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Literature summary for 4.1.99.13 extracted from

  • Hitomi, K.; Kim, S.T.; Iwai, S.; Harima, N.; Otoshi, E.; Ikenaga, M.; Todo, T.
    Binding and catalytic properties of Xenopus (6-4) photolyase (1997), J. Biol. Chem., 272, 32591-32598.
    View publication on PubMed
Search for more literature for 4.1.99.13

Activating Compound

Activating Compound Comment Organism Structure
DTT
-
 Xenopus laevis

Cloned(Commentary)

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

Metals/Ions

Metals/Ions Comment Organism Structure
Na+
-
 Xenopus laevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
T(6-4)T photoproduct (in DNA) Xenopus laevis
-
 2 thymine residues (in DNA)
-
 ?

Organism

Organism UniProt Comment Textmining
Xenopus laevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by using glutathione-sepharose columns 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
-
 (6-4) photolyase binds to T[6-4]T in double stranded DNA with high affinity (KD= 10*exp-9) and to T[6-4]T in single-stranded DNA with slightly lower-affinity (KD= 2*10 exp-8). Majority of the T[6–4]T-(6-4) photolyase complex dissociates very slowly (koff= 2.9* 10exp-5/sec). Its absolute action spectrum without a second chromophore in the 350-600 nm region closely matches the absorption spectrum of the enzyme Xenopus laevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
T(6-4)T photoproduct (in DNA)
-
 Xenopus laevis 2 thymine residues (in DNA)
-
 ?

Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Xenopus laevis

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Xenopus laevis