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Literature summary for 1.8.1.10 extracted from

  • Ondarza, R.N.; Abney, R.; Lopez-Colome, A.M.
    Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast (1969), Biochim. Biophys. Acta, 191, 239-248.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
phosphate 25 mM, partially inhibits Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
CoA-glutathione at pH 5.5 and a fixed value of 110 nmol NADPH Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
108000
-
sucrose density gradient ultracentrifugation Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
strain ATCC 1946
-

Purification (Commentary)

Purification (Comment) Organism
143fold partial purification, separated from GSSG reductase activity, EC 1.6.4.2 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CoA-glutathione + NADPH
-
Saccharomyces cerevisiae glutathione + CoA + NADP+
-
ir
additional information no reduction of CoASSCys, GSSCys or CysSSCys Saccharomyces cerevisiae ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
24
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NADPH NADPH-dependent Saccharomyces cerevisiae