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N-Deacetylation in Lincosamide Biosynthesis Is Catalyzed by a TIdD/PmbA Family Protein

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00533399" target="_blank" >RIV/61388971:_____/20:00533399 - isvavai.cz</a>

  • Result on the web

    <a href="https://pubs.acs.org/doi/abs/10.1021/acschembio.0c00224" target="_blank" >https://pubs.acs.org/doi/abs/10.1021/acschembio.0c00224</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acschembio.0c00224" target="_blank" >10.1021/acschembio.0c00224</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    N-Deacetylation in Lincosamide Biosynthesis Is Catalyzed by a TIdD/PmbA Family Protein

  • Original language description

    Lincosamides are clinically important antibiotics originally produced as microbial specialized metabolites. The complex biosynthesis of lincosamides is coupled to the metabolism of mycothiol as a sulfur donor. Here, we elucidated the N-deacetylation of the mycothiol-derived N-acetyl-L-cysteine residue of a lincosamide intermediate, which is comprised of an amino acid and an aminooctose connected via an amide bond. We purified this intermediate from the culture broth of a deletion mutant strain and tested it as a substrate of recombinant lincosamide biosynthetic proteins in the in vitro assays that were monitored via liquid chromatography-mass spectrometry. Our findings showed that the N-deacetylation reaction is catalyzed by CcbIH/CcbQ or LmbIH/LmbQ proteins in celesticetin and lincomycin biosynthesis, respectively. These are the first N-deacetylases from the TIdD/PmbA protein family, from which otherwise only several proteases and peptidases were functionally characterized. Furthermore, we present a sequence similarity network of TldD/PmbA proteins, which suggests that the lincosamide N-deacetylases are unique among these widely distributed proteins.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10606 - Microbiology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    ACS Chemical Biology

  • ISSN

    1554-8929

  • e-ISSN

    1554-8937

  • Volume of the periodical

    15

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    7

  • Pages from-to

    2048-2054

  • UT code for WoS article

    000563743000004

  • EID of the result in the Scopus database

    2-s2.0-85089786972