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Literature summary extracted from

  • Thiagarajan, V.; Byrdin, M.; Eker, A.P.; Mueller, P.; Brettel, K.
    Kinetics of cyclobutane thymine dimer splitting by DNA photolyase directly monitored in the UV (2011), Proc. Natl. Acad. Sci. USA, 108, 9402-9407.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.3
-
 Aspergillus nidulans

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.3 Aspergillus nidulans
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.99.3 cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) using a transient absorption setup, cyclobutane thymine dimer repair in the main UV absorption band of intact thymine at 266 nm is monitored. Flavin transitions that overlay DNA-based absorption changes at 266 nm are monitored independently in the visible and subtracted to obtain the true repair kinetics. Restoration of intact thymine show a short lag and a biexponential rise with time constants of 0.2 and 1.5 ns. The two time constants are assigned to splitting of the intradimer bonds (creating one intact thymine and one thymine anion radical T-) and electron return from T- to the FAD cofactor with recovery of the second thymine, respectively Aspergillus nidulans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.3 cyclobutadipyrimidine in DNA the substrate is a modified thymidine 10-mer with a central T = T and all other bases, except the one at the 3' end, replaced by 5,6-dihydrothymine (5S:5R stereoisomer ratio 90:10) Aspergillus nidulans pyrimidine residues in DNA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.3 CPD photolyase
-
 Aspergillus nidulans

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.3 FAD
-
 Aspergillus nidulans