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Literature summary extracted from

  • Schulz, G.E.; Schirmer, R.H.; Pai, E.F.
    The three-diemensional structure of glutathione reductase and its substrate complexes at 0.3 nm resolution (1978), Flavins and Flavoproteins (Proc. Int. Symp. , 6th, Meeting, Yagi, K. , Yamano, T. , eds. ), , 557-567.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.1.7 structure analysis overview, ligand binding, active center Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.7 GSSG + NADPH Homo sapiens role in cell division cycle and in stress adaption on cellular level glutathione + NADP+
-
 ?
1.8.1.7 GSSG + NADPH Homo sapiens maintenance of high levels of GSH in cytoplasm glutathione + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.7 Homo sapiens
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.7 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ mechanism Homo sapiens
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.1.7 erythrocyte
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.7 GSSG + NADPH
-
 Homo sapiens glutathione + NADP+
-
 r
1.8.1.7 GSSG + NADPH role in cell division cycle and in stress adaption on cellular level Homo sapiens glutathione + NADP+
-
 ?
1.8.1.7 GSSG + NADPH maintenance of high levels of GSH in cytoplasm Homo sapiens glutathione + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.1.7 More three-dimensional structure Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.7 FAD FAD enzyme Homo sapiens
1.8.1.7 NADPH
-
 Homo sapiens