Literature summary for 4.1.99.13 extracted from

Todo, T.; Ryo, H.; Yamamoto, K.; Toh, H.; Inui, T.; Ayaki, H.; Nomura, T.; Ikenaga, M.
Similarity among the Drosophila (6-4)photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family (1996), Science, 272, 109-112.

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinant protein expressed in Escherichia coli	Drosophila melanogaster

Protein Variants

Protein Variants	Comment	Organism
additional information	the predicted amino acid sequence of the human protein has 48% identity with the Drosophila (6-4)photolyase over the entire protein	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
62000	-	deduced from cDNA	Drosophila melanogaster

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by using affinity chromatography and UV-irradiated DNA attached beads	Drosophila melanogaster

Reaction

Reaction	Comment	Organism	Reaction ID
(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA)	The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent. In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases.This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack. In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH-) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures. The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases	Drosophila melanogaster	a
(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA)	The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent. In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases.This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack. In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH-) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures. The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases	Homo sapiens	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	by Northern blot analysis it is demonstrated that the transcript is expressed in multiple tissues	Homo sapiens	-
ovary	by Northern blot analysis it is demonstrated that the transcript is expressed at highest level only in adult ovary	Drosophila melanogaster	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(6-4) photoproduct (in DNA)	-	Drosophila melanogaster	2 pyrimidine residues (in DNA)	-	?

Synonyms

Synonyms	Comment	Organism
(6-4) photolyase	-	Drosophila melanogaster
human (6-4) photolyase homologous protein	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Drosophila melanogaster
FAD	-	Homo sapiens

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Release 2023.1 (January 2023)