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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.13 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.99.13 62000
-
 deduced from cDNA Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.13 Drosophila melanogaster
-
-
-
4.1.99.13 Homo sapiens
-
-
-

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.99.13 (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
4.1.99.13 (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

EC Number Source Tissue Comment Organism Textmining
4.1.99.13 additional information by Northern blot analysis it is demonstrated that the transcript is expressed in multiple tissues Homo sapiens
-
4.1.99.13 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.13 (6-4) photoproduct (in DNA)
-
 Drosophila melanogaster 2 pyrimidine residues (in DNA)
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.13 (6-4) photolyase
-
 Drosophila melanogaster
4.1.99.13 human (6-4) photolyase homologous protein
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.13 FAD
-
 Drosophila melanogaster
4.1.99.13 FAD
-
 Homo sapiens