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Literature summary for 4.2.99.18 extracted from

  • Su, D.; Delaplane, S.; Luo, M.; Rempel, D.; Vu, B.; Kelley, M.; Gross, M.; Georgiadis, M.
    Interactions of apurinic/apyrimidinic endonuclease with a redox inhibitor: Evidence for an alternate conformation of the enzyme (2011), Biochemistry, 50, 82-92.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis chemical footprinting-mass spectrometric assay using N-ethylmaleimide, an irreversible Cys modifier, to characterize the interaction of the redox inhibitor, E3330, with APE1. When APE1 is incubated with E3330, two N-ethylmaleimide-modified products are observed, one with two and a second with seven added N-ethylmaleimide molecules Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
E3330 forms a reversible adduct with DELTA40APE1, an N-terminal truncation of APE1 including residues 40-318. E3330 also increases the extent of disulfide bond formation involving redox critical Cys residues in APE1 Homo sapiens
N-ethylmaleimide treatment of fully denatured full-length APE1 and DELTA40APE1, an N-terminal truncation of APE1 including residues 40-318, results in modification of 7 and 2 resiudes, respectively Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information APE1 adopts a partially unfolded state, which is proposed to be the redox active form of the enzyme Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
APE1
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Homo sapiens