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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the reaction is initiated by blue light and proceeds through long-range energy transfer, single electron transfer and enzyme catalysis by a radical mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism of photoactivation
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
results support the electron hopping mechanism by which electron transfer from W306 to the flavin is mediated in a three-step electron hopping process (W306 to W359 to W382 to FADH)
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
by molecular dynamics simulation and quantum mechanical calculations it is shown that indirect electron tunneling via the protein medium is as important as direct electron transfer from the donor (FADH-) to the acceptor (cyclobutane pyrimidine dimmer). At Met353 site busy electron tunneling traffic is observed.
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
upon absorption of a visible photon, the photoexcited flavin radical FADH abstracts an electron from nearby W382. The tryptophanyl radical W382 thus formed abstracts an electron from the nearby middle tryptophan, W359. W359 radical abstracts an electron from W306. As the second and third steps are faster than the first one, the intermediate states are not populated in wild-type photolyase to any significant extent and escape spectroscopic detection. The described forward electron transfer steps between the tryptophans are in competition with back electron transfer from FADH- to the respective tryptophanyl cation radical, so that the quantum yield of formation of the terminal W306 radical is only 20%. W306 radical releases a proton to the aqueous phase in 200 ns. The resulting neutral radical W306 radical can be reduced by extrinsic reductants, leaving a photolyase that contains FADH as required for photorepair of DNA
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
on top of the transient formation of tryptophan radicals during photoactivation, evidence is found for oxidation of a tyrosine residue by a tryptophan radical. The tyrosine radical thus formed is reduced by an extrinsic reductant, suggesting that in this case the terminal intrinsic electron donor is tyrosine rather than tryptophan
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
using a transient absorption setup, cyclobutane thymine dimer repair in the main UV absorption band of intact thymine at 266 nm is monitored. Flavin transitions that overlay DNA-based absorption changes at 266 nm are monitored independently in the visible and subtracted to obtain the true repair kinetics. Restoration of intact thymine show a short lag and a biexponential rise with time constants of 0.2 and 1.5 ns. The two time constants are assigned to splitting of the intradimer bonds (creating one intact thymine and one thymine anion radical T-) and electron return from T- to the FAD cofactor with recovery of the second thymine, respectively
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism, detailed overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
substrate/cofactor binding and reaction mechanism, catalytic active site Met397, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the DNA repair enzyme recognizes a solvent-exposed cyclobutadipyrimidine as part of its damage recognition mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
cyclic electron-transfer radical mechanism with two fundamental processes, electron-tunneling pathways and cyclobutane ring splitting, the cyclobutane pyrimidine dimer splits in two sequential steps within 90 ps and the electron tunnels between the cofactor and substrate through a remarkable route with an intervening adenine, dynamics and mechanism of cyclobutane pyrimidine dimer repair by DNA photolyase, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
radical mechanism through a cyclic redox reaction. Photolyase binds DNA containing a CPD because the thymine dimer distorts the backbone of the DNA. Upon binding to damaged DNA, through ionic interactions between the positively charged groove on the photolyase surface and negatively charged DNA phosphodiester backbone the enzyme pulls the thymine dimer out from within the helix and into the core of the enzyme so that the thymine dimer is within Van der Waals contact with FADH-. It makes a very staple complex, and nothing happens until folate absorbs a photon and transfers the excitation energy to the flavin cofactor. The excited-state flavin, FADH- radical, repairs the thymine dimer by a cyclic redox reaction, and then the enzyme dissociates from the DNA to go on in search of other damage sites to carry out the repair reactions again
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview; the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
molecular mechanism of the electron transfer, overview. The electronic coupling matrix element is 36/cm from the donor (FADH-) to the acceptor (CPD) by Mulliken-Hush (GMH) method and the bridge green function (GF) methods, and the estimated electron transfer time is 386 ps. Molecular dynamics simulations and ab initio molecular orbital calculations, and exploration of the electron tunneling pathway for 20 different structures during the MD trajectory, QM/MM calculation. The electron transfer route via Asn349 is the dominant pathway among the five major routes via (adenine/Asn349), (adenine/Glu283), (adenine/Glu283/Asn349/Met353), (Met353/Asn349), and (Asn349), indicating that Asn349 is an essential amino acid residue in the electron transfer reaction
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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
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview. Proposed intraprotein electron transfer from W306 to FADH radical is not a part of the normal photolyase photocycle in vivo
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview; reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
dynamics and mechanism of CPD repair by photolyase, detailed overview. In contrast to the computational reaction model the thymine dimer splits by a sequential pathway
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview; photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
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-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism
-
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview
-
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
-
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism, detailed overview
-
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
molecular mechanism of the electron transfer, overview. The electronic coupling matrix element is 36/cm from the donor (FADH-) to the acceptor (CPD) by Mulliken-Hush (GMH) method and the bridge green function (GF) methods, and the estimated electron transfer time is 386 ps. Molecular dynamics simulations and ab initio molecular orbital calculations, and exploration of the electron tunneling pathway for 20 different structures during the MD trajectory, QM/MM calculation. The electron transfer route via Asn349 is the dominant pathway among the five major routes via (adenine/Asn349), (adenine/Glu283), (adenine/Glu283/Asn349/Met353), (Met353/Asn349), and (Asn349), indicating that Asn349 is an essential amino acid residue in the electron transfer reaction; photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview; the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview; reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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adenosine 5'-(beta,gamma-imido)triphosphate
?
