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Literature summary 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

Application

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

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.3 additional information mutation of Q403 and K406 affect the affinity toward cyclobutane-pyrimidine dimer-containing DNA Escherichia coli
4.1.99.3 additional information mutation of Q411 and K414 affect the affinity toward cyclobutane-pyrimidine dimer-containing DNA Aspergillus nidulans
4.1.99.3 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
4.1.99.3 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
4.1.99.3 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

EC Number Organism UniProt Comment Textmining
4.1.99.3 Arabidopsis thaliana
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-
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4.1.99.3 Aspergillus nidulans
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-
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4.1.99.3 Escherichia coli P00914
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4.1.99.3 Potorous tridactylus
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Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.3 FADH2 the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue Arabidopsis thaliana
4.1.99.3 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
4.1.99.3 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