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2 mycothiol + NADP+
mycothione + NADPH + H+
-
Substrates: -
Products: -
r
2,6-dimethylbenzoquinone + NADPH
?
2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide + NADPH
?
-
Substrates: -
Products: -
?
2-methyl-1,4-naphthoquinone + alpha-NADPH
?
Substrates: -
Products: -
?
5,8-dihydroxy-1,4-naphthoquinone + NADPH
?
Substrates: -
Products: -
?
5-(benzyl 2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside)-dithio-2-nitrobenzoate + NADPH
?
-
Substrates: 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
Products: -
?
5-hydroxy-1,4-naphthoquinone + NADPH
?
7-methyljuglone + NADPH
?
-
Substrates: potent subversive substrate
Products: -
?
8-chloro-5-methoxy-7-methyl-1,4-naphthoquinone + NADPH
?
-
Substrates: -
Products: -
?
AcCys-GlcN + NADPH
?
-
Substrates: -
Products: -
?
AcCys-GlcN-1-O-CH2Ph + NADPH
?
-
Substrates: -
Products: -
?
AcCys-GlcN-1-O-CH3 + NADPH
?
-
Substrates: -
Products: -
?
benzyl 2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide + NADPH
?
-
Substrates: -
Products: -
?
benzyl 2-(N-acetyl-L-cysteinyl)amino-2-deoxy-alpha-D-glucopyranoside disulfide + NADPH
?
-
Substrates: -
Products: -
?
des-myo-inositol mycothione + NADH
?
des-myo-inositol mycothione + reduced beta-nicotinamide hypoxanthine dinucleotide
?
Substrates: -
Products: -
?
des-myo-inositol mycothione + reduced beta-nicotinamide hypoxanthine dinucleotide phosphate
?
Substrates: -
Products: -
?
des-myo-inositol mycothione + thio-NADH
?
Substrates: -
Products: -
?
des-myo-inositol mycothione + thio-NADPH
?
Substrates: -
Products: -
?
desmyoinositol mycothione + NADPH
?
dimeric mycothiol disulfide + NADPH
2 mycothione + H+
-
Substrates: -
Products: -
?
diospyrin + NADPH
?
-
Substrates: subversive substrate
Products: -
?
juglone + NADPH
?
-
Substrates: subversive substrate
Products: -
?
menadione + NADPH
?
-
Substrates: subversive substrate
Products: -
?
methyl 2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide + NADPH
?
-
Substrates: -
Products: -
?
mycothione + NADPH
mycothiol + NADP+
mycothione + NADPH + H+
2 mycothiol + NADP+
mycothione + NADPH + H+
mycothiol + NADP+
-
Substrates: -
Products: -
?
neodiospyrin + NADPH
?
-
Substrates: subversive substrate
Products: -
?
additional information
?
-
2,6-dimethylbenzoquinone + NADPH
?
Substrates: -
Products: -
?
2,6-dimethylbenzoquinone + NADPH
?
Substrates: -
Products: -
?
5-hydroxy-1,4-naphthoquinone + NADPH
?
Substrates: -
Products: -
?
5-hydroxy-1,4-naphthoquinone + NADPH
?
Substrates: -
Products: -
?
des-myo-inositol mycothione + NADH
?
-
Substrates: -
Products: -
?
des-myo-inositol mycothione + NADH
?
Substrates: -
Products: -
?
desmyoinositol mycothione + NADPH
?
Substrates: -
Products: -
?
desmyoinositol mycothione + NADPH
?
Substrates: -
Products: -
?
DTNB + NADPH
?
Substrates: -
Products: -
?
DTNB + NADPH
?
Substrates: -
Products: -
?
mycothione + NADPH
mycothiol + NADP+
-
Substrates: -
Products: -
?
mycothione + NADPH
mycothiol + NADP+
Substrates: -
Products: -
?
mycothione + NADPH
mycothiol + NADP+
Substrates: -
Products: -
?
mycothione + NADPH
mycothiol + NADP+
-
Substrates: 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
Products: -
?
mycothione + NADPH + H+
2 mycothiol + NADP+
-
Substrates: -
Products: -
?
mycothione + NADPH + H+
2 mycothiol + NADP+
-
Substrates: -
Products: -
r
mycothione + NADPH + H+
2 mycothiol + NADP+
-
Substrates: -
Products: -
?
mycothione + NADPH + H+
2 mycothiol + NADP+
Substrates: -
Products: -
?
mycothione + NADPH + H+
2 mycothiol + NADP+
-
Substrates: -
Products: -
?
mycothione + NADPH + H+
2 mycothiol + NADP+
Substrates: -
Products: -
?
mycothione + NADPH + H+
2 mycothiol + NADP+
-
Substrates: -
Products: -
?
mycothione + NADPH + H+
2 mycothiol + NADP+
-
Substrates: -
Products: -
?
SeO32- + NADPH + H+
?
