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Enzyme Nomenclature
Information on EC 4.1.99.3 - deoxyribodipyrimidine photo-lyase
for references in articles please use BRENDA:EC4.1.99.3
Word Map on EC 4.1.99.3
- 4.1.99.3
-
single-stranded
-
helicase
-
photoreactivation
- flavin
- bacteriophage
- photoreceptors
- fork
-
photoproducts
-
polymerases
-
priming
-
circadian
-
uv-induced
-
clock
-
light-dependent
-
blue-light
-
duplex
-
photorepair
-
oligoribonucleotides
-
unwind
-
okazaki
-
dna-dependent
- replisome
-
primosome
- ssdna
-
polydt
-
photoreduction
-
phytochrome
-
uv-damaged
- aphidicolin
-
photomorphogenesis
-
lagging-strand
- anacystis
-
light-driven
-
pyrimidone
-
leading-strand
- rntp
- 5,10-methenyltetrahydrofolate
-
photocycle
-
photomorphogenic
-
primer-template
-
translesion
- fadh2
-
ultraviolet-b
-
polymerase-alpha
-
photoreversal
-
photolesions
-
loader
-
cis-syn
- analysis
-
magnetoreception
- medicine
- biotechnology
-
template-primer
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
4.1.99.3
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RECOMMENDED NAME
GeneOntology No.
deoxyribodipyrimidine photo-lyase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
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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
-
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
-
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
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)
reaction mechanism, detailed overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-C-bond cleavage
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SYSTEMATIC NAME
IUBMB Comments
deoxyribocyclobutadipyrimidine pyrimidine-lyase
A flavoprotein (FAD), containing a second chromophore group. The enzyme catalyses the reactivation by light of irradiated DNA. A similar reactivation of irradiated RNA is probably due to a separate enzyme.
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CAS REGISTRY NUMBER
COMMENTARY
37290-70-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene CL42_09140; UV-resistant strain isolated from high-altitude Andean lakes in Argentinean Puna, gene CL42_09140
UniProt
gene CL42_09140; UV-resistant strain isolated from high-altitude Andean lakes in Argentinean Puna, gene CL42_09140
UniProt
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
possesses two phr genes named Cc-phr1 and Cc-phr2, which share 45% identity at the amino acid level. Cc-phr1 shows no activity
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33474, 33476, 33477, 33478, 33479, 33480, 33482, 33483, 33486, 33489, 33491, 33492, 33498, 33500, 33502, 33506, 33507, 33510, 33511, 650966, 652308, 653629, 663615, 664023, 664598, 665299, 677709, 678141, 678403, 681594, 681765, 682575, 690995, 692023, 692754, 692770, 692778, 693173, 693836, 694570, 694876, 702373, 703398, 704520, 705335, 705348, 705621, 706557, 713768, 714792, 715995, 727010, 728187, 728664
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amino acid position 126 is Arg in cultivar Norin 1 and Gln in cultivar Sasanishiki
SwissProt
subspecies Oryza sativa japonica, strains Sasanishiki, Norin 1, and Surjamkhi
SwissProt
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33478, 33487, 33488, 33489, 33490, 33492, 33496, 33499, 33507, 650966, 653382, 681765, 692024, 705621, 706451
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
phylogenetic analysis, comparison of substrate binding and substrate specificity of class I and class II enzymes, overview. The enzyme shows the overall fold of the photolyase cryptochrome family, surface features of the photolyase-cryptochrome family bound to DNA lesions, overview
evolution
the PHR/CRY family consists of two major classes, class I and class II, the enzyme from rice belongs to class II
evolution
the PhrB sequence is conserved in both pathogenic and commensal Neisseria species but shares little identity to other bacterial species, phylogenetic analysis, overview. The gonococcal PhrB gene is not a functional orthologue of the Escherichia coli PhrB
evolution
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the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1299 strain shows ten amino acid differences, strain W1299 has the alterations: F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L; the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1626 strain shows three amino acid differences, strain W1299 has the alterations: P13S, Q126R and T416P
evolution
the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis strains shows several amino acid differences, strain W1299 has the alterations F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L, and strain W1626 P13S, Q126R and T416P
evolution
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phylogenetic analysis, comparison of substrate binding and substrate specificity of class I and class II enzymes, overview. The enzyme shows the overall fold of the photolyase cryptochrome family, surface features of the photolyase-cryptochrome family bound to DNA lesions, overview
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evolution
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the PhrB sequence is conserved in both pathogenic and commensal Neisseria species but shares little identity to other bacterial species, phylogenetic analysis, overview. The gonococcal PhrB gene is not a functional orthologue of the Escherichia coli PhrB
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evolution
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the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1299 strain shows ten amino acid differences, strain W1299 has the alterations: F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L; the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1626 strain shows three amino acid differences, strain W1299 has the alterations: P13S, Q126R and T416P
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evolution
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the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1299 strain shows ten amino acid differences, strain W1299 has the alterations: F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L; the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1626 strain shows three amino acid differences, strain W1299 has the alterations: P13S, Q126R and T416P
