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Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.1.7 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.7 0.0015
-
 NADPH
-
 Bos taurus
1.8.1.7 0.04
-
 GSSG
-
 Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.7 Bos taurus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.7 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ molecular modeling of enzyme inactivation by peroxynitrite, structure analysis Bos taurus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.1.7 intestine mucosa Bos taurus
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.8.1.7 GR
-
 Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.7 NADPH
-
 Bos taurus