Literature summary for 4.1.99.3 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 .

Search for more literature for 4.1.99.3

Activating Compound

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

Cloned(Commentary)

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P00914	-	-

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
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)

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

Synonyms

Synonyms	Comment	Organism
DNA photolyase	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
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
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

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)