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Literature summary extracted from

  • Henderson, G.B.; Fairlamb, A.H.; Ulrich, P.; Cerami, A.
    Substrate specificity of the flavoprotein trypanothione disulfide reductase from Crithidia fasciculata (1987), Biochemistry, 26, 3023-3027.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.1.12 additional information activity is dependent on a redox-active cysteine at the active centre Crithidia fasciculata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.12 additional information
-
additional information Km of several trypanothione disulfide derivatives, e.g. N1-monoglutathionylspermidine, mixed disulfide of N1-monoglutathionylspermidine and glutathione Crithidia fasciculata
1.8.1.12 0.022 0.275 glutathionylspermidine disulfide
-
Crithidia fasciculata
1.8.1.12 0.051
-
trypanothione disulfide
-
Crithidia fasciculata

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.12 Crithidia fasciculata
-
insect-parasitic trypanosomatid
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.12 glutathionylspermidine disulfide + NADPH
-
Crithidia fasciculata 2-glutathionylspermidine + NADP+
-
r
1.8.1.12 additional information reduces several trypanothione derivatives, e.g. N1-monoglutathionylspermidine, mixed disulfide of N1-monoglutathionylspermidine and glutathione Crithidia fasciculata ?
-
?
1.8.1.12 trypanothione disulfide + NADPH
-
Crithidia fasciculata trypanothione + NADP+
-
r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.12 27
-
assay at Crithidia fasciculata

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.12 7.8
-
-
Crithidia fasciculata

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.12 FAD
-
Crithidia fasciculata
1.8.1.12 NADPH
-
Crithidia fasciculata