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Cry1
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cis,syn-cyclobutane pyrimidine dimer
2 pyrimidine residues
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substrate binding and substrate conformation by isothermal titration calorimetry, overview
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?
cis-syn cyclobutadipyrimidine dimer DNA
pyrimidine residues in DNA
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
cyclobutadipyrimidine in calf thymus DNA
2 pyrimidine residues in calf thymus DNA
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optimal activity at 400 nm wavelength, no activity at 300 nm, 500 nm and in the dark
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
cyclobutadipyrimidine in DNA
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
cyclobutadipyrimidine in minichromosomes
2 pyrimidine residues in minichromosomes
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removes cyclobutane pyrimidine dimers predominantly from the ARS1 region
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?
cyclobutadipyrimidine in nucleosome DNA
2 pyrimidine residues in nucleosome DNA
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folding of DNA in nucleosomes efficiently protects DNA from being repaired
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?
cyclobutadipyrimidine in oligodeoxythymidylates
pyrimidine residues in oligodeoxythymidylates
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minimum size is about 9 residues
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?
cyclobutadipyrimidine in RNA
2 pyrimidine residues in RNA
cyclobutadipyrimidine in salmon sperm DNA
2 pyrimidine residues in salmon sperm DNA
cyclobutadipyrimidine in yeast urea3 gene
2 pyrimidine residues in yeast urea3 gene
thymine dimers in AnCPDI and Atcry3 complexes
?
additional information
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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enzyme AtCRY3 is specific for single-stranded DNA substrates
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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photolyases utilize near-ultraviolet blue light to specifically repair the major photoproducts of UV-induced damaged DNA. The enzyme specifically repairs CPD lesions
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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repair of a single CPD lesion within a double-stranded DNA molecule
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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various CPD substrates, T-T, T-U, U-T, U-U dimers
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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the entire catalytic cycle is complete in 1.2 ns, and the enzyme repairs thymine dimer with a quantum yield of 0.9
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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-
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the substrate used in binding experiments, UV-p(dT)10 (denoted as ssDNA), is a single strand oligothymidylate with an average of a single CPD lesion randomly arranged on the 10mer
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the substrate used in binding experiments, UV-p(dT)10 (denoted as ssDNA), is a single strand oligothymidylate with an average of a single CPD lesion randomly arranged on the 10mer
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme is involved in biological photoreactivation
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme is involved in biological photoreactivation
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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-
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio parahaemolyticus serotype 03:KG
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio parahaemolyticus serotype 03:KG RIMD 2210633
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Xiphophorus maculatus Jp 163 B
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
repairs cyclobutylpyrimidine dimers by a light-driven electron transfer
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
two photolyases specific for photoreactivation of either cyclobutane pyrimidine dimers or pyrimidine (6-4)pyrimidones
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
AtCry3 repairs the dimer but only in ssDNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
enzyme uses light to repair cyclobutylpryrimidine dimers in DNA, local structure around the thymidine lesion changes dramatically upon binding to photolyase
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
upon binding of DNA, the enzyme flips the pyrimidine dimer out of the duplex into a hole that contains the catalytic cofactor. The cyclobutane ring is then split by a light-initiated electron transfer reaction
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
steady-state fluorescence measurements of single- and double-stranded oligonucleotides shows that the local region around the 5'-side of the cyclobutadipyrimidine lesion is more disrupted and destacked than the 3'-side in substrate-protein complexes
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
active genes are faster repaired than silenced genes
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
active genes are faster repaired than silenced genes
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
dimeric and pentameric oligothymidine substrates, repairs cyclobutylpyrimidine dimers via photoinduced electron transfer from a reduced flavin adenine dinucleotide cofactor to the bound cyclobutylpyrimidine dimer
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
repairs cyclobutylpyrimidine dimers by using visible light
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
specific for cyclobutane pyrimidine dimers
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
DNA repair activity
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
VcCry1 repairs the dimer but only in ssDNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
XlCry-DASH repairs the dimer but only in ssDNA
-
-
?
cyclobutadipyrimidine in DNA
?
-
compared to the wild-type the rate of cyclobutane pyrimidine dimer accumulation is increased in the uvr2-1 mutant but decreases in the CPD photolyase overexpressors. Under conditions without UV-B, overexpression of photolyase does not have any negative effect on growth
-
-
?
cyclobutadipyrimidine in DNA
?
-
-
-
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme binds to DNA containing pyrimidine dimers with high affinity and then breaks the cyclobutane ring joining the two pyrimidines of the dimer in a light-dependent reaction, 300-500 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
about 20times more pyrimidine dimers are bound to the yeast photolyase than to the Escherichia coli photolyase. Ratio between the enzyme's binding constant for pyrimidine dimers and its binding constant for nondamaged DNA is very similar for yeast and Escherichia coli photolyases
-
-
?
cyclobutadipyrimidine in DNA
?
-
photolyase binds tighter to substrate than cryptochrome 1, binding constant is slightly sensitive to oxidation state
-
-
?
cyclobutadipyrimidine in DNA
?
-
presence of a very rigid antenna binding site, a relatively rigid active site in CPD photolyase but with large local orientation flexibility
-
-
?
cyclobutadipyrimidine in DNA
?
-
-
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
about 20times more pyrimidine dimers are bound to the yeast photolyase than to the Escherichia coli photolyase. Ratio between the enzyme's binding constant for pyrimidine dimers and its binding constant for nondamaged DNA is very similar for yeast and Escherichia coli photolyases
-
-
?
cyclobutadipyrimidine in DNA
?
-
the larger N-terminal domain of primase carboxy-terminal domain (PriL-CTD) assists the smaller catalytic subunit PriS in the simultaneous binding of the two initial ribonucleotides and in promoting their Watson-Crick base pairing at the initiation site on the template DNA
-
-
?
cyclobutadipyrimidine in DNA
?
