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Literature summary for 4.1.99.13 extracted from

  • Todo, T.; Tsuji, H.; Otoshi, E.; Hitomi, K.; Kim, S.T.; Ikenaga, M.
    Characterization of a human homolog of (6-4) photolyase (1997), Mutat. Res., 384, 195-204.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed as a GSTtagged fusion protein in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information expression of H64PRH does not show any photoreactivating effects on the survival of UV-irradiated Escherichia coli. Using a gel shift assay with with un-irradiated and UV-irradiated DNA probes it is shown that H64PRH protein does not possess any binding activity to either DNA probe Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63000
-
SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by using a glutathione sepharose column and a Hi Trap Q column. Concentrated fusion protein is cleaved with thrombin from bovine plasma by incubation overnight at 4°C. For chromophore determination, the eluate from the glutathione sepharose column is purified through a Q sepharose column, omitting gel filtration procedure, and concentrated by ultrafiltration Homo sapiens

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 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
additional information by Northern blot analysis an ubiquitous expression pattern is demonstrated Homo sapiens
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
enzyme does not show any detectable photolyase activity Homo sapiens

Synonyms

Synonyms Comment Organism
(6-4) photolyase
-
Homo sapiens
H64PRH
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Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens