Backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB).

Biomol NMR Assign

Institute of Medical Biochemistry (IBqM), National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.

Published: April 2020

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 [C, N, H]-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.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s12104-020-09931-0DOI Listing

Publication Analysis

Top Keywords

ribose-5-phosphate isomerase
16
backbone assignment
8
assignment ribose-5-phosphate
8
isomerase mycobacterium
8
mycobacterium tuberculosis
8
tuberculosis mtrpib
8
ribose-5-phosphate
4
isomerase
4
tuberculosis
4
mtrpib tuberculosis
4

Similar Publications

Brucellosis is a highly contagious zoonotic bacterial disease. It has considerable negative consequences on the animal production industry worldwide. The objective of this study was to investigate the genetic and molecular variations in Shami goat susceptible to Brucella infection.

View Article and Find Full Text PDF

The cascade of sugar isomerases is one of the most practical methods for producing rare sugars, and enzyme immobilization endows it with high economic efficiency, operational convenience and reusability. However, the most employed cross-linker glutaraldehyde (GA) has the disadvantages of enzyme deactivation and limitation of substrate binding. Herein, three compounds, glyoxal, GA, and 2,5-furandicarboxaldehyde (DFF) were evaluated within a previously developed cascade comprising ribose-5-phosphate isomerase and D-tagatose-3-epimerase to prepare D-ribulose form D-xylose.

View Article and Find Full Text PDF

In cells, the main enzymes involved in pentose interconversion are ribose-5-phosphate isomerases RpiA and RpiB and ribulose-5-phosphate epimerase Rpe. The inactivation of limits ribose-5-phosphate (R5P) synthesis via the oxidative branch of the pentose phosphate pathway (PPP) and unexpectedly results in antibiotic supersensitivity. This type of metabolism is accompanied by significant changes in the level of reducing equivalents of NADPH and glutathione, as well as a sharp drop in the ATP pool.

View Article and Find Full Text PDF
Article Synopsis
  • Prokaryotes utilize Bacterial Microcompartments (BMCs) to encapsulate metabolic pathways, enhancing enzyme activity for improved catalysis.
  • Sugar Phosphate Utilizing (SPU) BMCs, present in various environments from soils to hot springs, are characterized by their unique enzyme, deoxyribose 5-phosphate aldolase (DERA).
  • This study defines the key features of SPU BMCs, demonstrating the catalytic activity of DERA and its role as a signature enzyme, which could have significant implications for understanding their function and potential biotechnological uses.
View Article and Find Full Text PDF

The immune response to RNA suppresses nucleic acid synthesis by limiting ribose 5-phosphate.

EMBO J

July 2024

Centre for Innate Immunity and Infectious Diseases, Hudson Institute of Medical Research and Department of Molecular and Translational Sciences, Monash University, Clayton, VIC, 3168, Australia.

During infection viruses hijack host cell metabolism to promote their replication. Here, analysis of metabolite alterations in macrophages exposed to poly I:C recognises that the antiviral effector Protein Kinase RNA-activated (PKR) suppresses glucose breakdown within the pentose phosphate pathway (PPP). This pathway runs parallel to central glycolysis and is critical to producing NADPH and pentose precursors for nucleotides.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!