-
-
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
photolyase binds tighter to substrate than cryptochrome 1, binding constant is slightly sensitive to oxidation state
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
the enzyme repairs specifically cyclobutane pyrimidine dimers in UV-damaged single-stranded DNA, the enzyme catalyzes light-driven DNA repair like conventional photolyases but lacks an efficient flipping mechanism for interaction with cyclobutane pyrimidine dimer lesions within duplex DNA
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
the substrate is a modified thymidine 10-mer with a central T = T and all other bases, except the one at the 3' end, replaced by 5,6-dihydrothymine (5S:5R stereoisomer ratio 90:10)
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
DNA repair enzyme can absorb blue/ultraviolet A light as energy and split a pyrimidine dimer induced by ultraviolet radiation. PHR1 gene encodes a functional photolyase. The PHR1 transcripts are specifically enhanced by near-ultraviolet radiation (300-400 nm) and by sunlight
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
UV inactivated Haemophilus influenzae DNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light with wavelengths around 400 nm is utilized for DNA repair by PHR
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
the unique configuration of the phosphodiester backbone in the strand containing the pyrimidine dimer, as well as the cyclobutane ring of the dimer itself are the important structural determinants of the substrate for recognition by photolyase
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
binds to DNA containing pyrimidine dimers in a light-independent step and repairs the pyrimidine dimer upon absorbing a photon in the 300-600 nm range
-
-
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
no activity towards (6-4)pyrimidine-cytosine products in DNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
inactive on dimers in RNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
active on cis-syn-cyclobutylpyrimidine dimers in supercoiled DNA as in linear DNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to ultraviolet irradiation, 220-320 nm
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
catalyzes the repair of cyclobutadipyrimidine dimers in DNA under near-UV or blue light irradiation
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
Frog
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
the enzyme is one of the main factors determining UVB sensitivity in Oryza sativa. Cultivar Sasanishiki is resistant to the damaging effects of UVB while cultivar Norin 1 is less resistant. Amino acid position 126 is Arg in cultivar Norin 1 and Gln in cultivar Sasanishiki. The single amino acid alteration from Gln to Arg leads to a deficit of CPD photolyase activity
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
the enzyme preferentially repairs the non-transcribed strands of the URA3 and HIS3 genes in minichromosomes, repair of the non-transcribed strand is more quickly in the active gene than in the repressed gene indicating that transcription dependent disruption of chromatin facilitates repair of an active gene
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
UV inactivated Haemophilus influenzae DNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to ultraviolet irradiation, 220-320 nm
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to ultraviolet irradiation, 220-320 nm
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to ultraviolet irradiation, 220-320 nm
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
catalyzes photorepair of thymine dimers on UV damaged DNA
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
DNA photolyase recognizes ultraviolet-damaged DNA and breaks improperly formed covalent bonds within the cyclobutane pyrimidine dimer by a light-activated electron transfer reaction between FAD and cyclobutane pyrimidine dimer
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
NMR study of repair mechanism of DNA photolyase by FAD-induced paramagnetic relaxation enhancement
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in RNA
2 pyrimidine residues in RNA
-
-
-
-
?
cyclobutadipyrimidine in RNA
2 pyrimidine residues in RNA
-
-
-
-
?
cyclobutadipyrimidine in RNA
2 pyrimidine residues in RNA
-
-
-
-
?
cyclobutadipyrimidine in salmon sperm DNA
2 pyrimidine residues in salmon sperm DNA
-
optimal activity at 400 nm wavelength, no activity at 300 nm, 500 nm and in the dark
-
?
cyclobutadipyrimidine in salmon sperm DNA
2 pyrimidine residues in salmon sperm DNA
-
high activity
-
?
cyclobutadipyrimidine in yeast urea3 gene
2 pyrimidine residues in yeast urea3 gene
-
fast repair of the non-transcribed strand and slow repair of the transcribed strand
-
?
cyclobutadipyrimidine in yeast urea3 gene
2 pyrimidine residues in yeast urea3 gene
-
fast repair of the non-transcribed strand and slow repair of the transcribed strand
-
?
thymine dimers in AnCPDI and Atcry3 complexes
?
the conserved MmCPDII tryptophans W305 and W421 form the L-shaped walling of the active site that clamps the CPD lesion together with the side chain of the conserved M379. Upon repair the 5'-thymine base is expected to remain in place upon breakage of the C5-C5 and C6-C6 bonds by maintaining the p-stacking interactions with the indole moiety of W305, whereas the 3'-thymine dissociates by ca. 1 A away towards the thioether group of M379
-
-
?
thymine dimers in AnCPDI and Atcry3 complexes
?
-
the conserved MmCPDII tryptophans W305 and W421 form the L-shaped walling of the active site that clamps the CPD lesion together with the side chain of the conserved M379. Upon repair the 5'-thymine base is expected to remain in place upon breakage of the C5-C5 and C6-C6 bonds by maintaining the p-stacking interactions with the indole moiety of W305, whereas the 3'-thymine dissociates by ca. 1 A away towards the thioether group of M379
-
-
?
additional information
?
-
-
environmental stress enzyme
-
-
-
additional information
?
-
environmental stress enzyme
-
-
-
additional information
?
-
light-dependent repair of UV-induced damage products in DNA by direct reversal of base damage rather than via excision repair pathways
-
?
additional information
?
-
-
pre-inoculation UV-C (254 nm) treatment of normally susceptible Arabidopsis thaliana accessions induces prolonged, dose-dependent resistance to virulent isolates of the phytopathogenic oomycete Hyaloperonospora parasitica with cyclobutane pyrimidine dimers and (6-4) photoproducts playing a key role in this response
-
-
-
additional information
?
-
-
CPD-photolyase is a DNA repair protein, the electron-transport chain of Cry1 involves a Tyr residue as initial electron donor. For Cry3, weak but unspecific DNA binding, for Cry1, DNA binding cannot be detected. Cry2, whose surface largely resembles that of Cry1, does bind to DNA. Cry3 does repair cyclobutane-pyrimidine-dimers when the lesion is located in a preflipped out state such as in bulges of dsDNA. DASH cryptochromes are single-strand-specific CPD-photolyases
-
-
-
additional information
?
