Literature summary for 4.1.99.13 extracted from

Todo, T.; Takemori, H.; Ryo, H.; Ihara, M.; Matsunaga, T.; Nikaido, O.; Sato, K.; Nomura, T.
A new photoreactivating enzyme that specifically repairs ultraviolet light-induced (6-4)photoproducts (1993), Nature, 361, 371-374.

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Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by fractionation of crude cell extracts with Heparin agarose and UV DNA affinity column chromatography	Drosophila melanogaster

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	Drosophila melanogaster	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme catalyzes the light-dependent repair of (6-4) photoproducts in Drosophilia melanogaster	Drosophila melanogaster	?	-	?

Synonyms

Synonyms	Comment	Organism
(6-4) photolyase	-	Drosophila melanogaster

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Drosophila melanogaster

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Release 2023.1 (January 2023)