Photolyases bind complementary DNA strands and break certain types of pyrimidine dimers that arise when a pair of thymine or cytosine bases on the same strand of DNA become covalently linked.

Photolyase is typically used in topical creams or sunscreens which are used to prevent UV damage, and in therapy to restore the skin from conditions such as premature photoaging, actinic keratosis, and squamous cell carcinoma.

The photolyase enzyme reactivates DNA by direct repair of T>T lesions. It binds to the damaged DNA site, absorbs a (near UV-visible) photon, restores the pyrimidines to their monomeric forms, and dissociates from the substrate.

Photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) and pyrimidine-pyrimidone (6-4) photoproduct using blue light.

Photolyase, a class of flavoproteins, uses blue light to repair two types of ultraviolet-induced DNA damage, cyclobutane pyrimidine dimer (CPD) and pyrimidine-pyrimidone (6–4) photoproduct (6–4PP). In this perspective, we review the recent progress ...

Photolyase is an enzyme that plays a crucial role in the DNA repair process by specifically recognizing and repairing UV-induced damage, particularly pyrimidine dimers. This enzyme uses the energy from light to catalyze the cleavage of these dimers, thereby restoring the DNA to its normal structure and function.

Photolyases are CPD- or 6-4PP-specific enzymes that revert the lesions using the energy of visible light. Photolyase bends DNA by about 50° and flip out the pyrimidine dimer from the double helix into the active site cavity [153].

Photoreactivation results from the repair of these lesions in situ by flavoproteins called photoreactivating enzymes (photolyase) that use a blue-light photon as a co-substrate. Photolyases that repair these two photoproducts are evolutionarily related but functionally distinct.

Jan 11, 1994 · Photoreactivating enzyme (DNA photolyase) repairs DNA by utilizing the energy of visible light to break the cyclobutane ring of the dimer. Photolyases are monomeric proteins of 50-60 kDa with stoichiometric amounts of two noncovalent chromophore/cofactors.

Photolyases catalyze light-triggered repair of CPD-DNA, thus contributing to genome stability in many organisms. Combining time-resolved crystallography and computational analyses, we report an atomic visualization of the photolyase-catalyzed DNA repair process.