-
Substrates: the enzyme exibits a strong substrate preference for TeO32- over SeO32-
Products: -
?
SeO32- + NADPH + H+
?
-
Substrates: the enzyme exibits a strong substrate preference for TeO32- over SeO32-
Products: -
?
TeO32- + NADPH + H+
?
-
Substrates: the enzyme exibits a strong substrate preference for TeO32- over SeO32-
Products: -
?
TeO32- + NADPH + H+
?
-
Substrates: the enzyme exibits a strong substrate preference for TeO32- over SeO32-
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
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4
2,6-dimethylbenzoquinone
-
0.463
2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide
-
30°C, pH 7.5
0.24
2-methyl-1,4-naphthoquinone
-
0.34
5,8-Dihydroxy-1,4-naphthoquinone
-
0.268
5-(benzyl 2-(N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside)-dithio-2-nitrobenzoate
-
-
0.54
5-hydroxy-1,4-naphthoquinone
-
2.365
7-methyljuglone
-
pH 7.6, 30°C
0.142
8-chloro-5-methoxy-7-methyl-1,4-naphthoquinone
-
pH 7.6, 30°C
0.055
alpha-NADPH
des-myo-inositol mycothione as second substrate
0.438
benzyl 2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide
-
30°C, pH 7.5
0.438
benzyl 2-(N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide
-
-
0.008
beta-NADPH
des-myo-inositol mycothione as second substrate
0.4 - 0.51
des-myo-inositol mycothione
0.118
diospyrin
-
pH 7.6, 30°C
1.088
juglone
-
pH 7.6, 30°C
0.732
menadione
-
pH 7.6, 30°C
0.61
methyl 2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide
-
30°C, pH 7.5
0.043
NADH
des-myo-inositol mycothione as second substrate
0.308
neodiospyrin
-
pH 7.6, 30°C
0.2
reduced beta-nicotinamide hypoxanthine dinucleotide
des-myo-inositol mycothione as second substrate
0.023
reduced beta-nicotinamide hypoxanthine dinucleotide phosphate
des-myo-inositol mycothione as second substrate
0.09
thio-NADH
des-myo-inositol mycothione as second substrate
0.001
thio-NADPH
des-myo-inositol mycothione as second substrate
additional information
additional information
-
0.4
des-myo-inositol mycothione
-
-
0.51
des-myo-inositol mycothione
-
0.073
mycothione
-
0.113
mycothione
-
30°C, pH 7.5
35.23
SeO32-
-
in 20 mM TEA-HCl, at pH 7.6, temperature not specified in the publication
41.14
SeO32-
-
in 20 mM HEPES, at pH 7.0, temperature not specified in the publication
43.9
SeO32-
-
in 20 PBS, at pH 7.4, temperature not specified in the publication
0.413
TeO32-
-
in PBS at pH 7.4, temperature not specified in the publication
-
0.517
TeO32-
-
in 20 mM HEPES, at pH 7.0, temperature not specified in the publication
-
0.779
TeO32-
-
in 20 mM TEA-HCl, at pH 7.6, temperature not specified in the publication
-
additional information
additional information
stopped-flow kinetics
-
additional information
additional information
-
stopped-flow kinetics
-
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malfunction
-
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
metabolism
-
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
physiological function
-
in a mycothione disulfide reductase mutant, mycothiol levels decrease only upon treatment with peroxide
physiological function
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
physiological function
-
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
physiological function
-
in a mycothione disulfide reductase mutant, mycothiol levels decrease only upon treatment with peroxide
-
physiological function
-
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
-
additional information
MtMtr is predicted to undergo a mono-to-dimeric equilibrium in solution during catalysis. Enzyme homology structure modelling
additional information
-
MtMtr is predicted to undergo a mono-to-dimeric equilibrium in solution during catalysis. Enzyme homology structure modelling
additional information
-
MtMtr is predicted to undergo a mono-to-dimeric equilibrium in solution during catalysis. Enzyme homology structure modelling
-
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?
-
x * 49000, SDS-PAGE
?
-
x * 49000, SDS-PAGE
-
dimer
2 * 49800, about, sequence calculation, spectroscopic and dynamic light scattering structure analysis, modelling
dimer
-
2 * 49800, about, sequence calculation, spectroscopic and dynamic light scattering structure analysis, modelling
-
homodimer
alpha2, 2 * 50000, SDS-PAGE
homodimer
-
2 * 49800, apoenzyme in solution, calculated from amino acid sequence
homodimer
-
2 * 49800, apoenzyme in solution, calculated from amino acid sequence
-
homodimer
-
alpha2, 2 * 50000, SDS-PAGE
-
homotetramer
-
4 * 49800, enzyme bound to NADPH, calculated from amino acid sequence
homotetramer
-
4 * 49800, enzyme bound to NADPH, calculated from amino acid sequence
-
additional information
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
additional information
-
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
additional information
-
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
-
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Patel, M.P.; Blanchard, J.S.
