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Literature summary for 4.1.99.3 extracted from

  • MacFarlane, A.W.t.; Stanley, R.J.
    cis-syn Thymidine dimer repair by DNA photolyase in real time (2003), Biochemistry, 42, 8558-8568.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Synechococcus elongatus PCC 7942 = FACHB-805

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclobutadipyrimidine in DNA Synechococcus elongatus PCC 7942 = FACHB-805
-
2 pyrimidine residues in DNA
-
?

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
Synechococcus elongatus PCC 7942 = FACHB-805

Reaction

Reaction Comment Organism Reaction ID
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) mechanism Synechococcus elongatus PCC 7942 = FACHB-805

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclobutadipyrimidine in DNA
-
Synechococcus elongatus PCC 7942 = FACHB-805 2 pyrimidine residues in DNA
-
?
cyclobutadipyrimidine in DNA dimeric and pentameric oligothymidine substrates, repairs cyclobutylpyrimidine dimers via photoinduced electron transfer from a reduced flavin adenine dinucleotide cofactor to the bound cyclobutylpyrimidine dimer Synechococcus elongatus PCC 7942 = FACHB-805 2 pyrimidine residues in DNA
-
?

Synonyms

Synonyms Comment Organism
PL
-
Synechococcus elongatus PCC 7942 = FACHB-805

Cofactor

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