Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Protein Variants Comment Organism
4.1.99.3 E283A the mutation impairs enzyme activity by diminishing the quantum yield for the repair reaction by 60% Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 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

EC Number Organism UniProt Comment Textmining
4.1.99.3 Synechococcus elongatus PCC 7942 = FACHB-805
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Cofactor

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