1.8.1.15: mycothione reductase
This is an abbreviated version!
For detailed information about mycothione reductase, go to the full flat file.
Word Map on EC 1.8.1.15
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1.8.1.15
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tuberculosis
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actinobacteria
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glutamicum
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mycoredoxin-1
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dithiolic
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sulfenic
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antituberculosis
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ms-based
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subversive
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natalensis
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nadph-binding
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antimycobacterial
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monothiolic
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mtahpe
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euclea
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isoniazid
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mycothiol-dependent
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peroxidatic
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oxidized-reduced
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medicine
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molecular biology
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analysis
- 1.8.1.15
- tuberculosis
- actinobacteria
- glutamicum
- mycoredoxin-1
-
dithiolic
-
sulfenic
-
antituberculosis
-
ms-based
-
subversive
- natalensis
-
nadph-binding
-
antimycobacterial
-
monothiolic
-
mtahpe
-
euclea
- isoniazid
-
mycothiol-dependent
-
peroxidatic
-
oxidized-reduced
- medicine
- molecular biology
- analysis
Reaction
Synonyms
MSH disulfide reductase, MtMtr, MTR, mycothiol disulfide reductase, mycothiol disulphide reductase, mycothiol-disulfide reductase, mycothione disulphide reductase, mycothione reductase, NADPH-dependent mycothiol reductase, NADPH-dependent mycothione reductase
ECTree
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Subunits
Subunits on EC 1.8.1.15 - mycothione reductase
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dimer
homodimer
homotetramer
additional information
2 * 49800, about, sequence calculation, spectroscopic and dynamic light scattering structure analysis, modelling
dimer
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2 * 49800, about, sequence calculation, spectroscopic and dynamic light scattering structure analysis, modelling
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homodimer
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2 * 49800, apoenzyme in solution, calculated from amino acid sequence
homodimer
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2 * 49800, apoenzyme in solution, calculated from amino acid sequence
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4 * 49800, enzyme bound to NADPH, calculated from amino acid sequence
homotetramer
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4 * 49800, enzyme bound to NADPH, calculated from amino acid sequence
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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
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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
-