of bacterial peptidoglycan synthesis indicated a mode of action different from those of other peptide antibiotics. Here we describe the identification and assignment of the feglymycin (feg) biosynthesis gene cluster, which codes for a 13-module nonribosomal peptide synthetase (NRPS) system. Inactivation of an NRPS gene and supplementation of a hydroxymandelate oxidase mutant with the amino acid l-Hpg proved the identity of the feg cluster. Feeding of Hpg-related unnatural amino acids was not successful. This characterization of the feg cluster is an important step to understanding the biosynthesis of this potent antibacterial peptide.
    MeSH term(s) Anti-Bacterial Agents/analysis ; Anti-Bacterial Agents/biosynthesis ; Anti-Bacterial Agents/chemistry ; Chromatography, High Pressure Liquid ; Mass Spectrometry ; Multigene Family ; Open Reading Frames/genetics ; Peptide Synthases/genetics ; Peptide Synthases/metabolism ; Peptides/analysis ; Peptides/chemistry ; Peptides/metabolism ; Proteins/analysis ; Proteins/chemistry ; Proteins/metabolism ; Streptomyces/enzymology ; Streptomyces/genetics
    Chemical Substances Anti-Bacterial Agents ; Peptides ; Proteins ; feglymycin ; Peptide Synthases (EC 6.3.2.-) ; non-ribosomal peptide synthase (EC 6.3.2.-)
    Language English
    Publishing date 2015-12
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020469-3
    ISSN 1439-7633 ; 1439-4227
    ISSN (online) 1439-7633
    ISSN 1439-4227
    DOI 10.1002/cbic.201500432
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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  5. Article ; Online: Dissecting reactions of nonlinear precursor peptide processing of the class III lanthipeptide curvopeptin.

    Jungmann, Natalia A / Krawczyk, Bartlomiej / Tietzmann, Marcel / Ensle, Paul / Süssmuth, Roderich D

    Journal of the American Chemical Society

    2014  Volume 136, Issue 43, Page(s) 15222–15228

    Abstract: Lanthipeptides are ribosomally synthesized peptides which undergo extensive post-translational modifications. In addition to novel structural features and bioactivities, the in vitro study on the biosynthesis of the class III lanthipeptide ... ...

    Abstract Lanthipeptides are ribosomally synthesized peptides which undergo extensive post-translational modifications. In addition to novel structural features and bioactivities, the in vitro study on the biosynthesis of the class III lanthipeptide labyrinthopeptin revealed a unique C- to N-terminal directionality of biosynthetic processing. The recently described class III lanthipeptide curvopeptin allowed investigating the directionality aspect in much greater detail: Structural characterization of nine curvopeptin biosynthesis intermediates by high-resolution mass spectrometry combined with a deuterium-labeling approach enabled for the first time building a comprehensive biosynthesis model featuring all three post-translational modification reactions: phosphorylation, elimination, and cyclization. These results point to a nonlinear processing scheme with a predominant C → N-terminal directionality. Our data give important mechanistic insights into the concerted processing and directionality of the multifunctional class III modifying enzymes. The data are of significance in the light of obtaining a mechanistic understanding of the post-translational biosynthesis machinery of the growing variety of ribosomally synthesized and post-translationally modified peptides.
    MeSH term(s) Amino Acid Sequence ; Cyclization ; Molecular Sequence Data ; Peptides/chemistry ; Peptides/metabolism ; Phosphorylation ; Protein Processing, Post-Translational ; Ribosomes/metabolism
    Chemical Substances Peptides
    Language English
    Publishing date 2014-10-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/ja5062054
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 4' 55/32: Show issues
    Z 7.3: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

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