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Literature summary for 1.8.1.7 extracted from

  • Krauth-Siegel, R.L.; Jockers-Scheruebl, M.C.; Becker, K.; Schirmer, R.H.
    NADPH-dependent disulphide reductases (1989), Biochem. Soc. Trans., 17, 315-317.
    View publication on PubMed
Search for more literature for 1.8.1.7

Activating Compound

Activating Compound Comment Organism Structure
cysteine redox active disulfide at the catalytic site Homo sapiens

Application

Application Comment Organism
medicine mimicking of favism by inhibiting the enzyme with specific inhibitors to protect against malaria Homo sapiens
medicine potential target of antimalarial and cytostatic agents Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
carmustine irreversible inhibito of enzyme in reduced state Homo sapiens
NADPH slow inactivation in vitro due to inter- or intramolecular disulfide formation Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ mechanism Homo sapiens
a
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ member of pyridine-nucleotide disulfide oxidoreductase family of flavoenzymes Homo sapiens
a
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ catalytic cycle Homo sapiens
a
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ substrate and cofactor binding site, three-dimensional structure Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GSSG + NADPH
-
 Homo sapiens glutathione + NADP+
-
 r

Cofactor

Cofactor Comment Organism Structure
FAD FAD enzyme Homo sapiens
additional information as malaria brings riboflavin deficiency, in effection regions a large portion of enzymes miss FAD, but are as well active Homo sapiens
NADPH can utilize both NADPH and NADH, more active with NADPH Homo sapiens