Non-ribosomal peptide synthetases: Identifying the cryptic gene clusters and decoding the natural product

Journal of biosciences

SANDEEP CHAUDHARY¹  MANGAL SINGH¹  DIPTI SAREEN1¹ 

[1] Department of Biochemistry, Panjab University, Chandigarh, India$$

关键词: Adenylation assay;    genome mining;    MbtH;    natural product;    NRPS;    structure prediction;   

DOI  :  

来源: Indian Academy of Sciences

【 摘 要 】

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.

【 授权许可】

Unknown