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Literature summary for 4.1.99.3 extracted from

  • Essen, L.O.; Klar, T.
    Light-driven DNA repair by photolyases (2006), Cell. Mol. Life Sci., 63, 1266-1277.
    View publication on PubMed
Search for more literature for 4.1.99.3

Application

Application Comment Organism
medicine exploring therapeutic possibilities of ectopic CPD photolyase expression Potorous tridactylus

Protein Variants

Protein Variants Comment Organism
additional information mutation of Q403 and K406 affect the affinity toward cyclobutane-pyrimidine dimer-containing DNA Escherichia coli
additional information mutation of Q411 and K414 affect the affinity toward cyclobutane-pyrimidine dimer-containing DNA Aspergillus nidulans
additional information transgenic mice are generated with a transgene for a marsupial CPD photolyase. These mice exhibit a 40% increase of repair for CPD lesions in intact skin and cultured fibroblasts that is accompanied by an improved resistance against acute UV-induced effects like erythema (sunburn), epidermal hyperplasia or apoptosis. Expression of the CPD photolyase in mice efficiently suppresses the formation of skin carcinomas Potorous tridactylus
R342A conserved arginine forms a salt bridge with phosphate+1. Among several active-site mutants this R/A mutant is found to exhibit the greatest effect by lowering the selectivity toward cyclobutane-pyrimidine dimer-containing DNA 32-fold and the quantum yield of CPD cleavage from 98% to about 60% Escherichia coli
R350A conserved arginine forms a salt bridge with phosphate+1. Among several active-site mutants this R/A mutant is found to exhibit the greatest effect by lowering the selectivity toward cyclobutane-pyrimidine dimer-containing DNA 32-fold and the quantum yield of CPD cleavage from 98% to about 60% Aspergillus nidulans

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
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Aspergillus nidulans
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Escherichia coli P00914
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Potorous tridactylus
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Synonyms

Synonyms Comment Organism
CPD photolyase
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 Potorous tridactylus
Cry1
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 Aspergillus nidulans
Cry1
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 Arabidopsis thaliana
DNA photolyase
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 Aspergillus nidulans
DNA photolyase
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 Arabidopsis thaliana
DNA photolyase
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 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FADH2 the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue Arabidopsis thaliana
FADH2 the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378 Escherichia coli
FADH2 the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H) Aspergillus nidulans