Tuberculosis is one of the deadliest diseases worldwide affecting approximately 10 million people in 2018. This classifies tuberculosis as epidemic in several countries and leads to an increasing number of multidrug-resistant strains. Thus, the development of new drugs is essential to effective treatments. A potential drug target is the ribose-5-phosphate isomerase, a ubiquitous enzyme important to nucleotide and cofactor biosynthesis. Here, we report the backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB) that has been performed by triple resonance sequential approach using a [13C, 15N, 2H]-labeled protein. This is the first ribose-5-phosphate isomerase, an enzyme previously classified as highly druggable, to be assigned. These data will be important to further screening studies to find inhibitors and determine their interaction with MtRpiB.
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This work was funded by FAPERJ Grants 239229 and 204432, awarded to FCLA and 225356 awarded to CDAB and CNPq Grant 309564/2017-4, awarded to FCLA. We also thank to INBEB-INCT for funding. LB is funded by CNPq scholarship, CDAB and LFCS is funded by FAPERJ. The authors declare no conflict of interest.
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Bartkevihi, L., Martins, B., de Oliveira, D.M.P. et al. Backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB). Biomol NMR Assign (2020). https://doi.org/10.1007/s12104-020-09931-0
- Mycobacterium tuberculosis
- Pentose phosphate pathway