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Literature summary for 1.2.1.12 extracted from

  • Schmalhausen, E.V.; Zhlobek, E.B.; Shalova, I.N.; Firuzi, O.; Saso, L.; Muronetz, V.I.
    Antioxidant and prooxidant effects of quercetin on glyceraldehyde-3-phosphate dehydrogenase (2007), Food Chem. Toxicol., 45, 1988-1993.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Fe2+ in the absence of quercetin, GAPDH can be oxidized by ferrous ions due to the formation of reactive oxygen species according to the following series of reactions Oryctolagus cuniculus
H2O2 GAPDH is oxidized by H2O2 which is likely formed due to the spontaneous dismutation of the superoxide anion that is formed during the autooxidation of quercetin that can result in the oxidation of SH-groups of GAPDH Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Synonyms

Synonyms Comment Organism
GAPDH
-
Oryctolagus cuniculus