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Literature summary for 4.1.99.3 extracted from

  • Masson, F.; Laino, T.; Rothlisberger, U.; Hutter, J.
    A QM/MM investigation of thymine dimer radical anion splitting catalyzed by DNA photolyase (2009), Chemphyschem, 10, 400-410.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E283A the mutation impairs enzyme activity by diminishing the quantum yield for the repair reaction by 60% Synechococcus elongatus PCC 7942 = FACHB-805
R350A the mutation demonstrates a 60% decrease in quantum yield, which indicates that Arg350 plays a key role in stabilizing the dimer Synechococcus elongatus PCC 7942 = FACHB-805

Organism

Organism UniProt Comment Textmining
Synechococcus elongatus PCC 7942 = FACHB-805
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclobutadipyrimidine in DNA
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Synechococcus elongatus PCC 7942 = FACHB-805 pyrimidine residues in DNA
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Subunits

Subunits Comment Organism
dimer x-ray crystallography Synechococcus elongatus PCC 7942 = FACHB-805

Synonyms

Synonyms Comment Organism
CPD photolyase
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Synechococcus elongatus PCC 7942 = FACHB-805
photolyase
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Synechococcus elongatus PCC 7942 = FACHB-805

Cofactor

Cofactor Comment Organism Structure
FADH2
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Synechococcus elongatus PCC 7942 = FACHB-805