Literature summary 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.

Cloned(Commentary)

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

Protein Variants

EC Number	Protein Variants	Comment	Organism
4.1.99.3	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

EC Number	Organism	UniProt	Comment	Textmining
4.1.99.3	Escherichia coli	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4.1.99.3	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

EC Number	Synonyms	Comment	Organism
4.1.99.3	DNA photolyase	-	Escherichia coli

Cofactor

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

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Release 2023.1 (January 2023)