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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jbsc/042/01/0175-0187

    • Keywords

       

      Adenylation assay; genome mining; MbtH; natural product; NRPS; structure prediction

    • Abstract

       

      Non-ribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs) present in bacteria and fungi are themajor multi-modular enzyme complexes which synthesize secondary metabolites like the pharmacologically importantantibiotics and siderophores. Each of the multiple modules of an NRPS activates a different amino or aryl acid,followed by their condensation to synthesize a linear or cyclic natural product. The studies on NRPS domains, theknowledge of their gene cluster architecture and tailoring enzymes have helped in the in silico genetic screening of theever-expanding sequenced microbial genomic data for the identification of novel NRPS/PKS clusters and thusdeciphering novel non-ribosomal peptides (NRPs). Adenylation domain is an integral part of the NRPSs and is thesubstrate selecting unit for the final assembled NRP. In some cases, it also requires a small protein, the MbtHhomolog, for its optimum activity. The presence of putative adenylation domain and MbtH homologs in a sequencedgenome can help identify the novel secondary metabolite producers. The role of the adenylation domain in the NRPSgene clusters and its characterization as a tool for the discovery of novel cryptic NRPS gene clusters are discussed.

    • Author Affiliations

       

      MANGAL SINGH1 SANDEEP CHAUDHARY1 DIPTI SAREEN1

      1. Department of Biochemistry, Panjab University, Chandigarh, India
    • Dates

       
  • Journal of Biosciences | News

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