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Literature summary for 4.1.99.13 extracted from

  • Hitomi, K.; Nakamura, H.; Kim, S.T.; Mizukoshi, T.; Ishikawa, T.; Iwai, S.; Todo, T.
    Role of two histidines in the (6-4) photolyase reaction (2001), J. Biol. Chem., 276, 10103-10109.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Xenopus laevis

Protein Variants

Protein Variants Comment Organism
H354A almost complete loss of repair activity Xenopus laevis
H358A almost complete loss of repair activity, suggesting that His354 and His358 are essential for catalytic activity Xenopus laevis
L355A large decrease in the affinity to the (6-4) photoproduct substrate, suggesting a hydrophobic interaction with the (6-4)photoproduct Xenopus laevis
Q288A repair activity is not reduced Xenopus laevis
W291A some enzymatic activity is retained Xenopus laevis
W398A some enzymatic activity is retained Xenopus laevis

Organism

Organism UniProt Comment Textmining
Xenopus laevis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA) A mechanism is proposed in which the histidines residues His 354 and His 358 catalyze the formation of the four-membered ring intermediate in the repair process of this enzyme. When deuterium oxide is used as a solvent, the repair activity is decreased. The proton transfer shown by this isotope effect supports the proposed mechanism 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 thymidine residues (in DNA)
-
?

Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Xenopus laevis

pH Range

pH Minimum pH Maximum Comment Organism
8.5 9
-
Xenopus laevis

Cofactor

Cofactor Comment Organism Structure
FAD
-
Xenopus laevis