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Literature summary for 1.8.1.7 extracted from

  • Wirth, E.; Latzko, E.
    Partial purification and properties of spinach leaf glutathione reductase (1978), Z. Pflanzenphysiol., 89, 69-75.
No PubMed abstract available
Search for more literature for 1.8.1.7

General Stability

General Stability Organism
partial inactivation after incubation with ATP Spinacia oleracea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 GSSG
-
 Spinacia oleracea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
125000
-
 gel filtration Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
 spinach
-

Purification (Commentary)

Purification (Comment) Organism
-
 Spinacia oleracea

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Spinacia oleracea
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
108
-
-
 Spinacia oleracea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GSSG + NADPH no activity Spinacia oleracea glutathione + NADP+
-
 ?
additional information not: cysteamine Spinacia oleracea ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.1
-
-
 Spinacia oleracea

pH Range

pH Minimum pH Maximum Comment Organism
7.3 8.8 pH 7.3: about 65% of activity maximum, pH 8.6: about 90% of activity maximum Spinacia oleracea

Cofactor

Cofactor Comment Organism Structure
FAD FAD enzyme Spinacia oleracea
NADH 10% activity of that with NADPH Spinacia oleracea
NADPH
-
 Spinacia oleracea