Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.1.12 extracted from

  • Azam, S.; Jouvet, N.; Jilani, A.; Vongsamphanh, R.; Yang, X.; Yang, S.; Ramotar, D.
    Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1 (2008), J. Biol. Chem., 283, 30632-30641.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.12

Protein Variants

Protein Variants Comment Organism
C152G mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1 Homo sapiens
C156G mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P04406
-
-

Expression

Organism Comment Expression
Homo sapiens GAPDH-small interfering RNA knockdown sensitizes the cells to methyl methane sulfonate and bleomycin, which generate lesions that are repaired by APE1, but cells show normal sensitivity to 254-nm UV. GAPDH knockdown cells exhibit an increased level of spontaneous abasic sites in the genomic DNA as a result of diminished APE1 endonuclease activity down

General Information

General Information Comment Organism
physiological function GAPDH physically associates with DNA repair enzyme APE1. This interaction allows GAPDH to convert the oxidized species of APE1 to the reduced form, thereby reactivating its endonuclease activity to cleave abasic sites Homo sapiens