-
-
CryA can repair DNA upon exposure to UVA light similar to other photolyase proteins, CryA represses sexual development under UVA350-370 nm light and exhibits a regulatory function during light-dependent development and DNA repair activity, in the wild type strain mechanisms such as excision repair mask the DNA photolyase activity of CryA
-
-
-
additional information
?
-
the enzyme has blue light photoreceptor activity and CPD photolyase activity. Signaling might be mediated by the PHR besides its effects on the C-terminal extension, conformational changes in cryptochromes upon illumination, overview
-
-
-
additional information
?
-
conformational changes in the PHR, infrared spectral analysis and isotope labeling, overview
-
-
-
additional information
?
-
-
CPD-photolyase binds 8-hydroxy-7,8-didemethyl-5-deazariboflavin which is an antenna chromophore present in various photolyases
-
-
-
additional information
?
-
-
PHR1 and PHR2 are able to bind the CLOCK protein, a transcription activator controlling the molecular circadian clock. But only for PHR2, the physical interaction with CLOCK represses CLOCK/BMAL1-driven transcription, binding of photolyase per se is not sufficient to inhibit the CLOCK/BMAL1 heterodimer
-
-
-
additional information
?
-
CpPL is fully competent to bind and base flip CPDs, and to repair them when exposed to blue light. rCpPL recognizes and flips out a CPD into its active site, base flipping of the CPD by photolyase is accompanied by a large distortion of the local structure of the DNA duplex around the lesion, including the loss of DNA base stacking. 2-Ap base-flipping assay, overview. Thermodynamically, the apparent lack of rigidity of the chains forming the active site would impart a high degree of conformational entropy to the active site of CpPL
-
-
-
additional information
?
-
CpPL is fully competent to bind and base flip CPDs, and to repair them when exposed to blue light. rCpPL recognizes and flips out a CPD into its active site, base flipping of the CPD by photolyase is accompanied by a large distortion of the local structure of the DNA duplex around the lesion, including the loss of DNA base stacking. 2-Ap base-flipping assay, overview. Thermodynamically, the apparent lack of rigidity of the chains forming the active site would impart a high degree of conformational entropy to the active site of CpPL
-
-
-
additional information
?
-
-
CPD photolyase, which rapidly repairs CPDs, is essential for plant survival under sunlight containing UVB
-
-
-
additional information
?
-
comparison of repair activity of the photolyase in the wild-type strain PGEX-4T-1-DsPHR2 and the mutant strain PGEX-4T-1-DsPHR2-Q336H in vitro and in vitro and under different salt concentrations, overview. The mutant shows reduced repair activity compared to wild-type, and the survival rate declines rapidly as salinity increased in the mutant Q336H, while in the wild-type strain, there is no change in the survival rate
-
-
-
additional information
?
-
-
major pathway to remove UV-induced DNA lesions from the genome
-
?
additional information
?
-
-
photoreduction by intraprotein electron transfer is not part of the photolyase photocycle under physiological conditions
-
-
-
additional information
?
-
-
4-amino-6-methyl-8-(2'-deoxy-beta-D-ribofuranosyl)-7(8H)-pteridone (6MAP) is a fluorescent adenine analogue that demonstrates high sensitivity to base-stacking interactions in duplex DNA. 6MAP is a sensitive probe of cyclobutylpyrimidine dimers base flipping by photolyase and does does not interfere with the repair of the substrate. It is shown that 6MAP/cyclobutylpyrimidine dimers duplexes are true substrates of photolyase
-
-
-
additional information
?
-
-
absolute dependence of catalysis by photolyase on light
-
-
-
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
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-
-
additional information
?
-
-
DNA repair protein
-
-
-
additional information
?
-
-
electrostatic interactions and protonation are affected by the oxidation state of the required FAD cofactor and substrate conformation
-
-
-
additional information
?
-
-
the enzyme shows light-induced reduction of FAD, and photorepair involves the transfer of an electron from the photoexcited reduced FAD to the damaged DNA for cleaving the dimers to maintain the DNA's integrity, substrate specificity, overview
-
-
-
additional information
?
-
-
anaerobic repair assay in argon atmosphere
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-
-
additional information
?
-
-
detailed repair dynamics of damaged DNA by photolyases and a biomimetic system through resolving all elementary steps on the ultrafast timescales, including multiple intermolecular electron- and proton-transfer reactions and bond-breaking and -making processes
-
-
-
additional information
?
-
direct measurements of photolyase binding to cyclobutane pyrimidine dimers (CPD)-containing undecamer DNA that has been labeled with a fluorophore, photolyase csCPD-DNA binding kinetics detected by fluorescence spectroscopy, overview. Preparation and purification of csCPD-containing oligonucleotides. Photolyase finds its target through a three-dimensional diffusion-controlled search. Photolyase may not recognize an intrahelical CPD but only an extrahelical CPD
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-
-
additional information
?
-
-
enzyme in complex with CPD moiety, molecular docking study
-
-
-
additional information
?
-
-
photochemistry of wild-type and N378D mutant DNA photolyase with oxidized FAD cofactor studied by transient absorption spectroscopy, overview
-
-
-
additional information
?
-
-
enzyme promotes virus survival in the environment
-
?
additional information
?
-
enzyme promotes virus survival in the environment
-
?
additional information
?
-
-
Cry2 protein binds to ssDNA with high affinity
-
-
-
additional information
?
-
-
the class II enzyme lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA, in contrast to class I enzymes. The lesion-binding mode differs from other photolyases by a larger DNA binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 3'-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophan dyad as electron transfer pathway to the catalytic FAD cofactor
-
-
-
additional information
?
