Structural basis of mapping the spontaneous mutations with 5-flurouracil in uracil phosphoribosyltransferase from Mycobacterium tuberculosis
Tuberculosis (TB) remains the second leading cause of death from an infectious disease globally, despite the incessant efforts to control it. Research and development into new TB medicines is imperative for effective TB control; however, new strategies for the rational use of existing drugs, such as...
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Published in | Biochemical and biophysical research communications Vol. 467; no. 3; pp. 577 - 582 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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Elsevier Inc
20.11.2015
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Abstract | Tuberculosis (TB) remains the second leading cause of death from an infectious disease globally, despite the incessant efforts to control it. Research and development into new TB medicines is imperative for effective TB control; however, new strategies for the rational use of existing drugs, such as through the identification of new drug targets, could also significantly enhance this process. Key enzymes involved in the essential metabolic and regulatory pathways are usually sought in the pursuit of potential drug targets. Uracil phosphoribosyltransferase (UPRT) is a key salvage pathway enzyme in the synthesis of uridine 5′-monophosphate (UMP) and a probable target of 5-fluorouracil (5-FU) in Mycobacterium tuberculosis (Mtb). To date, there is no structure available for UPRT from Mtb (MtUPRT) that would assist in the identification of appropriate inhibitors for the enzyme. Here we report the structure of MtUPRT along with its spontaneous mutational studies in the presence of 5-FU. We further mapped these four single nucleotide polymorphisms (SNPs) onto the MtUPRT structure, with two residues found to be conserved among the MtUPRT homologs. Notably, none of these SNPs are located in the 5-FU binding pocket. However, the mutants harboring these mutations showed increased MICs (minimum inhibitory concentration) as compared to wild type strains. The present study will aid in the screening of inhibitors of MtUPRT and thus assist in TB drug design and development. |
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AbstractList | Tuberculosis (TB) remains the second leading cause of death from an infectious disease globally, despite the incessant efforts to control it. Research and development into new TB medicines is imperative for effective TB control; however, new strategies for the rational use of existing drugs, such as through the identification of new drug targets, could also significantly enhance this process. Key enzymes involved in the essential metabolic and regulatory pathways are usually sought in the pursuit of potential drug targets. Uracil phosphoribosyltransferase (UPRT) is a key salvage pathway enzyme in the synthesis of uridine 5'-monophosphate (UMP) and a probable target of 5-fluorouracil (5-FU) in Mycobacterium tuberculosis (Mtb). To date, there is no structure available for UPRT from Mtb (MtUPRT) that would assist in the identification of appropriate inhibitors for the enzyme. Here we report the structure of MtUPRT along with its spontaneous mutational studies in the presence of 5-FU. We further mapped these four single nucleotide polymorphisms (SNPs) onto the MtUPRT structure, with two residues found to be conserved among the MtUPRT homologs. Notably, none of these SNPs are located in the 5-FU binding pocket. However, the mutants harboring these mutations showed increased MICs (minimum inhibitory concentration) as compared to wild type strains. The present study will aid in the screening of inhibitors of MtUPRT and thus assist in TB drug design and development. |
Author | Sivaraman, J. Ghode, Pramila Jobichen, Chacko Ramachandran, Sarath Bifani, Pablo |
Author_xml | – sequence: 1 givenname: Pramila surname: Ghode fullname: Ghode, Pramila organization: Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore – sequence: 2 givenname: Chacko surname: Jobichen fullname: Jobichen, Chacko organization: Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore – sequence: 3 givenname: Sarath surname: Ramachandran fullname: Ramachandran, Sarath organization: Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore – sequence: 4 givenname: Pablo surname: Bifani fullname: Bifani, Pablo organization: Novartis Institute for Tropical Diseases, 10 Biopolis Road, Singapore, 138670, Singapore – sequence: 5 givenname: J. surname: Sivaraman fullname: Sivaraman, J. email: dbsjayar@nus.edu.sg organization: Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore |
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Keywords | 5-fluorouracil (5-FU) Uracil phosphoribosyltransferase (UPRT) upp (Rv3309c) Mycobacterium tuberculosis (Mtb) Spontaneous mutants |
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SubjectTerms | 5-fluorouracil (5-FU) Amino Acid Sequence Fluorouracil - pharmacology Molecular Sequence Data Mutation Mycobacterium tuberculosis Mycobacterium tuberculosis (Mtb) Mycobacterium tuberculosis - enzymology Mycobacterium tuberculosis - genetics Pentosyltransferases - chemistry Pentosyltransferases - genetics Pentosyltransferases - metabolism Sequence Homology, Amino Acid Spontaneous mutants upp (Rv3309c) Uracil phosphoribosyltransferase (UPRT) |
Title | Structural basis of mapping the spontaneous mutations with 5-flurouracil in uracil phosphoribosyltransferase from Mycobacterium tuberculosis |
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