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

BRENDA support

Literature summary extracted from

  • Xu, L.; Zhang, D.; Mu, W.; van Berkel, W.J.; Luo, Z.
    Reversible resolution of flavin and pterin cofactors of His-tagged Escherichia coli DNA photolyase (2006), Biochim. Biophys. Acta, 1764, 1454-1461.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.3 cloned in Escherichia coli as a C-terminal His-tagged fusion protein Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.3 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.3 by using Ni2+ chelating Sepharose Fast Flow columns and Sephadex gel filtration resins. Methenyltetrahydrofolate-free photolyase is obtained by binding the C-terminal His-tagged holoenzyme to a metal-affinity column at neutral pH and washing the column with deionized water. The defolated enzyme can be eluated with 0.5 M imidazole pH 7.2. Apo-photolyase is obtained by treating the His-tagged holoenzyme with 0.5 M imidazole pH 10.0 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.99.3 additional information
-
 activity of freshly prepared holoenzyme methenyltetrahydrofolate + FADH is considered 100%. After methenyltetrahydrofolate cofactor removal the activity of the enzyme decreases to 70%, reconstituted oxidized photolyase shows the lowest activity with 34%. Activity after dithionite reduction: 83% Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.1.99.3 DNA photolyase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.3 20
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.3 FAD
-
 Escherichia coli
4.1.99.3 methenyltetrahydrofolate
-
 Escherichia coli