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evolution
Oryza sativa Japonica Group Sasanishiki
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the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis strains shows several amino acid differences, strain W1299 has the alterations F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L, and strain W1626 P13S, Q126R and T416P
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malfunction
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transient expression in an Escherichia coli strain that lacks its endogenous photolyase, rescues growth of the UV-irradiated bacteria in a light-dependent manner, showing that AMV025 encodes a functional DNA photolyase
malfunction
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the CPD photoreactivation rate is undetectable in chloroplasts, mitochondria or nuclei in transgenic rice (AS-D) engineered to express antisense RNA targeting CPD photolyase in wildtype Sasanishiki rice cultivar with low levels of CPD photolyase activity
malfunction
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using transgenic mice expressing Potorous tridactylus CPD-photolyase, it is shown that Potorous CPD-photolyase affects the clock by shortening the period of behavioral rhythms. Constitutively expressed CPD-photolyase is shown to reduce the amplitude of circadian oscillations in cultured cells and to inhibit CLOCK/BMAL1 driven transcription by interacting with CLOCK. Potorous CPD-photolyase can restore the molecular oscillator in the liver of (clock-deficient) Cry1/Cry2 double knockout mice
malfunction
disruption of Saci 1227 produces an Sulfolobus acidocaldarius strain that exhibits negligible photoreactivation
malfunction
loss of phrB does not result in a mutator phenotype. A Neisseria gonorrhoeae phrB mutant has a reduced colony size that is not a result of a growth defect and the mutant cells exhibit an altered morphology. Although the phrB mutant exhibits increased sensitivity to oxidative killing, it shows increased survival on media containing nalidixic acid or rifampicin, but does not have an increased mutation rate with these antibiotics or spectinomycin and kasugamycin. The phrB mutant shows increased negative DNA supercoiling, but while the protein bound double-stranded DNA, it does not express topoisomerase activity. The Neisseria gonorrhoeae phrB cannot complement an Escherichia coli phrB mutant strain CSR603, and the Neisseria gonorrhoeae phrB mutant is not more sensitive to UV irradiation, independent of visible light exposure, phenotype, overview
malfunction
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loss of phrB does not result in a mutator phenotype. A Neisseria gonorrhoeae phrB mutant has a reduced colony size that is not a result of a growth defect and the mutant cells exhibit an altered morphology. Although the phrB mutant exhibits increased sensitivity to oxidative killing, it shows increased survival on media containing nalidixic acid or rifampicin, but does not have an increased mutation rate with these antibiotics or spectinomycin and kasugamycin. The phrB mutant shows increased negative DNA supercoiling, but while the protein bound double-stranded DNA, it does not express topoisomerase activity. The Neisseria gonorrhoeae phrB cannot complement an Escherichia coli phrB mutant strain CSR603, and the Neisseria gonorrhoeae phrB mutant is not more sensitive to UV irradiation, independent of visible light exposure, phenotype, overview
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malfunction
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disruption of Saci 1227 produces an Sulfolobus acidocaldarius strain that exhibits negligible photoreactivation
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metabolism
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photoreduction kinetics of class II photolyases are very similar to those of the other classes with even higher photoreduction rates in class II as compared to class I. W399-W378-W406 electron-transfer pathway is conserved among class II CPD photolyase enzymes
metabolism
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photoreduction kinetics of class II photolyases are very similar to those of the other classes with even higher photoreduction rates in class II as compared to class I. W399-W378-W406 electron-transfer pathway is conserved among class II CPD photolyase enzymes
metabolism
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third electron transfer pathway exists in members of the photolyase family, e.g. DASH cryptochrome, that remained undiscovered so far
metabolism
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third electron transfer pathway exists in members of the photolyase family that remained undiscovered so far
physiological function
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photolyase can repair UV-damaged DNA in a mechanism requiring light and DNA base flipping, whereas cytochromes cannot repair DNA. Evolution of loop sequence likely plays a key role in functional diversification of cryptochromes and photolyases, through tuning of substrate recognition. Cryptochrome-DASH recognition loop peptide folds 2.5fold faster than its counterpart in photolyase, predominantly due to a lower enthalpy of activation. Binding duplex DNA in the catalytically-active base-flipped conformation imposes significant order on the recognition loop, and a corresponding entropic penalty, which may be surmounted by the more preorganized photolyase recognition loop, but may impose too large a barrier for the more dynamic loop in cryptochrome-DASH
physiological function
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PhrB breaks pyrimidine dimers caused by UV exposure, using energy from visible light in the process of photoreactivation. UV-hyper-resistant strain contains a single mutation: a 1 bp deletion in the intergenic region directly upstream of the mutT-phrB operon, encoding nudix hydrolase and photolyase
physiological function
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PHR2 protein plays a role in baculovirus DNA repair
physiological function