-
the class II enzyme lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA, in contrast to class I enzymes. The lesion-binding mode differs from other photolyases by a larger DNA binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 3'-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophan dyad as electron transfer pathway to the catalytic FAD cofactor
-
-
-
additional information
?
-
-
enzyme-substrate complex structure of class II PL from Methanosarcina mazei (MmPL)
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-
-
additional information
?
-
enzyme-substrate complex structure of class II PL from Methanosarcina mazei (MmPL)
-
-
-
additional information
?
-
-
the class II enzyme lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA, in contrast to class I enzymes. The lesion-binding mode differs from other photolyases by a larger DNA binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 3'-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophan dyad as electron transfer pathway to the catalytic FAD cofactor
-
-
-
additional information
?
-
-
PhrB does not function as a photolyase
-
-
-
additional information
?
-
PhrB does not function as a photolyase
-
-
-
additional information
?
-
PhrB does not function as a photolyase
-
-
-
additional information
?
-
the native rice CPD photolyase is phosphorylated, whereas the Escherichia coli-expressed rice CPD photolyase is not
-
-
-
additional information
?
-
-
expression in transgenic mice leads to superior survival, reduced acute UV effects like erythema, hyperplasia or apoptosis when treated with photoreactivating light
-
?
additional information
?
-
-
CPDs and 6-4PPs play different roles in UV-induced cell death in normal and NER-deficient human cells
-
-
-
additional information
?
-
the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry
-
-
-
additional information
?
-
the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry
-
-
-
additional information
?
-
-
photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
?
-
-
predominant role of photolyase is CDP repair of an origin or replication
-
?
additional information
?
-
-
photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
?
-
-
absolute dependence of catalysis by photolyase on light
-
-
-
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
-
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
-
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)
-
-
-
additional information
?
-
-
DNA repair protein
-
-
-
additional information
?
-
-
with photolyase (PL), proteinase K (PK) generates two large daughter proteins (PL-PK1 and PL-PK2), and lower molecular products (PL-PK3 and PL-PK4). PL-PK3 and PL-PK4 may derive from secondary proteolysis of PL-PK1 and PL-PK2, respectively. In photolyase, proteinase K is active at both proteolysis sites. Cleavage to yield PL-chymotrypsin, and PL-PK1 occurs at a common site in photolyase, specifically within the N-terminal, alpha/beta-domain at the W98-N99 and E94-A95 peptide bonds, respectively. PL-PK2 is generated by a cleavage between residues 402 and 404
-
-
-
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
-
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
-
additional information
?
-
-
enzyme in complex with CPD moiety, molecular docking study
-
-
-
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
-
additional information
?
-
CmPHR2 and CmPHR5 specifically repair ssDNA, while the other CRY-DASH (CmPHR6) repairs neither (6-4) photoproduct nor CPD damage in ssDNA or dsDNA. Comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
-
additional information
?
-
CmPHR2 and CmPHR5 specifically repair ssDNA, while the other CRY-DASH (CmPHR6) repairs neither (6-4) photoproduct nor CPD damage in ssDNA or dsDNA. Comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
-
additional information
?
-
comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
-
additional information
?
-
comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
-
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
-
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
-
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
CmPHR2 and CmPHR5 specifically repair ssDNA, while the other CRY-DASH (CmPHR6) repairs neither (6-4) photoproduct nor CPD damage in ssDNA or dsDNA. Comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
-
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
CmPHR2 and CmPHR5 specifically repair ssDNA, while the other CRY-DASH (CmPHR6) repairs neither (6-4) photoproduct nor CPD damage in ssDNA or dsDNA. Comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
-
additional information
?
-
Vibrio parahaemolyticus serotype 03:KG
usage of salmon sperm DNA with introduced CPDs (UVC-irradiation) as assay substrate
-
-
-
additional information
?
-
Vibrio parahaemolyticus serotype 03:KG RIMD 2210633
usage of salmon sperm DNA with introduced CPDs (UVC-irradiation) as assay substrate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
cyclobutadipyrimidine in DNA
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
additional information
?
-
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
photolyases utilize near-ultraviolet blue light to specifically repair the major photoproducts of UV-induced damaged DNA. The enzyme specifically repairs CPD lesions
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme is involved in biological photoreactivation
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme is involved in biological photoreactivation
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio parahaemolyticus serotype 03:KG
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio parahaemolyticus serotype 03:KG RIMD 2210633
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Xiphophorus maculatus Jp 163 B
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
DNA repair activity
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme binds to DNA containing pyrimidine dimers with high affinity and then breaks the cyclobutane ring joining the two pyrimidines of the dimer in a light-dependent reaction, 300-500 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
-
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
-
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
DNA repair enzyme can absorb blue/ultraviolet A light as energy and split a pyrimidine dimer induced by ultraviolet radiation. PHR1 gene encodes a functional photolyase. The PHR1 transcripts are specifically enhanced by near-ultraviolet radiation (300-400 nm) and by sunlight
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
the enzyme is one of the main factors determining UVB sensitivity in Oryza sativa. Cultivar Sasanishiki is resistant to the damaging effects of UVB while cultivar Norin 1 is less resistant. Amino acid position 126 is Arg in cultivar Norin 1 and Gln in cultivar Sasanishiki. The single amino acid alteration from Gln to Arg leads to a deficit of CPD photolyase activity
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-
?
additional information
?
-
-
environmental stress enzyme
-
-
-
additional information
?
-
environmental stress enzyme
-
-
-
additional information
?
-
light-dependent repair of UV-induced damage products in DNA by direct reversal of base damage rather than via excision repair pathways
-
?
additional information
?
