Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.99.13 extracted from

  • Todo, T.; Kim, S.T.; Hitomi, K.; Otoshi, E.; Inui, T.; Morioka, H.; Kobayashi, H.; Ohtsuka, E.; Toh, H.; Ikenaga, M.
    Flavin adenine dinucleotide as a chromophore of the Xenopus (6-4)photolyase (1997), Nucleic Acids Res., 25, 764-768.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.99.13

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a GST-fusion protein Xenopus laevis

Protein Variants

Protein Variants Comment Organism
additional information sequencing of the cDNA clone reveals an open reading frame of encoding a protein of 526 amino acids (60600 Da) cDNA shows 58-54% amino acid identity to Drosophila (6-4)photolyase and its human homologue and 20-24% identity to the class I CPD photolyase Xenopus laevis

Organism

Organism UniProt Comment Textmining
Xenopus laevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by using a glutathione-sepharose column and UV-irradiated DNA affinity column, fusion protein is cleaved with thrombin Xenopus laevis

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 Xenopus laevis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 the recombinant protein repairs (6–4)photoproducts Xenopus laevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
T(6-4)T photoproduct (in DNA)
-
 Xenopus laevis thymidine residues (in DNA)
-
 ?

Synonyms

Synonyms Comment Organism
(6-4) photolyase
-
 Xenopus laevis

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Xenopus laevis