{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["6"],"submitter":["Eniyan K"],"pubmed_abstract":["The cell wall of Mycobacterium tuberculosis (Mtb) consists of peptidoglycan, arabinogalactan and mycolic acids. The cytoplasmic steps in the peptidoglycan biosynthetic pathway, catalyzed by the Mur (A-F) enzymes, involve the synthesis of UDP-n-acetylmuramyl pentapeptide, a key precursor molecule required for the formation of the peptidoglycan monomeric building blocks. Mur enzymes are indispensable for cell integrity and their lack of counterparts in eukaryotes suggests them to be promising Mtb drug targets. However, the caveat is that most of the current assays utilize a single Mur enzyme, thereby identifying inhibitors against only one of the enzymes. Here, we report development of a one-pot assay that reconstructs the entire Mtb Mur pathway in vitro and has the advantage of eliminating "],"journal":["Scientific reports"],"pagination":["35134"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5062083"],"repository":["biostudies-literature"],"pubmed_title":["Development of a one-pot assay for screening and identification of Mur pathway inhibitors in Mycobacterium tuberculosis."],"pmcid":["PMC5062083"],"pubmed_authors":["Bajpai U","Rayasam GV","Eniyan K","Perdih A","Kumar A"],"additional_accession":[]},"is_claimable":false,"name":"Development of a one-pot assay for screening and identification of Mur pathway inhibitors in Mycobacterium tuberculosis.","description":"The cell wall of Mycobacterium tuberculosis (Mtb) consists of peptidoglycan, arabinogalactan and mycolic acids. The cytoplasmic steps in the peptidoglycan biosynthetic pathway, catalyzed by the Mur (A-F) enzymes, involve the synthesis of UDP-n-acetylmuramyl pentapeptide, a key precursor molecule required for the formation of the peptidoglycan monomeric building blocks. Mur enzymes are indispensable for cell integrity and their lack of counterparts in eukaryotes suggests them to be promising Mtb drug targets. However, the caveat is that most of the current assays utilize a single Mur enzyme, thereby identifying inhibitors against only one of the enzymes. Here, we report development of a one-pot assay that reconstructs the entire Mtb Mur pathway in vitro and has the advantage of eliminating ","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Oct","modification":"2025-04-21T19:20:54.036Z","creation":"2019-03-27T02:26:33Z"},"accession":"S-EPMC5062083","cross_references":{"pubmed":["27734910"],"doi":["10.1038/srep35134"]}}