Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
arseno-mycothiol + mycoredoxin
arsenite + mycothiol-mycoredoxin disulfide
insulin + dithiothreitol
?
-
-
-
?
additional information
?
-
arseno-mycothiol + mycoredoxin
arsenite + mycothiol-mycoredoxin disulfide
-
-
a second mycothiol recycles mycoredoxin and forms mycothione
-
?
arseno-mycothiol + mycoredoxin
arsenite + mycothiol-mycoredoxin disulfide
-
reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate. The substrate arseno-mycothiol is formed by arsenate-mycothiol transferase. A second mycothiol recycles mycoredoxin and forms mycothione
-
-
?
additional information
?
-
-
the enzyme reduces the sulfenic acid intermediate via the formation of an S-mycothiolated methionine sulfoxide reductase A intermediate which is then recycled by mycoredoxin and the second molecule of mycothiol
-
-
?
additional information
?
-
-
the enzyme serve as reducing power for mycothiol peroxidase
-
-
?
additional information
?
-
-
the enzyme directly reduces the oxidized form of alkyl hydroxyperoxide reductase E, through a protein mixed disulfide with the N-terminal cysteine of mycoredoxin-1 and the sulfenic acid derivative of the peroxidatic cysteine of alkyl hydroxyperoxide reductase E
-
-
?
additional information
?
-
the enzyme receives electrons through the mycothiol/mycothione reductase/NADPH pathway to activate TP053, preferentially via a dithiol-disulfide mechanism. The enzyme uses a monothiol-disulfide exchange mechanism to reduce S-mycothiolated mixed disulfides and intramolecular disulfides. The enzyme has no oxidase properties
-
-
?
additional information
?
-
-
the enzyme receives electrons through the mycothiol/mycothione reductase/NADPH pathway to activate TP053, preferentially via a dithiol-disulfide mechanism. The enzyme uses a monothiol-disulfide exchange mechanism to reduce S-mycothiolated mixed disulfides and intramolecular disulfides. The enzyme has no oxidase properties
-
-
?
additional information
?
-
the enzyme receives electrons through the mycothiol/mycothione reductase/NADPH pathway to activate TP053, preferentially via a dithiol-disulfide mechanism. The enzyme uses a monothiol-disulfide exchange mechanism to reduce S-mycothiolated mixed disulfides and intramolecular disulfides. The enzyme has no oxidase properties
-
-
?
additional information
?
-
-
isoform mycoredoxin-1 acts as an oxidoreductase exclusively linked to the mycothiol electron transfer pathway and can reduce S-mycothiolated mixed disulfides. Mycoredoxin-1 has a redox potential of -218 mV and hydrogen bonding with neighbouring residues lowers the pKa of its N-terminal nucleophilic cysteine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Infections
Involvement of a mycothiol-dependent reductase NCgl0018 in oxidative stress response of Corynebacterium glutamicum.
Infections
Mycoredoxins Are Required for Redox Homeostasis and Intracellular Survival in the Actinobacterial Pathogen Rhodococcus equi.
Tuberculosis
Mycoredoxin-1 is one of the missing links in the oxidative stress defense mechanism of Mycobacteria.
Tuberculosis
Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis.
Tuberculosis
Redox chemistry of Mycobacterium tuberculosis alkylhydroperoxide reductase E (AhpE): Structural and mechanistic insight into a mycoredoxin-1 independent reductive pathway of AhpE via mycothiol.
Tuberculosis
Rv0579 Is Involved in the Resistance to the TP053 Antitubercular Prodrug.
Tuberculosis
Rv2466c mediates the activation of TP053 to kill replicating and non-replicating Mycobacterium tuberculosis.
Tuberculosis
The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis.
Tuberculosis
The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of Mycobacterium tuberculosis.
Tuberculosis
The Redox State Regulates the Conformation of Rv2466c to Activate the Antitubercular Prodrug TP053.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Wu, B.; Song, J.; Beitz, E.
Novel channel enzyme fusion proteins confer arsenate resistance
J. Biol. Chem.
285
40081-40087
2010
Salinispora tropica
brenda
Van Laer, K.; Buts, L.; Foloppe, N.; Vertommen, D.; Van Belle, K.; Wahni, K.; Roos, G.; Nilsson, L.; Mateos, L.M.; Rawat, M.; van Nuland, N.A.; Messens, J.
Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of mycobacteria
Mol. Microbiol.
86
787-804
2012
Mycolicibacterium smegmatis
brenda
Si, M.; Zhang, L.; Chaudhry, M.T.; Ding, W.; Xu, Y.; Chen, C.; Akbar, A.; Shen, X.; Liu, S.J.
Corynebacterium glutamicum methionine sulfoxide reductase A uses both mycoredoxin and thioredoxin for regeneration and oxidative stress resistance
Appl. Environ. Microbiol.
81
2781-2796
2015
Corynebacterium glutamicum
brenda
Si, M.; Xu, Y.; Wang, T.; Long, M.; Ding, W.; Chen, C.; Guan, X.; Liu, Y.; Wang, Y.; Shen, X.; Liu, S.J.
Functional characterization of a mycothiol peroxidase in Corynebacterium glutamicum that uses both mycoredoxin and thioredoxin reducing systems in the response to oxidative stress
Biochem. J.
469
45-57
2015
Corynebacterium glutamicum
brenda
Eberle, R.J.; Kawai, L.A.; de Moraes, F.R.; Tasic, L.; Arni, R.K.; Coronado, M.A.
Biochemical and biophysical characterization of a mycoredoxin protein glutaredoxin A1 from Corynebacterium pseudotuberculosis
Int. J. Biol. Macromol.
107
1999-2007
2018
Corynebacterium pseudotuberculosis (D9Q987), Corynebacterium pseudotuberculosis
brenda
Hugo, M.; Van Laer, K.; Reyes, A.; Vertommen, D.; Messens, J.; Radi, R.; Trujillo, M.
Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis
J. Biol. Chem.
289
5228-5239
2014
Mycobacterium tuberculosis
brenda
Rosado, L.A.; Wahni, K.; Degiacomi, G.; Pedre, B.; Young, D.; de la Rubia, A.G.; Boldrin, F.; Martens, E.; Marcos-Pascual, L.; Sancho-Vaello, E.; Albesa-Jove, D.; Provvedi, R.; Martin, C.; Makarov, V.; Versees, W.; Verniest, G.; Guerin, M.E.; Mateos, L.M.; Manganelli, R.; Messens, J.
The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of Mycobacterium tuberculosis
J. Biol. Chem.
292
13097-13110
2017
Mycobacterium tuberculosis (O53193), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (O53193)
brenda