Cloned (Comment) | Organism |
---|---|
functional recombinant expression of tagged enzyme | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | stopped-flow kinetics | Mycobacterium tuberculosis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
92000 | - |
recombinant enzyme, gel filtration | Mycobacterium tuberculosis |
137000 | - |
recombinant enzyme, dynamic light scattering analysis | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mycobacterium tuberculosis | 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 | ? | - |
? | |
additional information | Mycobacterium tuberculosis H37Rv | 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 | ? | - |
? | |
mycothione + NADPH + H+ | Mycobacterium tuberculosis | - |
2 mycothiol + NADP+ | - |
? | |
mycothione + NADPH + H+ | Mycobacterium tuberculosis H37Rv | - |
2 mycothiol + NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WHH3 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WHH3 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant tagged enzyme by affinity chromatography and gel filtration | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | 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 | Mycobacterium tuberculosis | ? | - |
? | |
additional information | 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 | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
mycothione + NADPH + H+ | - |
Mycobacterium tuberculosis | 2 mycothiol + NADP+ | - |
? | |
mycothione + NADPH + H+ | - |
Mycobacterium tuberculosis H37Rv | 2 mycothiol + NADP+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 49800, about, sequence calculation, spectroscopic and dynamic light scattering structure analysis, modelling | Mycobacterium tuberculosis |
More | 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 | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
MtMtr | - |
Mycobacterium tuberculosis |
MTR | - |
Mycobacterium tuberculosis |
mycothiol disulfide reductase | - |
Mycobacterium tuberculosis |
mycothiol disulphide reductase | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | the FAD-binding- and interface domain participate in the dimer formation | Mycobacterium tuberculosis | |
NADPH | structure analysis of the two NADPH-binding domains inside the dimeric MtMtr in different conformations | Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
additional information | MtMtr is predicted to undergo a mono-to-dimeric equilibrium in solution during catalysis. Enzyme homology structure modelling | Mycobacterium tuberculosis |
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 | Mycobacterium tuberculosis |