-
-
pre-inoculation UV-C (254 nm) treatment of normally susceptible Arabidopsis thaliana accessions induces prolonged, dose-dependent resistance to virulent isolates of the phytopathogenic oomycete Hyaloperonospora parasitica with cyclobutane pyrimidine dimers and (6-4) photoproducts playing a key role in this response
-
-
-
additional information
?
-
-
CryA can repair DNA upon exposure to UVA light similar to other photolyase proteins, CryA represses sexual development under UVA350-370 nm light and exhibits a regulatory function during light-dependent development and DNA repair activity, in the wild type strain mechanisms such as excision repair mask the DNA photolyase activity of CryA
-
-
-
additional information
?
-
the enzyme has blue light photoreceptor activity and CPD photolyase activity. Signaling might be mediated by the PHR besides its effects on the C-terminal extension, conformational changes in cryptochromes upon illumination, overview
-
-
-
additional information
?
-
-
PHR1 and PHR2 are able to bind the CLOCK protein, a transcription activator controlling the molecular circadian clock. But only for PHR2, the physical interaction with CLOCK represses CLOCK/BMAL1-driven transcription, binding of photolyase per se is not sufficient to inhibit the CLOCK/BMAL1 heterodimer
-
-
-
additional information
?
-
-
CPD photolyase, which rapidly repairs CPDs, is essential for plant survival under sunlight containing UVB
-
-
-
additional information
?
-
-
major pathway to remove UV-induced DNA lesions from the genome
-
?
additional information
?
-
-
photoreduction by intraprotein electron transfer is not part of the photolyase photocycle under physiological conditions
-
-
-
additional information
?
-
-
absolute dependence of catalysis by photolyase on light
-
-
-
additional information
?
-
-
enzyme promotes virus survival in the environment
-
?
additional information
?
-
enzyme promotes virus survival in the environment
-
?
additional information
?
-
-
PhrB does not function as a photolyase
-
-
-
additional information
?
-
PhrB does not function as a photolyase
-
-
-
additional information
?
-
PhrB does not function as a photolyase
-
-
-
additional information
?
-
the native rice CPD photolyase is phosphorylated, whereas the Escherichia coli-expressed rice CPD photolyase is not
-
-
-
additional information
?
-
-
expression in transgenic mice leads to superior survival, reduced acute UV effects like erythema, hyperplasia or apoptosis when treated with photoreactivating light
-
?
additional information
?
-
-
CPDs and 6-4PPs play different roles in UV-induced cell death in normal and NER-deficient human cells
-
-
-
additional information
?
-
-
photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
?
-
-
predominant role of photolyase is CDP repair of an origin or replication
-
?
additional information
?
-
-
photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
?
-
-
absolute dependence of catalysis by photolyase on light
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,10-methenyltetrahydrofolate
5,10-methenyltetrahydropterolypolyglutamate
-
-
5,10-methylenetetrahydrofolate
-
antenna pigment in Escherichia coli absorbs blue/near UV light and transfers the excitation energy fast and efficiently to FADH-
7,8-didemethyl-8-hydroxy-5-deazaflavin
7,8-didemethyl-8-hydroxy-5-deazariboflavin
8-hydroxy-5-deazariboflavin
8-hydroxy-7,8-didemethyl-5-deazariboflavin
-
antenna pigment in Anacystis nidulans absorbs blue/near UV light and transfers the excitation energy fast and efficiently to FADH-
8-iodo-8-demethylriboflavin
-
-
8-iodoflavin
-
chromophore binding site of Thermus photolyase is reconstited also with a novel synthetic flavin, 8-iodoflavin
ATP
-
stimulates, utilization of ATP for the photorepair process of the pyrimidine dimer containing DNA, not only an allosteric effector
deazaflavin
-
antenna cofactor
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
acts as a light-harvesting pigment
5,10-methenyltetrahydrofolate
-
5,10-methenyltetrahydrofolate
-
antenna cofactor
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
Cry3
5,10-methenyltetrahydrofolate
-
bound at the interface between N-terminal and C-terminal domain
5,10-methenyltetrahydrofolate
-
bound at the interface between N-terminal and C-terminal domain
5,10-methenyltetrahydrofolate
-
an electron transfer pathway exists in DASH cryptochrome, where the 5,10-methenyltetrahydrofolate cofactor is photoreduced to 5,10-methylenetetrahydrofolate. Reduction requires the intact tryptophan triad. DASH cryptochrome forms 5,10-methylenetetrahydrofolate when treated with UV-A. Light-driven formation of 5,10-methylenetetrahydrofolate by DASH cryptochrome can be coupled with the formation of NADPH in the presence of 5,10-methylenetetrahydrofolate dehydrogenase
5,10-methenyltetrahydrofolate
-
an electron transfer pathway exists in photolyase, where the 5,10-methenyltetrahydrofolate cofactor is photoreduced to 5,10-methylenetetrahydrofolate. Reduction requires the intact tryptophan triad. Photolyase forms 5,10-methylenetetrahydrofolate when treated with UV-A. Light-driven formation of 5,10-methylenetetrahydrofolate by photolyase can be coupled with the formation of NADPH in the presence of 5,10-methylenetetrahydrofolate dehydrogenase
5,10-methenyltetrahydrofolate
FAD and 5,10-methenyltetrahydrofolate act as chromophore and antenna molecules, respectively
5,10-methenyltetrahydrofolate
-
5,10-methenyltetrahydrofolate
-
observed in the cleft between the two domains, where it interacts with two critical amino acid residues, Cys292 and Lys293
5,10-methenyltetrahydrofolate
;
5-deazaflavin
-
prosthetic group
7,8-didemethyl-8-hydroxy-5-deazaflavin
-
part of the chromophore
7,8-didemethyl-8-hydroxy-5-deazaflavin
-
essential chromogenic part of the cofactor
7,8-didemethyl-8-hydroxy-5-deazariboflavin
-
chromophore binding site of Thermus photolyase is reconstited also with 7,8-didemethyl-8-hydroxy-5-deazariboflavin (8-HDF). However, in the genome sequence of Thermus thermophilus it is found that the genes essential for the biosynthesis of 8-HDF are missing
7,8-didemethyl-8-hydroxy-5-deazariboflavin
-
-
8-hydroxy-5-deazaflavin
-
cofactor
8-hydroxy-5-deazaflavin
-
