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Literature summary for 1.8.1.12 extracted from

  • Mittal, M.K.; Misra, S.; Owais, M.; Goyal, N.
    Expression, purification, and characterization of Leishmania donovani trypanothione reductase in Escherichia coli (2005), Protein Expr. Purif., 40, 279-286.
    View publication on PubMed

Application

Application Comment Organism
medicine enzyme is a target for development of antileishmanial drugs Leishmania donovani

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3) as soluble glutathione-S-transferase fusion protein Leishmania donovani

Inhibitors

Inhibitors Comment Organism Structure
Melarsen oxide over 95% inhibition at 0.05 mM Leishmania donovani
additional information no inhibition by melarsoprol Leishmania donovani
nifurtimox
-
Leishmania donovani
nitrofurazone
-
Leishmania donovani

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic mechanism Leishmania donovani
0.02
-
NADPH pH 7.8, 25°C, recombinant enzyme Leishmania donovani
0.05
-
trypanothione disulfide pH 7.8, 25°C, recombinant enzyme Leishmania donovani

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54668
-
2 * 54668, recombinant enzyme, mass spectrometry and SDS-PAGE Leishmania donovani
110000
-
recombinant enzyme, native PAGE Leishmania donovani

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Leishmania donovani phylogenetic relationship ?
-
?
additional information Leishmania donovani Dd8 phylogenetic relationship ?
-
?
trypanothione disulfide + NADPH Leishmania donovani
-
trypanothione + NADP+
-
?
trypanothione disulfide + NADPH Leishmania donovani Dd8
-
trypanothione + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Leishmania donovani Q95PT6
-
-
Leishmania donovani Dd8 Q95PT6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant soluble glutathione-S-transferase fusion protein from Escherichia coli strain BL21(DE3) to homogeneity, 20fold Leishmania donovani

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12.53
-
purified recombinant enzyme Leishmania donovani

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information phylogenetic relationship Leishmania donovani ?
-
?
additional information no activity with oxidized glutathione of the recombinant enzyme Leishmania donovani ?
-
?
additional information phylogenetic relationship Leishmania donovani Dd8 ?
-
?
additional information no activity with oxidized glutathione of the recombinant enzyme Leishmania donovani Dd8 ?
-
?
trypanothione disulfide + NADPH
-
Leishmania donovani trypanothione + NADP+
-
?
trypanothione disulfide + NADPH
-
Leishmania donovani Dd8 trypanothione + NADP+
-
?

Subunits

Subunits Comment Organism
dimer 2 * 54668, recombinant enzyme, mass spectrometry and SDS-PAGE Leishmania donovani
More amino acid sequence of the active site Leishmania donovani

Synonyms

Synonyms Comment Organism
TR
-
Leishmania donovani
trypanothione reductase
-
Leishmania donovani

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Leishmania donovani

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
18.18
-
trypanothione disulfide pH 7.8, 25°C, recombinant enzyme Leishmania donovani

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Leishmania donovani

Cofactor

Cofactor Comment Organism Structure
FAD amino acid sequence of the binding site Leishmania donovani
NADPH amino acid sequence of the binding site Leishmania donovani