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Literature summary for 4.1.99.3 extracted from

  • Komori, H.; Masui, R.; Kuramitsu, S.; Yokoyama, S.; Shibata, T.; Inoue, Y.; Miki, K.
    Crystal structure of thermostable DNA photolyase: pyrimidine-dimer recognition mechanism (2001), Proc. Natl. Acad. Sci. USA, 98, 13560-13565.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
vapor diffusion method, native enzyme and complexed with thymine Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclobutadipyrimidine in DNA Thermus thermophilus
-
 2 pyrimidine residues in DNA
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus P61497
-
-

Reaction

Reaction Comment Organism Reaction ID
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) mechanism Thermus thermophilus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclobutadipyrimidine in DNA
-
 Thermus thermophilus 2 pyrimidine residues in DNA
-
 ?
cyclobutadipyrimidine in DNA repairs cyclobutylpyrimidine dimers by using visible light Thermus thermophilus 2 pyrimidine residues in DNA
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD enzyme contains two chromophore cofactors: FAD is a catalytic cofactor which directly contributes to the repair of a pyrimidine-dimer, the other is an unidentified light harvesting cofactor, which absorbs visible light and transfers energy to the catalytic cofactor Thermus thermophilus