Literature summary 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.

Protein Variants

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
4.1.99.3	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
4.1.99.3	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

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Release 2023.1 (January 2023)