in vivo Mtr knockout strain shows that the enzyme is involved in arsenate (As(V)) resistance suggesting a possible relation with the arsenate reductase activities
cellular mycothiol metabolism, overview. Under stress conditions, proteins are oxidized to mixed disulfides with MSH to form S-mycothiolated proteins that is reversed by the Mrx1/Mtr/MSH pathway
in Mycobacterium tuberculosis, the enzyme is part of a versatile machinery of the mycothiol-dependent system, containing the proteins mycothiol disulfide reductase (Mtr), the oxido-reductase mycoredoxin-1 (Mrx-1) and the alkyl-hydroperoxide subunit E (AhpE), system overview. The mycothiol-dependent protein ensemble regulates the balance of oxidized-reduced mycothiol, to ensure a reductive intracellular environment for optimal functioning of its proteins even uponexposure to oxidative stress
the enzyme maintains intracellular redox homeostasis. The physiological roles of Mtr in resistance to oxidative stresses are corroborated by decreased reactive oxygen species levels, reduced carbonylation damage, decreased loss of reduced protein thiols, and a massive increase in the levels of reversible protein thiols in Mtr-overexpressing cells exposed to stressful conditions
in Mycobacterium tuberculosis, the enzyme is part of a versatile machinery of the mycothiol-dependent system, containing the proteins mycothiol disulfide reductase (Mtr), the oxido-reductase mycoredoxin-1 (Mrx-1) and the alkyl-hydroperoxide subunit E (AhpE), system overview. The mycothiol-dependent protein ensemble regulates the balance of oxidized-reduced mycothiol, to ensure a reductive intracellular environment for optimal functioning of its proteins even uponexposure to oxidative stress
a 5,5'-dithiobis-2-nitrobenzoic acid (DTNB)-coupled assay is developed. The mixed disulfide substrate liberates one molecule of TNB on NADPH-dependent reduction by Mycobacterium tubercolosis reductase. The liberated mycothiol analogue then reacts with DTNB to regenerate the mixed disulfide substrate and another molecule of TNB. Reaction progress can be measured by the increase in absorbance (412 nm) from the two molecules of TNB produced per turn of this catalytic cycle
the enzyme is involved in mycothiol metabolism. Mycothiol may play an important role in the survival and adaption of mycobacteria to oxidative stress caused by normal metabolism, ir induced by the action of anti-tubercular drugs
many naphthoquinones operate as subversive substrates. The native functions of these enzyme involves the NADPH-dependent reduction of disulfide bonds in the substrate. The enzyme-mediated toxicity of quinones/naphthoquinones is a consequence of their enzymatic reduction to semiquinone radicals. The naphthoquinone is then regenerated via the concomitant reduction of oxygen to toxic superoxide anion radicals. In this manner the naphthoquinone substrate is regenerated and the futile redox cycle continues
mycothiol disulfide reductase (Mtr) interacts with the oxido-reductase Mycoredoxin-1 (Mrx-1). the MtMtr-MtMrx-1 interaction is characterized by a fast exchange regime, critical residues by NMR spectroscopy and docking studies, overview
mycothiol disulfide reductase (Mtr) interacts with the oxido-reductase Mycoredoxin-1 (Mrx-1). the MtMtr-MtMrx-1 interaction is characterized by a fast exchange regime, critical residues by NMR spectroscopy and docking studies, overview
the enzyme is involved in mycothiol metabolism. Mycothiol may play an important role in the survival and adaption of mycobacteria to oxidative stress caused by normal metabolism, ir induced by the action of anti-tubercular drugs
mycothiol disulfide reductase (Mtr) interacts with the oxido-reductase Mycoredoxin-1 (Mrx-1). the MtMtr-MtMrx-1 interaction is characterized by a fast exchange regime, critical residues by NMR spectroscopy and docking studies, overview
mycothiol disulfide reductase (Mtr) interacts with the oxido-reductase Mycoredoxin-1 (Mrx-1). the MtMtr-MtMrx-1 interaction is characterized by a fast exchange regime, critical residues by NMR spectroscopy and docking studies, overview
in the presence of 4% (v/v) DMSO, Mycobacterium tubercolosis reductase activity is reduced by only 10%. It is recommended that the DMSO content in sets of inhibition assays should be kept at a constant with 4% (v/v) DMSO as the upper limit
MtMtr is predicted to undergo a mono-to-dimeric equilibrium in solution during catalysis. Enzyme homology structure modelling, the FAD-binding- and interface domain participate in the dimer formation
MtMtr is predicted to undergo a mono-to-dimeric equilibrium in solution during catalysis. Enzyme homology structure modelling, the FAD-binding- and interface domain participate in the dimer formation
overexpression of His6-tagged enzyme from expression vector pXMJ19 in Corynebacterium glutamicum. Transfected cells show increased tolerance to reactive oxygen species induced by oxidants, bactericidal antibiotics, alkylating agents, and heavy metals
overexpression of mycothiol disulfide reductase enhances Corynebacterium glutamicum robustness by modulating cellular redox homeostasis and antioxidant proteins under oxidative stress. Overexpression of Mtr causes a marked increase in the ratio of reduced to oxidized mycothiol (MSH:MSSM), and significantly enhances the activities of a variety of antioxidant enzymes, including mycothiol peroxidase (MPx), mycoredoxin 1 (Mrx1), thioredoxin 1 (Trx1), and methionine sulfoxide reductase A (MsrA). The mycothione levels of enzyme expressing cells are lower than those of untransfectde cells under H2O2, ciprofloxacin, CdCl2, N-ethylmaleimide, iodoacetamide, methylglyoxal, and 1-chloro-2,4-dinitrobenzene stresses, no significant difference in MSH or MSSM levels when both cells are exposed to formaldehyde and rifamycin SV
a DTNB-coupled assay is developed for time-dependent inhibition of Mycobacterium tubercolosis reductase employing a benzyl glycoside analogue of MSH, from which an efficient mixed disulfide substrate is chemically recycled in situ, thereby greatly reducing the substrate quantities needed for such assays
rapid method for the relative quantification of mycothiol using high-sensitivity mass spectrometry with selected ion monitoring. The method uses only minimal sample cleanup, and does not require advanced chromatographic equipment or fluorescent compounds
rapid method for the relative quantification of mycothiol using high-sensitivity mass spectrometry with selected ion monitoring. The method uses only minimal sample cleanup, and does not require advanced chromatographic equipment or fluorescent compounds
Kumar, A.; Nartey, W.; Shin, J.; Manimekalai, M.S.S.; Grueber, G.
Structural and mechanistic insights into mycothiol disulphide reductase and the mycoredoxin-1-alkylhydroperoxide reductase E assembly of Mycobacterium tuberculosis
Overexpression of mycothiol disulfide reductase enhances Corynebacterium glutamicum robustness by modulating cellular redox homeostasis and antioxidant proteins under oxidative stress