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Literature summary for 1.8.1.15 extracted from

  • Kumar, A.; Nartey, W.; Shin, J.; Manimekalai, M.S.S.; Grueber, G.
    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 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
functional recombinant expression of tagged enzyme Mycobacterium tuberculosis

KM Value [mM]

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WHH3
-
-
Mycobacterium tuberculosis H37Rv P9WHH3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant tagged enzyme by affinity chromatography and gel filtration Mycobacterium tuberculosis

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
MtMtr
-
Mycobacterium tuberculosis
MTR
-
Mycobacterium tuberculosis
mycothiol disulfide reductase
-
Mycobacterium tuberculosis
mycothiol disulphide reductase
-
Mycobacterium tuberculosis

Cofactor

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

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