EC Number   |
General Information |
Reference |
|---|
   1.8.1.15 | 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 |
698899 |
| 1.8.1.15 | 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 |
743814 |
| 1.8.1.15 | more |
MtMtr is predicted to undergo a mono-to-dimeric equilibrium in solution during catalysis. Enzyme homology structure modelling |
-, 741994 |
| 1.8.1.15 | physiological function |
in a mycothione disulfide reductase mutant, mycothiol levels decrease only upon treatment with peroxide |
-, 725157 |
| 1.8.1.15 | 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 |
-, 741994 |
| 1.8.1.15 | 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 |
743814 |