light-harvesting chromophore, not essential for correct folding of the enzyme
8-hydroxy-5-deazaflavin
-
contains the chromophore 8-hydroxy-5-deazaflavin
8-hydroxy-5-deazariboflavin
-
bound at the interface between N-terminal and C-terminal domain
8-hydroxy-5-deazariboflavin
-
bound at the interface between N-terminal and C-terminal domain
8-hydroxy-5-deazariboflavin
-
photolyase can bind next to the natural cofactor 8-hydroxy-5-deazariboflavin also FMN
FAD
-
flavoprotein
FAD
-
only FAD as cofactor, no second cofactor detectable
FAD
-
enzyme contains two chromophore cofactors: FAD is a catalytic cofactor which directly contributes to the repair of a pyrimidine-dimer, the other is an unidentified light harvesting cofactor, which absorbs visible light and transfers energy to the catalytic cofactor
FAD
-
is indispensable for catalytic activity
FAD
-
the photolyase in its native state contains FAD in the two-electron reduced and deprotonated FADH- form, during purification under aerobic conditions, FADH- is oxidized to the rather stable blue neutral radical
FAD
-
the photolyase in its native state contains FAD in the two-electron reduced and deprotonated FADH- form, during purification under aerobic conditions, FADH- is oxidized to the rather stable blue neutral radical
FAD
-
the purified enzyme binds a FAD, which is in the neutral radical semiquinone form
FAD
-
the repair reaction involves electron transfer to the cyclobutane pyrimidine dimers from the photoexcited FAD cofactor in its fully reduced form
FAD
-
the photoexcited FAD cofactor is reduced from the semiquinone or fully oxidized state to the catalytically active FADH- state
FAD
-
large kinetic isotope and pH effects on the rate constants for FAD semiquinone oxidation, which reveal that proton transfer is rate-limiting. Photolyase-specific residues, Trp392 and Gly389, independently ensure a high kinetic barrier to semiquinone reactivity in photolyase, possibly through interactions with the adenine moiety of FAD and/or adjusting the polarity of the binding site. These residues have a much greater impact on semiquinone reactivity than the more FAD proximal Met353 or Ser395
FAD
-
Cry1, which does not bind to DNA, possesses a strongly reduced surface charge around the FAD binding pocket
FAD
-
alpha-helical domain is harboring the FAD cofactor, essential for catalysis
FAD
-
a second FAD molecule is present in the antenna pigment binding pocket
FAD
-
alpha-helical domain is harboring the FAD cofactor, essential for catalysis
FAD
-
binds the flavin cofactor in a pocket that is conserved in terms of its electronic properties
FAD
-
binds the flavin cofactor in a pocket that is conserved in terms of its electronic properties. W399-W378-W406 may function as potential electron donors to the flavin and are possible candidate tryptophans for light-induced electron transfer
FAD
-
critical W382 residue relative to the flavin for efficient vectorial electron transfer leading to photoreduction
FAD
-
photoreduction of FAD under blue light irradiation is faster in photolyase than in Arabidopsis cry3
FAD
-
photoreduction of FAD under blue light irradiation is faster in photolyase than in Arabidopsis cry3
FAD
-
; photolyase's essential cofactor is a non-covalently bound flavin adenine dinucleotide in fully reduced state (FADH-)
FAD
-
photolyase's essential cofactor is a non-covalently bound flavin adenine dinucleotide in fully reduced state (FADH-)
FAD
-
the physiological form of the enzyme contains a fully reduced FAD (FADH-) that is required for its activity both in vivo and in vitro. It binds a cyclobutane pyrimidine dimer (CPD) in DNA independent of light and flips the dimer out of the double helix into the active site cavity to make a stable enzyme-substrate complex. Enzyme usually purified with FAD in the blue neutral radical form. The purified enzyme can hold its radical flavin cofactor unoxidized in aerobic conditions for several days
FAD
-
light-induced reduction of FAD, and transfer of an electron from the photoexcited reduced FAD to the damaged DNA for cleaving the dimers
FAD
-
the enzyme appears to utilize an unusual, conserved tryptophan dyad as electron transfer pathway to the catalytic FAD cofactor; the enzyme is capable to photoreduce its catalytic FAD to the active FADH- form. The C-terminal FAD-binding subdomain contains the catalytic cofactor FAD in the U-shaped conformation. FAD-binding site and electron transfer pathway in class II photolyases, overview
FAD
the C-terminal domain frames a concave pocket that holds the FAD cofactor in the U-shaped conformation. The U-shaped FAD is positioned with the isoalloxazine ring buried and the adenine ring solvent-exposed beneath the substrate binding pocket. A salt bridge (Arg396 to Asp427) across the isoalloxazine ring orients the guanidinium to stabilize a semiquinone radical at the C4a position. Cofactor binding and interactions with the enzyme, overview
FAD
-
the FAD binding region is required for the catalytic activity of DNA photolyase
FAD
FAD and 5,10-methenyltetrahydrofolate act as chromophore and antenna molecules, respectively. The Ver3 chromophore always remains partly (including the semiquinone state) or fully reduced under all experimental conditions tested
FAD
-
absorption spectra of FADH+, FADH radical, and FADH- of wild-type and mutant enzymes, overview. All three flavin species and decays to zero upon completion of repair
FAD
-
catalytic cofactor, 4 different redox states of flavin, overview
FAD
-
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state; dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state
FAD
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state
FAD
-
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state. Using femtosecond (fs)-resolved spectroscopy and site-directed mutagenesis, the dynamics of class I PL from Escherichia coli (EcPL) in four redox states are investigated
FAD
-
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state
FAD
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state
FAD
-
