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Literature summary extracted from

  • Danielson, U.H.; Jiang, F.; Hansson, L.O.; Mannervik, B.
    Probing the kinetic mechanism and coenzyme specificity of glutathione reductase from the Cyanobacterium Anabaena PCC 7120 by redesign of the pyridine-nucleotide-binding site (1999), Biochemistry, 38, 9254-9263.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.7 expression of wild-type and mutant in Escherichia coli, structure modeling Anabaena sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.7 additional information a mutant lacking a loop involved in ligand binding, showing reduced activity, and a mutant with a modified loop, which is more efficient with NADPH and NADH Anabaena sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.7 additional information
-
 additional information Km of wild-type and mutants Anabaena sp.

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.7 Anabaena sp.
-
 PCC 7120, cyanobacterium
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.7 wild-type and recombinant from Escherichia coli Anabaena sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.7 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ member of pyridine-nucleotide disulfide oxidoreductase family of flavoenzymes Anabaena sp.
a
1.8.1.7 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ substrate and cofactor binding site, three-dimensional structure Anabaena sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.7 GSSG + NADPH
-
 Anabaena sp. glutathione + NADP+
-
 ir

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.7 30
-
 assay at Anabaena sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.7 7
-
 NADPH + GSSG Anabaena sp.
1.8.1.7 8
-
 NADH + GSSG Anabaena sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.7 FAD FAD enzyme Anabaena sp.
1.8.1.7 NADH 48fold less activity than with NADPH Anabaena sp.
1.8.1.7 NADPH 48fold more activity than with NADH Anabaena sp.