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Literature summary for 4.1.99.3 extracted from

  • Henbest, K.B.; Maeda, K.; Hore, P.J.; Joshi, M.; Bacher, A.; Bittl, R.; Weber, S.; Timmel, C.R.; Schleicher, E.
    Magnetic-field effect on the photoactivation reaction of Escherichia coli DNA photolyase (2008), Proc. Natl. Acad. Sci. USA, 105, 14395-14399.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
E109A non-5,10-methenyltetrahydrofolate-binding mutant Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ferricyanide blue light irradiation converts fully oxidized FAD to the semiquinone state, but in the presence of ferricyanide as electron acceptor further photoreduction to the fully reduced catalytically active form FADH- is inhibited Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclobutadipyrimidine in DNA
-
Escherichia coli pyrimidine residues in DNA
-
?

Synonyms

Synonyms Comment Organism
CPD photolyase
-
Escherichia coli
DNA photolyase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
5,10-methenyltetrahydrofolate
-
Escherichia coli
FAD the photoexcited FAD cofactor is reduced from the semiquinone or fully oxidized state to the catalytically active FADH- state Escherichia coli