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Literature summary for 4.1.99.3 extracted from

  • Xu, L.; Mu, W.; Ding, Y.; Luo, Z.; Han, Q.; Bi, F.; Wang, Y.; Song, Q.
    Active site of Escherichia coli DNA photolyase: Asn378 is crucial both for stabilizing the neutral flavin radical cofactor and for DNA repair (2008), Biochemistry, 47, 8736-8743.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
N378S the recombinant mutant photolyase contains oxidized FAD (FADox) but not FADH after routine purification procedures, the mutant protein contains FADH in vivo as the wild type enzyme, the mutant photolyase is photoreducible and capable of binding cyclobutadipyrimidine dimers in DNA, but catalytically inert Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+ chelating Sepharose column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclobutadipyrimidine in DNA catalyzes the repair of cyclobutadipyrimidine dimers in DNA under near-UV or blue light irradiation Escherichia coli pyrimidine residues in DNA
-
?

Synonyms

Synonyms Comment Organism
DNA photolyase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FADH2 the catalytic activity of the enzyme requires fully reduced FAD Escherichia coli