Synthesis of des-myo-inositol mycothiol and demonstration of a mycobacterial specific reductase activity
J. Am. Chem. Soc.
120
11538-11539
1998
Mycobacterium tuberculosis
-
brenda
Patel, M.P.; Blanchard, J.S.
Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase
Biochemistry
38
11827-11833
1999
Mycobacterium tuberculosis (P9WHH3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WHH3)
brenda
Patel, M.P.; Blanchard, J.S.
Mycobacterium tuberkulosis mycothione reductase: pH dependence of the kinetic parameters and kinetic isotope effects
Biochemistry
40
5119-5126
2001
Mycobacterium tuberculosis
brenda
Hayward, D.; Wiid, I.; van Helden, P.
Differential expression of mycothiol pathway genes: are they affected by antituberculosis drugs?
IUBMB Life
56
131-138
2004
Mycobacterium tuberculosis variant bovis
brenda
Mahapatra, A.; Mativandlela, S.P.; Binneman, B.; Fourie, P.B.; Hamilton, C.J.; Meyer, J.J.; van der Kooy, F.; Houghton, P.; Lall, N.
Activity of 7-methyljuglone derivatives against Mycobacterium tuberculosis and as subversive substrates for mycothiol disulfide reductase
Bioorg. Med. Chem.
15
7638-7646
2007
Mycobacterium tuberculosis
brenda
Newton, G.L.; Buchmeier, N.; Fahey, R.C.
Biosynthesis and functions of mycothiol, the unique protective thiol of actinobacteria
Microbiol. Mol. Biol. Rev.
72
471-494
2008
Mycobacterium tuberculosis
brenda
Stewart, M.J.; Jothivasan, V.K.; Rowan, A.S.; Wagg, J.; Hamilton, C.J.
Mycothiol disulfide reductase: solid phase synthesis and evaluation of alternative substrate analogues
Org. Biomol. Chem.
6
385-390
2008
Mycobacterium tuberculosis
brenda
Ordonez, E.; Van Belle, K.; Roos, G.; De Galan, S.; Letek, M.; Gil, J.A.; Wyns, L.; Mateos, L.M.; Messens, J.
Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchange
J. Biol. Chem.
284
15107-15116
2009
Corynebacterium glutamicum
brenda
Hamilton, C.J.; Finlay, R.M.; Stewart, M.J.; Bonner, A.
Mycothiol disulfide reductase: A continuous assay for slow time-dependent inhibitors
Anal. Biochem.
388
91-96
2009
Mycobacterium tuberculosis
brenda
Holsclaw, C.M.; Muse, W.B.; Carroll, K.S.; Leary, J.A.
Mass Spectrometric Analysis of Mycothiol levels in wild-type and mycothiol disulfide reductase mutant Mycobacterium smegmatis
Int. J. Mass Spectrom.
305
151-156
2011
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
brenda
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
Biochim. Biophys. Acta
1861
2354-2366
2017
Mycobacterium tuberculosis (P9WHH3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WHH3)
brenda
Si, M.; Zhao, C.; Zhang, B.; Wei, D.; Chen, K.; Yang, X.; Xiao, H.; Shen, X.
Overexpression of mycothiol disulfide reductase enhances Corynebacterium glutamicum robustness by modulating cellular redox homeostasis and antioxidant proteins under oxidative stress
Sci. Rep.
6
29491
2016
Corynebacterium glutamicum
brenda
Liu, Y.; Li, X.; Luo, J.; Su, T.; Si, M.; Chen, C.
A novel mycothiol-dependent thiol-disulfide reductase in Corynebacterium glutamicum involving oxidative stress resistance
3 Biotech
11
372
2021
Corynebacterium glutamicum
brenda
Kumar, A.; Subramanian Manimekalai, M.S.; Grueber, G.
Substrate-induced structural alterations of Mycobacterial mycothione reductase and critical residues involved
FEBS Lett.
592
568-585
2018
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Butz, Z.J.; Hendricks, A.; Borgognoni, K.; Ackerson, C.J.
Identification of a TeO32- reductase/mycothione reductase from Rhodococcus erythropolis PR4
FEMS Microbiol. Ecol.
97
fiaa220
2020
Rhodococcus erythropolis, Rhodococcus erythropolis PR4
brenda
Chen, K.; Yu, X.; Zhang, X.; Li, X.; Liu, Y.; Si, M.; Su, T.
Involvement of a mycothiol-dependent reductase NCgl0018 in oxidative stress response of Corynebacterium glutamicum
J. Gen. Appl. Microbiol.
67
225-239
2021
Corynebacterium glutamicum
brenda
Oosthuizen, C.; Gasa, N.; Hamilton, C.; Lall, N.
Inhibition of mycothione disulphide reductase and mycobacterial biofilm by selected South African plants
South Afr. J. Bot.
120
291-297
2019
Mycobacterium tuberculosis
-
brenda