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

BRENDA support

Literature summary for 4.1.99.3 extracted from

  • Balland, V.; Byrdin, M.; Eker, A.P.; Ahmad, M.; Brettel, K.
    What makes the difference between a cryptochrome and DNA photolyase? A spectroelectrochemical comparison of the flavin redox transitions (2009), J. Am. Chem. Soc., 131, 426-427.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
N378S the mutation stabilizes the oxidized state of the flavin Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Synechococcus elongatus PCC 7942 = FACHB-805
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclobutadipyrimidine in DNA
-
Synechococcus elongatus PCC 7942 = FACHB-805 pyrimidine residues in DNA
-
?
cyclobutadipyrimidine in DNA
-
Escherichia coli pyrimidine residues in DNA
-
?

Synonyms

Synonyms Comment Organism
CPD photolyase
-
Synechococcus elongatus PCC 7942 = FACHB-805
CPD photolyase
-
Escherichia coli
DNA photolyase
-
Synechococcus elongatus PCC 7942 = FACHB-805
DNA photolyase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
flavin requires fully reduced flavin for photorepair of DNA, full oxidation to FAD is not necessary for biological function, the reaction mechanism involves electron transfer to the substrate from the excited state of the flavin in its fully reduced state FADH- with subsequent electron return within a nanosecond Synechococcus elongatus PCC 7942 = FACHB-805
flavin requires fully reduced flavin for photorepair of DNA, full oxidation to FAD is not necessary for biological function, the reaction mechanism involves electron transfer to the substrate from the excited state of the flavin in its fully reduced state FADH- with subsequent electron return within a nanosecond Escherichia coli