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photolyase may function to facilitate DNA repair during UVB exposure. Increased resistance of Photobacterium angustum as compared to Sphingopyxis alaskensis under high UVB doses results from a UVB-induction of CPD photolyase(s) that may directly repair DNA damage and/or act indirectly by enhancing the rate of nucleotide excision repair. Presence of 3 genes coding for DNA photolyase type I enzymes in Photobacterium angustum compared to only 1 for Sphingopyxis alaskensis. Photoresistance strategy may involve a capacity to utilize 3 distinct gene products, including the UVB-induced overexpression of the gene(s). Photolyase activity not only leads to the repair of DNA through a photochemical process, but may also enhance the efficiency of nucleotide excision repair, which is far more efficient in Photobacterium angustum than in Sphingopyxis alaskensis
physiological function
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photolyase may function to facilitate DNA repair during UVB exposure. Increased resistance of Photobacterium angustum as compared to Sphingopyxis alaskensis under high UVB doses results from a UVB-induction of CPD photolyase(s) that may directly repair DNA damage and/or act indirectly by enhancing the rate of nucleotide excision repair. Presence of three genes coding for DNA photolyase type I enzymes in Photobacterium angustum compared to only one for Sphingopyxis alaskensis. Photolyase activity not only leads to the repair of DNA through a photochemical process, but may also enhance the efficiency of nucleotide excision repair, which is far more efficient in Photobacterium angustum than in Sphingopyxis alaskensis
physiological function
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overexpression of CPD photolyase strongly enhances the repair of cyclobutane pyrimidine dimers and results in a moderate increase of biomass production under elevated UV-B
physiological function
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structural similarity between the larger N-terminal domain of primase (PriL) with the active site region of DNA photolyase
physiological function
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the Cc-phr2 gene product can complement an Escherichia coli photolyase deficiency and can repair T-T dimers in vitro, showing that the Cc-PHR2 protein has photolyase activity
physiological function
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
physiological function
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photolyases use visible light to repair ultraviolet-induced DNA damage. PHR2 binds the CLOCK protein and represses CLOCK/BMAL1-driven transcription, it also affects the oscillation of immortalized mouse embryonic fibroblasts, suggesting that PHR2 can regulate the molecular circadian clock
physiological function
the enzyme PhrB has a role in maintaining DNA supercoiling that is important for normal cell physiology
physiological function
M0VZZ1
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
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in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
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in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
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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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physiological function
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the enzyme PhrB has a role in maintaining DNA supercoiling that is important for normal cell physiology
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physiological function
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in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
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physiological function
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in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
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physiological function
Oryza sativa Japonica Group Sasanishiki
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in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
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physiological function
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PhrB breaks pyrimidine dimers caused by UV exposure, using energy from visible light in the process of photoreactivation. UV-hyper-resistant strain contains a single mutation: a 1 bp deletion in the intergenic region directly upstream of the mutT-phrB operon, encoding nudix hydrolase and photolyase
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additional information
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repair mechanism and the substrate specificity that distinguish enzyme CPD-PHR from enzyme (6-4) PHR, EC 4.1.99.13, which uniquely repairs (6-4) photoproducts, using Fourier transform infrared spectroscopy, overview
additional information
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illumination leads to the neutral semiquinoid state of the photolyase with maxima at 590 nm and 632 nm, respectively. Stabilizing role of asparagine N403 in class II photolyases. The innermost tryptophan W381 is crucial for catalytic activity, electron transfer pathway along the tryptophan catalytic triad W388-W360-W381 to FAD
additional information
illumination leads to the neutral semiquinoid state of the photolyase with maxima at 590 nm and 632 nm, respectively. Stabilizing role of asparagine N403 in class II photolyases. The innermost tryptophan W381 is crucial for catalytic activity, electron transfer pathway along the tryptophan catalytic triad W388-W360-W381 to FAD
additional information
structure-activity relationships in class II PHRs, overview. Structural comparisons with prokaryotic class I CPD PHRs identify differences in the binding site for UV-damaged DNA substrate
additional information
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electron-tunneling pathways and functional role of adenine moiety of wild-type and mutant enzymes, overview
additional information
