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Literature summary for 1.8.1.7 extracted from

  • Boggaram, V.; Larson, K.; Mannervik, B.
    Characterization of glutathione reductase from porcine erythrocytes (1978), Biochim. Biophys. Acta, 527, 337-347.
    View publication on PubMed
Search for more literature for 1.8.1.7

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
 2 * 59000, SDS-PAGE Sus scrofa
103000
-
 analytical ultracentrifugation Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GSSG + NADPH S-sulfoglutathione and some mixed disulfides, with the exception of the mixed disulfide of coenzyme A and GSH, are poor substrates Sus scrofa glutathione + NADP+
-
 ?
additional information low transhydrogenase activity with oxidized pyridine nucleotide analogs and diaphorase activity with 2,6-dichlorophenolindophenol as acceptor substrates, NADPH and NADH as donors Sus scrofa ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 59000, SDS-PAGE Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 NADH + GSSG Sus scrofa
7
-
 NADPH + GSSG Sus scrofa

Cofactor

Cofactor Comment Organism Structure
FAD 2 mol of FAD per mol of enzyme Sus scrofa
FAD FAD enzyme Sus scrofa
NADH 200times less effective than NADPH Sus scrofa
NADPH 200times more activity than with NADH Sus scrofa