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Literature summary for 4.1.99.3 extracted from

  • Moldt, J.; Pokorny, R.; Orth, C.; Linne, U.; Geisselbrecht, Y.; Marahiel, M.A.; Essen, L.O.; Batschauer, A.
    Photoreduction of the folate cofactor in members of the photolyase family (2009), J. Biol. Chem., 284, 21670-21683.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
cry3 cocrystallized with a thymine dimer-comprising oligonucleotide containing a synthetic CPD-like lesion. When cocrystals are exposed to UV-A at 180 K, a decrease in absorption at 380 nm together with the accumulation of semiquinoid and probably also fully reduced FAD is observed. Initial strong fluorescence emission of 5,10-methenyltetrahydrofolate at 440-460 nm seen for cry3 in solution is decreased in the crystal Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
W356F photobleaching of 5,10-methenyltetrahydrofolate under UV-A irradiation is strongly reduced in the mutant compared with wild-type. The amount of 5,10-methenyltetrahydrofolate after UV-A irradiation is reduced by 64% for wild-type and by 20% for the mutant. Increase in the amount of oxidized FAD under UV-A irradiation due to electron donation to 5,10-methenyltetrahydrofolate by residual FADH- but a lack of photoreduction of the flavin caused by the interrupted tryptophan triad Arabidopsis thaliana
W432F photobleaching of 5,10-methenyltetrahydrofolate under UV-A irradiation is strongly reduced in the mutant compared with wild-type Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-
Escherichia coli
-
-
-

Synonyms

Synonyms Comment Organism
cry3
-
Arabidopsis thaliana
DASH cryptochrome
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Arabidopsis thaliana
DNA photolyase
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
5,10-methenyltetrahydrofolate an electron transfer pathway exists in DASH cryptochrome, where the 5,10-methenyltetrahydrofolate cofactor is photoreduced to 5,10-methylenetetrahydrofolate. Reduction requires the intact tryptophan triad. DASH cryptochrome forms 5,10-methylenetetrahydrofolate when treated with UV-A. Light-driven formation of 5,10-methylenetetrahydrofolate by DASH cryptochrome can be coupled with the formation of NADPH in the presence of 5,10-methylenetetrahydrofolate dehydrogenase Arabidopsis thaliana
5,10-methenyltetrahydrofolate an electron transfer pathway exists in photolyase, where the 5,10-methenyltetrahydrofolate cofactor is photoreduced to 5,10-methylenetetrahydrofolate. Reduction requires the intact tryptophan triad. Photolyase forms 5,10-methylenetetrahydrofolate when treated with UV-A. Light-driven formation of 5,10-methylenetetrahydrofolate by photolyase can be coupled with the formation of NADPH in the presence of 5,10-methylenetetrahydrofolate dehydrogenase Escherichia coli
FAD photoreduction of FAD under blue light irradiation is faster in photolyase than in Arabidopsis cry3 Escherichia coli
FAD photoreduction of FAD under blue light irradiation is faster in photolyase than in Arabidopsis cry3 Arabidopsis thaliana

General Information

General Information Comment Organism
metabolism third electron transfer pathway exists in members of the photolyase family that remained undiscovered so far Escherichia coli
metabolism third electron transfer pathway exists in members of the photolyase family, e.g. DASH cryptochrome, that remained undiscovered so far Arabidopsis thaliana