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illumination leads to the neutral semiquinoid state of the photolyase with maxima at 590 nm and 632 nm, respectively. Stabilizing role of asparagine N403 in class II photolyases. The innermost tryptophan W381 is crucial for catalytic activity, electron transfer pathway along the tryptophan catalytic triad W388-W360-W381 to FAD
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 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 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 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)
-
-
-
?
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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-
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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)
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
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
repairs cyclobutylpyrimidine dimers by a light-driven electron transfer
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
two photolyases specific for photoreactivation of either cyclobutane pyrimidine dimers or pyrimidine (6-4)pyrimidones
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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AtCry3 repairs the dimer but only in ssDNA
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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 uses light to repair cyclobutylpryrimidine dimers in DNA, local structure around the thymidine lesion changes dramatically upon binding to photolyase
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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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
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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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
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-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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active genes are faster repaired than silenced genes
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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active genes are faster repaired than silenced genes
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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dimeric and pentameric oligothymidine substrates, repairs cyclobutylpyrimidine dimers via photoinduced electron transfer from a reduced flavin adenine dinucleotide cofactor to the bound cyclobutylpyrimidine dimer
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?
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
-
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
?
-
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
?
-
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
?
-
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
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
-
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
-
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
-
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
-
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
-
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
-
-
-
?
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
-
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
-
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
-
NMR study of repair mechanism of DNA photolyase by FAD-induced paramagnetic relaxation enhancement
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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)
Q8PYK9
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)
Q8PYK9
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)
Q4J9F6
the enzyme is involved in biological photoreactivation
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Q4J9F6
the enzyme is involved in biological photoreactivation
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
Q9XHE2
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
P61497
-
-
?
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
Q6F6A2
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
-
-
?
additional information
?
-
Q9SB00
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
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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
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CPD photolyase, which rapidly repairs CPDs, is essential for plant survival under sunlight containing UVB
-
-
-
additional information
?
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-
major pathway to remove UV-induced DNA lesions from the genome
-
?
additional information
?
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-
photoreduction by intraprotein electron transfer is not part of the photolyase photocycle under physiological conditions
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-
-
additional information
?
-
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absolute dependence of catalysis by photolyase on light
-
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-
additional information
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enzyme promotes virus survival in the environment
-
?
additional information
?
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Q9ICB3
enzyme promotes virus survival in the environment
-
?
additional information
?
-
-
PhrB does not function as a photolyase
-
-
-
additional information
?
-
Q5F659
PhrB does not function as a photolyase
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-
-
additional information
?
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Q5F659
PhrB does not function as a photolyase
-
-
-
additional information
?
-
Q6F6A2
the native rice CPD photolyase is phosphorylated, whereas the Escherichia coli-expressed rice CPD photolyase is not
-
-
-
additional information
?
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expression in transgenic mice leads to superior survival, reduced acute UV effects like erythema, hyperplasia or apoptosis when treated with photoreactivating light
-
?
additional information
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CPDs and 6-4PPs play different roles in UV-induced cell death in normal and NER-deficient human cells
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-
-
additional information
?
