Photolyase

Cryptochrome/photolyase, C-terminal, FAD binding
A deazaflavin photolyase from Anacystis nidulans, illustrating the two light-harvesting cofactors: FADH (yellow) and 8-HDF (cyan).
Identifiers
SymbolFAD_binding_7
PfamPF03441
InterProIPR005101
PROSITEPDOC00331
SCOP21qnf / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1u3cA:214-492 1u3dA:214-492 1iquA:176-418

1iqrA:176-418 1dnpB:202-469 1tezD:207-472 1owmA:207-472 1qnf :207-472 1owpA:207-472 1owoA:207-472 1owlA:207-472 1ownA:207-472

1np7B:213-453
deoxyribodipyrimidine photo-lyase (CPD)
A UV radiation induced thymine-thymine cyclobutane dimer (right) is the type of DNA damage which is repaired by DNA photolyase. Note: The above diagram is incorrectly labelled as thymine as the structures lack 5-methyl groups.
Identifiers
EC no.4.1.99.3
CAS no.37290-70-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Photolyases (EC 4.1.99.3) are DNA repair enzymes that repair damage caused by exposure to ultraviolet light. These enzymes require visible light (from the violet/blue end of the spectrum) both for their own activation and for the actual DNA repair. The DNA repair mechanism involving photolyases is called photoreactivation. They mainly convert pyrimidine dimers into a normal pair of pyrimidine bases. Photo reactivation, the first DNA repair mechanism to be discovered, was described initially by Albert Kelner in 1949 and independently by Renato Dulbecco also in 1949.