Literature summary for 4.1.99.13 extracted from

Kim, S.T.; Malhotra, K.; Taylor, J.S.; Sancar, A.
Purification and partial characterization of (6-4) photoproduct DNA photolyase from Xenopus laevis (1996), Photochem. Photobiol., 63, 292-295.

Search for more literature for 4.1.99.13

Activating Compound

Activating Compound	Comment	Organism	Structure
DTT	-	Xenopus laevis
DTT	-	Crotalus atrox

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Na+	-	Xenopus laevis
Na+	-	Crotalus atrox

Organism

Organism	UniProt	Comment	Textmining
Crotalus atrox	-	-	-
Xenopus laevis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
(6-4) photoproduct DNA photolyase activity is detected in Crotalus atrox fibroblast. Activity is considerably enhanced when a UV-damaged DNA affinity column is used for purification. However, the activity is unstable and it is lost during purification or upon storage at -20° or -70°C for 2-3 months	Crotalus atrox
protein is isolated from whole cell extracts from Xenopus laevis, purified by using a sepharose column and a UV-damaged DNA affinity column	Xenopus laevis

Reaction

Reaction	Comment	Organism	Reaction ID
(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA)	The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent. In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases.This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack. In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH-) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures. The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases	Xenopus laevis	a
(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA)	The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent. In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases.This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack. In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH-) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures. The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases	Crotalus atrox	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
fibroblast	-	Crotalus atrox	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	activity is unstable	Crotalus atrox

Storage Stability

Storage Stability	Organism
activity is unstable and it is lost upon storage at -20° or -70°C for 2-3 months	Crotalus atrox
protein in aliquots is kept at -20°C until further use or stored at -80°C. The protein sample remained active after 6 months storage	Xenopus laevis

Synonyms

Synonyms	Comment	Organism
(6-4) photolyase	-	Xenopus laevis
(6-4) photolyase	-	Crotalus atrox

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Xenopus laevis
7.4	-	assay at	Crotalus atrox

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Xenopus laevis
FAD	-	Crotalus atrox

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Release 2023.1 (January 2023)