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
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dithiolic
-
sulfenic
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antituberculosis
-
ms-based
-
subversive
- 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
- isoniazid
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mycothiol-dependent
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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
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Substrates Products
Substrates Products on EC 1.8.1.15 - mycothione reductase
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REACTION DIAGRAM
2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide + NADPH
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5-(benzyl 2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside)-dithio-2-nitrobenzoate + NADPH
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a 5,5'-dithiobis-2-nitrobenzoic acid (DTNB)-coupled assay is developed. The mixed disulfide substrate liberates one molecule of TNB on NADPH-dependent reduction by Mycobacterium tubercolosis reductase. The liberated mycothiol analogue then reacts with DTNB to regenerate the mixed disulfide substrate and another molecule of TNB. Reaction progress can be measured by the increase in absorbance (412 nm) from the two molecules of TNB produced per turn of this catalytic cycle
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8-chloro-5-methoxy-7-methyl-1,4-naphthoquinone + NADPH
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benzyl 2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide + NADPH
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benzyl 2-(N-acetyl-L-cysteinyl)amino-2-deoxy-alpha-D-glucopyranoside disulfide + NADPH
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des-myo-inositol mycothione + reduced beta-nicotinamide hypoxanthine dinucleotide
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des-myo-inositol mycothione + reduced beta-nicotinamide hypoxanthine dinucleotide phosphate
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methyl 2-(-N-acetyl-L-cysteinyl) amino-2-deoxy-alpha-D-glucopyranoside disulfide + NADPH
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mycothione + NADPH
mycothiol + NADP+
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the enzyme is involved in mycothiol metabolism. Mycothiol may play an important role in the survival and adaption of mycobacteria to oxidative stress caused by normal metabolism, ir induced by the action of anti-tubercular drugs
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the enzyme exibits a strong substrate preference for TeO32- over SeO32-
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SeO32- + NADPH + H+
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the enzyme exibits a strong substrate preference for TeO32- over SeO32-
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the enzyme exibits a strong substrate preference for TeO32- over SeO32-
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TeO32- + NADPH + H+
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the enzyme exibits a strong substrate preference for TeO32- over SeO32-
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many naphthoquinones operate as subversive substrates. The native functions of these enzyme involves the NADPH-dependent reduction of disulfide bonds in the substrate. The enzyme-mediated toxicity of quinones/naphthoquinones is a consequence of their enzymatic reduction to semiquinone radicals. The naphthoquinone is then regenerated via the concomitant reduction of oxygen to toxic superoxide anion radicals. In this manner the naphthoquinone substrate is regenerated and the futile redox cycle continues
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additional information
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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
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additional information
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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
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additional information
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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
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