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

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>

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
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology

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

Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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