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photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
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predominant role of photolyase is CDP repair of an origin or replication
-
?
additional information
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photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
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absolute dependence of catalysis by photolyase on light
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,10-methylenetetrahydrofolate
-
antenna pigment in Escherichia coli absorbs blue/near UV light and transfers the excitation energy fast and efficiently to FADH-
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-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
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
-
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
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
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
-
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
-
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
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
-
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
-
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 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
-
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
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
-
contains the chromophore methenyltetrahydrofolate
pterin
-
contains not only reduced FAD but also a reduced pterin, or a cofactor with similar properties, as a chromophore
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ferricyanide
-
blue light irradiation converts fully oxidized FAD to the semiquinone state, but in the presence of ferricyanide as electron acceptor further photoreduction to the fully reduced catalytically active form FADH- is inhibited
RNA polymerase III
-
transcription by RNAPII and RNAPIII slows down the repair by photolyase on the transcribed strands
-
yeast DNA
-
inhibition due to inferences in the binding of photolyase with UV-irradiated DNA by yeast RNA
-
H2O2
-
addition of H2O2 to the enzyme solution also inactivates CPD photolyase activity
RNA polymerase II
-
transcription by RNAPII and RNAPIII slows down the repair by photolyase on the transcribed strands
-
RNA polymerase II
-
inhibition of photoreactivation by RNAP-II in the transcribed strand, which is in contrast to genes transcribed by RNAP-I
-
additional information
-
CPD but not 6-4PP enzyme activity exhibits a lagperiod in photoreactivation after 3 days dark exposure
-
additional information
-
product inhibition through interaction with either the protease or the parent protein. The former leads to cleavage of the daughter proteins and can account for reduced cleavage of parent photolyase
-
additional information
-
DNA repair protein photolyase as a model protein, because it is the most widely studied enzyme among its family members including photolyases and cryptochromes with a well-known three-dimensional structure, for characterization of interactions of the FAD region of photolyase with available drugs, which significant to determine the possible unknown effects of known drugs on the suppressor activity of human cryptosome on CLOCK. Cryptochromes act as negative transcriptional regulator of CLOCK in mammals. Molecular docking of drugs to the FAD region of Vibrio cholerae DNA photolyase, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,10-methenyltetrahydrofolate
-
binds to the enzyme and acts as a light-harvesting pigment
blue-light regulator 2
-
the blue-light regulator 2 gene is involved in near-ultraviolet radiation-enhanced PHR1 gene expression
-
5,10-methenyltetrahydrofolic acid
-
the enzyme contains 5,10-methenyltetrahydrofolic acid
5,10-methenyltetrahydrofolic acid
-
cofactor
FAD
-
enzyme contains FAD as catalytic cofactor and a second chromophore as a light harvesting antenna
FADH2
-
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
FADH2
-
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH2
-
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
FADH2
-
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
additional information
-
the transcription of the CPD photolyase gene is activated by UVB light (310 nm)
-
additional information
-
an electric field can enhance the electron transfer from the enzyme to its substrate
-
additional information
-
reduction potential is unchanged in the presence of 120× molar excess of Mg-ATP
-
additional information
-
the nucleotide excision repair proteins Rad7 and Rad16 have no obvious impact on cyclobutadipyrimidine dimer repair by photolyase nor does deletion of rad7 and rad16 affect the chromatin structure and accessibility in the promoter region
-
additional information
-
reduction potential is unchanged in the presence of 120× molar excess of Mg-ATP
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
-
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
drug ligand binding follows pseudo-first-order kinetics, equivalent and independent for all binding sites, theoretical docking and dissociation constants, overview
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
AtCry1 shows no photorepair activity under any condition; it is shown by in vitro and in vivo by photoreactivation assays and electrophoretic mobility shift assays that AtCry3, as a member of the Cry-DASH enzymes, is specific for cyclobutane pyrimidine dimers in ssDNA
