Literature summary for 4.1.99.13 extracted from

Zhang, Y.; Iwata, T.; Yamamoto, J.; Hitomi, K.; Iwai, S.; Todo, T.; Getzoff, E.D.; Kandori, H.
FTIR study of light-dependent activation and DNA repair processes of (6-4) photolyase (2011), Biochemistry, 50, 3591-3598.

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Organism

Organism	UniProt	Comment	Textmining
Xenopus laevis	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA)	Fourier transform infrared spectroscopy is applied to (6-4)DNA photolyase. Differences in FTIR spectra that correspond to (6-4)DNA photolyase photoactivation, substrate binding, and light-dependent DNA repair processes are reported. The presence of DNA carrying a single (6-4) PP uniquely influences vibrations of the protein backbone and a protonated carboxylic acid, whereas photoactivation produces IR spectral changes for the FAD cofactor and the surrounding protein. Difference FTIR spectra for the light-dependent DNA damage repair reaction directly show significant DNA structural changes in the (6-4) lesion and the neighboring phosphate group. Time-dependent illumination of samples with different enzyme:substrate stoichiometries successfully distinguish signals characteristic of structural changes in the protein and the DNA resulting from binding and catalysis	Xenopus laevis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(6-4) photoproduct (in DNA)	-	Xenopus laevis	2 pyrimidine residues (in DNA)	-	?

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Xenopus laevis

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Release 2023.1 (January 2023)