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Literature summary extracted from

  • Narayanan, M.; Singh, V.R.; Kodali, G.; Moravcevic, K.; Stanley, R.J.
    An ethenoadenine FAD analog accelerates UV dimer repair by DNA photolyase (2017), Photochem. Photobiol., 93, 343-354 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.99.3 ethenoadenine the FAD analogue accelerates UV dimer repair by DNA photolyase Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.3 gene phrB, overexpression in MS09 cells Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.3 cyclobutadipyrimidine (in DNA) Escherichia coli
-
 2 pyrimidine residues (in DNA)
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.3 Escherichia coli P00914
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.3 recombinant enzyme from MS09 cells by ammonium sulfate fractionation and gel filtration, followed by an adsorption chromatography, and heparin affinity chromatography Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.99.3 cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) reduced anionic flavin adenine dinucleotide (FADH-) is the critical cofactor in DNA photolyase (PL) for the repair of cyclobutane pyrimidine dimers (CPD) in UV-damaged DNA. The initial step involves photoinduced electron transfer from FADH- radical to the CPD. The adenine (Ade) moiety is nearly stacked with the flavin ring, an unusual conformation compared to other FAD-dependent proteins Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Escherichia coli 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 additional information anaerobic repair assay in argon atmosphere Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.3 DNA photolyase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.3 FAD reduced anionic flavin adenine dinucleotide (FADH-) is the critical cofactor in DNA photolyase (PL) for the repair of cyclobutane pyrimidine dimers (CPD) in UV-damaged DNA Escherichia coli
4.1.99.3 additional information FAD analogues containing either an ethano- or etheno-bridged Ade between the AN1 and AN6 atoms (e-FAD and epsilon-FAD, respectively) are used to reconstitute apo-PL, giving e-PL and epsilon-PL, respectively. The reconstitution yield of e-PL is very poor, suggesting that the hydrophobicity of the ethano group prevents its uptake, while epsilon-PL shows 50% reconstitution yield. The substrate binding constants for epsilon-PL and rPL are identical. epsilon-PL shows a 15% higher steady-state repair yield compared to FAD-reconstituted photolyase (rPL). Evaluation of an epsilon-Ade radical intermediate versus a superexchange mechanism, preparation of apophotolyase (apo-PL) and reconstitution of apo-PL with FAD, e-FAD and epsilon-FAD, overview. Incorporation of the more hydrophobic e-FAD is so inefficient that it can not be made in sufficient quantities to study further. Ligand binding structure analysis Escherichia coli

General Information

EC Number General Information Comment Organism
4.1.99.3 additional information reduced anionic flavin adenine dinucleotide (FADH-) is the critical cofactor in DNA photolyase (PL) for the repair of cyclobutane pyrimidine dimers (CPD) in UV-damaged DNA. The initial step involves photoinduced electron transfer from FADH- radical to the CPD. The adenine (Ade) moiety is nearly stacked with the flavin ring, an unusual conformation compared to other FAD-dependent proteins Escherichia coli