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Literature summary for 1.8.1.7 extracted from

  • Francescutti, D.; Baldwin, J.; Lee, L.; Mutus, B.
    Peroxynitrite modification of glutathione reductase: modeling studies and kinetic evidence suggest the modification of tyrosines at the glutathione disulfide binding site (1996), Protein Eng., 9, 189-194.
    View publication on PubMed

General Stability

General Stability Organism
NADPH is not protective against induced inactivation by peroxynitrite Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
peroxynitrite inactivation of enzyme by formation of nitrotyrosine near the catalytic center, 2.5fold increased Km-value and 1.7fold decreased Vmax, molecular modeling Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
NADPH
-
Bos taurus
0.04
-
GSSG
-
Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ molecular modeling of enzyme inactivation by peroxynitrite, structure analysis Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
intestine mucosa Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GSSG + NADPH
-
Bos taurus glutathione + NADP+
-
?

Synonyms

Synonyms Comment Organism
GR
-
Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Bos taurus