four redox states of FAD are relevant for the various functions of DNA photolyases: fully reduced FADH- required for DNA photorepair, and the two semireduced radical states FAD- radical and FADH radical formed in electron transfer reactions. Absorption spectra of wild-type EcPL and MTHF antenna-free mutant E109A/N378D EcPL, transient absorption kinetics on nano- and microsecond time scales at six characteristic wavelengths, spectral analysis of transient absorption kinetics, overview
FAD
involved in catalysis, cold-adapted DNA photolyase binds a catalytic flavin adenine dinucleotide (FAD) cofactor noncovalently. UV/Vis and fluorescence spectroscopy reveal that the FAD-binding site in this psychrophilic protein is unique compared to meso/thermophilic PLs. FAD-binding pocket of the CpPL model, overview
FAD
enzyme SsPL is an unusual photolyase in that it contains two FAD cofactors. One FAD cofactor is part of the active site of the protein and required for both DNA binding and repair. The second cofactor, the putative accessory chromophore, may play a role as a light-harvesting pigment, it is always present in the fully oxidized FAD state. The active site cycles between FADH-, the fully reduced form required for activity, and FADH radical, the one-electron oxidized or semiquinone form, SsPL is isolated with the active site mainly in the FADH· state. The accessory FAD does not appear to readily undergo any reduction-oxidation chemistry, and it is always found in the fully oxidized state
FAD
-
the adenine moiety of FADH- bridges between the electron donating isoalloxazine ring and CPD via two hydrogen bonds, suggesting the presence of electron transfer pathways via adenine
FAD
Vibrio parahaemolyticus serotype 03:KG
-
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
FAD
-
bound in a C-terminal alpha-helix cavity, the C-terminal alpha-helical domain consists of 14 alpha-helices. FAD is held in a U-shaped conformation by interaction with 14 conserved amino acid residues
FAD
-
steady-state spectra of flavin at various redox states and active-site solvation dynamics in photolyases, overview
FAD
-
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions; the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FAD
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FAD
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FAD
-
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FAD
-
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FADH2
-
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
FADH2
-
purified enzyme contains FAD
FADH2
-
enzyme contains FAD
FADH2
-
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
FADH2
-
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity; FADH2 cofactor
FADH2
-
enzyme contains FAD
FADH2
-
catalytic cofactor
FADH2
-
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
FADH2
-
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
FADH2
-
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
FADH2
-
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
FADH2
-
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
FADH2
-
the catalytic activity of the enzyme requires fully reduced FAD
FADH2
-
contains the chromophore FADH2
FADH2
-
contains the chromophore FADH2
FADH2
-
uses the anionic state of flavin, FADH-,as cofactor
FADH2
-
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
FADH2
-
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
FADH2
-
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
flavin
-
prosthetic group
flavin
-
enzyme contains a stable flavin radical, the one-electron reduction potential of the excited quartet state of the flavin radical must be at least 1.23 V more positive than the ground state
flavin
-
flavin-mononucleotide (FMN), crystal strucutre analysis reveals the binding of flavin mononucleotide as an antenna chromophore
flavin
-
requires fully reduced flavin for photorepair of DNA, full oxidation to FAD is not necessary for biological function, the reaction mechanism involves electron transfer to the substrate from the excited state of the flavin in its fully reduced state FADH- with subsequent electron return within a nanosecond
flavin
-
requires fully reduced flavin for photorepair of DNA, full oxidation to FAD is not necessary for biological function, the reaction mechanism involves electron transfer to the substrate from the excited state of the flavin in its fully reduced state FADH- with subsequent electron return within a nanosecond
FMN
-
increases the light absorption efficiency of the enzyme, direct electron transfer between FMN and the enzyme is not likely to occur. FMN acts as a highly efficient light harvester that gathers light and transfers the energy to FAD
FMN
-
photolyase can bind next to the natural cofactor 8-hydroxy-5-deazariboflavin also FMN
folate
-
enzyme contains folate
methenyltetrahydrofolate
-
the enzyme utilizes the the antenna cofactor to harvest light energy for the repair of thymine dimers in DNA. For this purpose, the enzyme evolved to bind the cofactor and red-shift its absorption maximum by 25 nm
methenyltetrahydrofolate
-
-
methenyltetrahydrofolate
-
contains the chromophore methenyltetrahydrofolate
methenyltetrahydrofolate
-
-
methenyltetrahydrofolate
-
is the solar panel or photoantenna of the enzyme
methenyltetrahydrofolate
MTHF, the molecule is bound as an antenna molecule and found in substoichiometric amounts
pterin
-
cofactor
pterin
-
contains not only reduced FAD but also a reduced pterin, or a cofactor with similar properties, as a chromophore
additional information
-
light-driven blue light flavophotoreceptors all operate from the excited state, whether singlet oxidized (e.g., BLUF and LOV domains) or doublet semiquinone
-
additional information
recombinant CpPL (rCpPL) binds two different second cofactor molecules, flavin mononucleotide (FMN) when overexpressed and purified from Escherichia coli BL21(DE3) inclusion bodies, and a folate (possibly MTHF) when overexpressed and purified from Escherichia coli Arctic Express (DE3) cells as a His6-tagged protein or in strain BL21-DE3 cells as a maltose-binding-protein fusion protein. CpPL might be somewhat promiscuous in antenna cofactor binding
-
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
-
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4.1.99.3 deoxyribodipyrimidine photo-lyase
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