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Literature summary extracted from
- Structural and mechanistic insights into mycothiol disulphide reductase and the mycoredoxin-1-alkylhydroperoxide reductase E assembly of Mycobacterium tuberculosis (2017), Biochim. Biophys. Acta, 1861, 2354-2366 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.8.1.15 | functional recombinant expression of tagged enzyme | Mycobacterium tuberculosis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.1.15 | additional information | - |
additional information | stopped-flow kinetics | Mycobacterium tuberculosis |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.15 | 92000 | - |
recombinant enzyme, gel filtration | Mycobacterium tuberculosis |
| 1.8.1.15 | 137000 | - |
recombinant enzyme, dynamic light scattering analysis | Mycobacterium tuberculosis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.15 | 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 | ? | - |
? |  |
| 1.8.1.15 | 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 | ? | - |
? | |
| 1.8.1.15 | mycothione + NADPH + H+ | Mycobacterium tuberculosis | - |
2 mycothiol + NADP+ | - |
? | |
| 1.8.1.15 | mycothione + NADPH + H+ | Mycobacterium tuberculosis H37Rv | - |
2 mycothiol + NADP+ | - |
? | |
| 1.11.1.29 | mycoredoxin + ROOH | Mycobacterium tuberculosis | Mycobacteria employ a versatile machinery of the mycothiol-dependent system, containing the proteins mycothiol disulfide reductase, the oxido-reductase Mycoredoxin-1 and the alkyl-hydroperoxide subunit E (AhpE). 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 upon exposure to oxidative stress. The epitopes of MtMrx-1 and MtAhpE interaction are described | mycoredoxin disulfide + H2O + ROH | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.15 | Mycobacterium tuberculosis | P9WHH3 | - |
- |
| 1.8.1.15 | Mycobacterium tuberculosis H37Rv | P9WHH3 | - |
- |
| 1.11.1.29 | Mycobacterium tuberculosis | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.1.15 | recombinant tagged enzyme by affinity chromatography and gel filtration | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.15 | 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 | ? | - |
? | |
| 1.8.1.15 | 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 | ? | - |
? | |
| 1.8.1.15 | mycothione + NADPH + H+ | - |
Mycobacterium tuberculosis | 2 mycothiol + NADP+ | - |
? | |
| 1.8.1.15 | mycothione + NADPH + H+ | - |
Mycobacterium tuberculosis H37Rv | 2 mycothiol + NADP+ | - |
? | |
| 1.11.1.29 | mycoredoxin + ROOH | Mycobacteria employ a versatile machinery of the mycothiol-dependent system, containing the proteins mycothiol disulfide reductase, the oxido-reductase Mycoredoxin-1 and the alkyl-hydroperoxide subunit E (AhpE). 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 upon exposure to oxidative stress. The epitopes of MtMrx-1 and MtAhpE interaction are described | Mycobacterium tuberculosis | mycoredoxin disulfide + H2O + ROH | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.8.1.15 | dimer | 2 * 49800, about, sequence calculation, spectroscopic and dynamic light scattering structure analysis, modelling | Mycobacterium tuberculosis |
| 1.8.1.15 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.1.15 | MtMtr | - |
Mycobacterium tuberculosis |
| 1.8.1.15 | MTR | - |
Mycobacterium tuberculosis |
| 1.8.1.15 | mycothiol disulfide reductase | - |
Mycobacterium tuberculosis |
| 1.8.1.15 | mycothiol disulphide reductase | - |
Mycobacterium tuberculosis |
| 1.11.1.29 | AhpE | - |
Mycobacterium tuberculosis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.15 | FAD | the FAD-binding- and interface domain participate in the dimer formation | Mycobacterium tuberculosis | |
| 1.8.1.15 | NADPH | structure analysis of the two NADPH-binding domains inside the dimeric MtMtr in different conformations | Mycobacterium tuberculosis | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.8.1.15 | additional information | MtMtr is predicted to undergo a mono-to-dimeric equilibrium in solution during catalysis. Enzyme homology structure modelling | Mycobacterium tuberculosis |
| 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 | Mycobacterium tuberculosis |
| 1.11.1.29 | drug target | the essential residue of oxido-reductase Mycoredoxin-1 (MtMrx-1) identified in the interaction with mycothiol disulfide reductase (MtMtr) and MtAhpE form a platform for structure-guided drug design against the versatile enzyme machinery of the mycothiol-dependent system inside Mycobacterium tuberculosis | Mycobacterium tuberculosis |
| 1.11.1.29 | physiological function | Mycobacteria employ a versatile machinery of the mycothiol-dependent system, containing the proteins mycothiol disulfide reductase, the oxido-reductase Mycoredoxin-1 (Mrx-1) and the alkyl-hydroperoxide subunit E (AhpE). 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 upon exposure to oxidative stress | Mycobacterium tuberculosis |
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Release 2023.1 (January 2023)
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