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Literature summary for 4.1.99.3 extracted from

  • Thiagarajan, V.; Villette, S.; Espagne, A.; Eker, A.P.; Brettel, K.; Byrdin, M.
    DNA repair by photolyase: a novel substrate with low background absorption around 265 nm for transient absorption studies in the UV (2010), Biochemistry, 49, 297-303.
    View publication on PubMed

Application

Application Comment Organism
analysis the novel substrate (a modified thymidine 10-mer with a central CPD and all bases, except the one at the 3' end, replaced by 5,6-dihydrothymine) is a promising tool for fast and ultrafast transient absorption studies on pyrimidine dimer splitting by CPD photolyase Escherichia coli
analysis the novel substrate (a modified thymidine 10-mer with a central cyclobutane pyrimidine dimer and all bases, except the one at the 3' end, replaced by 5,6-dihydrothymine) is a promising tool for fast and ultrafast transient absorption studies on pyrimidine dimer splitting by CPD photolyase Synechococcus elongatus PCC 7942 = FACHB-805

Cloned(Commentary)

Cloned (Comment) Organism
apophotolyase (devoid of the antenna cofactor 5,10-methenyltetrahydrofolate) overproduced in Escherichia coli Synechococcus elongatus PCC 7942 = FACHB-805
holophotolyase (both flavin and antenna cofactor 5,10-methenyltetrahydrofolate present) overexpressed Escherichia coli

Protein Variants

Protein Variants Comment Organism
E109A lacks the antenna cofactor Escherichia coli

Organism

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

Purification (Commentary)

Purification (Comment) Organism
apophotolyase Synechococcus elongatus PCC 7942 = FACHB-805
holophotolyase Escherichia coli

Storage Stability

Storage Stability Organism
-80°C, 2-mercaptoethanol, 20% glycerol Synechococcus elongatus PCC 7942 = FACHB-805
-80°C, 2-mercaptoethanol, 20% glycerol Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information a novel substrate (a modified thymidine 10-mer with a central cyclobutane pyrimidine dimer and all bases, except the one at the 3' end, replaced by 5,6-dihydrothymine) is repaired with an efficiency very similar to that of the conventional substrates (a 10-mer of unmodified thymidines containing a central cyclobutane pyrimidine dimer and an acetone-sensitized thymidine 18-mer containing in average six randomly distributed cyclobutane pyrimidine dimers per strand) Synechococcus elongatus PCC 7942 = FACHB-805 ?
-
?
additional information a novel substrate (a modified thymidine 10-mer with a central cyclobutane pyrimidine dimer and all bases, except the one at the 3' end, replaced by 5,6-dihydrothymine) is repaired with an efficiency very similar to that of the conventional substrates (a 10-mer of unmodified thymidines containing a central cyclobutane pyrimidine dimer and an acetone-sensitized thymidine 18-mer containing in average six randomly distributed cyclobutane pyrimidine dimers per strand). Significantly lower repair quantum yield for the holoenzyme compared to its apo form due to an additional process, i.e., excitation energy transfer from the antenna cofactor to the reduced flavin Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
CPD photolyase
-
Synechococcus elongatus PCC 7942 = FACHB-805
CPD photolyase photolyase
-
Escherichia coli
cyclobutane pyrimidine dimer photolyase
-
Synechococcus elongatus PCC 7942 = FACHB-805
cyclobutane pyrimidine dimer photolyase
-
Escherichia coli
photolyase
-
Synechococcus elongatus PCC 7942 = FACHB-805

Cofactor

Cofactor Comment Organism Structure
5,10-methenyltetrahydrofolate
-
Synechococcus elongatus PCC 7942 = FACHB-805
5,10-methenyltetrahydrofolate antenna cofactor Escherichia coli
FAD
-
Synechococcus elongatus PCC 7942 = FACHB-805
FAD
-
Escherichia coli