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Literature summary extracted from

  • Yamamoto, A.; Tanbir, N.; Hirouchi, T.; Teranishi, M.; Hidema, J.; Morioka, H.; Yamamoto, K.
    Temperature-sensitive photoreactivation of cyclobutane thymine dimer in soybean (2008), J. Radiat. Res., 49, 189-196.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.3 expressed in a photolyase-deficient Escherichia coli strains NKJ3002 and KY20 Glycine max

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.99.3 85000
-
 SDS-PAGE Glycine max

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.3 Glycine max B1B538
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.3 partial purification, glutathione-Sepharose column chromatography Glycine max

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.3 cyclobutadipyrimidine in DNA
-
 Glycine max pyrimidine residues in DNA
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.99.3 ? x * 85000, SDS-PAGE Glycine max

Synonyms

EC Number Synonyms Comment Organism
4.1.99.3 CDP photolyase class II CPD photolyase Glycine max

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.99.3 25 45 when CDP photolyase is heat-treated in vitro from 25 to 45°C for 3 min, thymine dimer-binding activity and photoreactivation activity are decreased and FAD is released from the enzyme, on the other hand photoreactivation activity is stable when the enzyme-CDP complex is heat-treated from 25 to 45°C, the enzyme alone is unstable but once it binds to a substrate the enzyme becomes thermostable Glycine max

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.3 FAD
-
 Glycine max