additional information
-
BsUvrC shows no photorepair activity under any condition
additional information
-
monochromatic UV irradiation at wavelengths above 300 nm increases the level of CsPHR transcripts similarly to irradiation at wavelengths below 320 nm, but reduces CPD photolyase activity compared with the dark control. Exposure of a CPD photolyase solution to UV-C (254 nm) reduces enzyme activity and induces accumulation of H2O2. Addition of H2O2 to the enzyme solution also inactivates CPD photolyase activity; polychromatic UV- irradiation increases activity of CPD photolyase by an amount which depends on UV irradiance, and the level of CsPHR transcripts temporarily increases before the activity reaches a constant level. UV light above 320 nm is more effective than visible light at increasing CPD photolyase activity
additional information
photoreactivation of the Dunaliella salina photolyase is determined by an complementation assay in an Escherichia coli mutant strain SY2 which is deficient in photoreactivation, nucleotide excision repair, and recombination: cells show a significant increase in survival rate when irradiated with UV-C
additional information
-
photoreactivation of the Dunaliella salina photolyase is determined by an complementation assay in an Escherichia coli mutant strain SY2 which is deficient in photoreactivation, nucleotide excision repair, and recombination: cells show a significant increase in survival rate when irradiated with UV-C
additional information
-
medium-pressure UV irradiation results in a greater reduction in photolyase activity than low-pressure UV radiation. It is suggested that oxidation of the flavin adenine dinucleotide in photolyase may cause the decrease in activity
additional information
-
activity of freshly prepared holoenzyme methenyltetrahydrofolate + FADH is considered 100%. After methenyltetrahydrofolate cofactor removal the activity of the enzyme decreases to 70%, reconstituted oxidized photolyase shows the lowest activity with 34%. Activity after dithionite reduction: 83%
additional information
-
transgenic rice plants bearing the CPD photolyase gene of the UV-resistant rice cultivar Sasanishiki in the sense orientation reveal up to 45.7fold higher CPD photolyase activities compared to wildtype are significantly more resistant to UVB-induced growth damage, and maintain significantly lower CPD levels in their leaves during growth under elevated UVB radiation. Rice plants bearing the CPD photolyase gene in the antisense orientation have little photolyase activity, are severely damaged by elevated UVB radiation, and maintain higher CPD levels in its leaves during growth under UVB radiation.
additional information
-
specific activity is shown by an enhanced survival rate of wildtype Rhodobacter sphaeroides (53%) cells compared to deltaphrA cells (3%) after exposure to UV light. A complementation by plasmid-borne phrA restores photoreactivation properties and increases the survival rate of the deletion mutant 14fold
additional information
-
protein shows phoreactive activity determined by UV/Vis-spectroscopy at 265 nm
additional information
-
photoreactivation experiments indicate that the survival rate decreases from 100 to 2.6% when the UV-C flux is increased from 1.1 to 68.5 microWatt/cm2. Photolyase is inactivated at UV-C intensities = 25.5 microWatt/cm2 due to structure changes of the photolyase.
additional information
-
it is shown by in vitro and in vivo by photoreactivation assays and electrophoretic mobility shift assays that VcCry1, as a member of the Cry-DASH enzymes,is specific for cyclobutane pyrimidine dimers in ssDNA; it is shown that VcCry1 repairs photodimers in the deoxyribonucleotide homopolymers poly dU (uracil cyclobutane dimer) and poly dT much more efficiently than the dimers in the ribopolynucleotide homopolymer
additional information
-
phr confers light-dependent resistance to UV light. However, upon comparing ES114 to a phr mutant, consisting of an in-frame deletion of the gene, and a dark deltaluxCDABEG mutant, it is shown that bioluminescence does not affect photolyase-mediated resistance to UV light. Results indicate that in Vibrio fischeri strain ES114, the benefits of bioluminescence during symbiotic colonization are not mediated by photolyase, and no evidence is found that light production supports cells by stimulating photolyase in this strain.
additional information
-
it is shown by in vitro and in vivo by photoreactivation assays and electrophoretic mobility shift assays that XlCry-DASH, as a member of the Cry-DASH enzymes, is specific for cyclobutane pyrimidine dimers in ssDNA
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.6
-
pH 6.0: 45% of maximal activity, pH 8.6: about 35% of maximal activity
6.8 - 8.1
-
pH 6.8: 49% of maximal activity, pH 8.1: about 29% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 37
-
decrease in photoreactivation capacity with increasing temperature
additional information
-
temperature dependence of the binding enthalpy for dsDNA and damaged DNA, overview
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
confluent murine cells have higher specific activity than do rapidly growing cells
highly expressed under conditions of 14-h light and 10-h dark cycle, both in male and in female plants
highly expressed under conditions of 14-h light and 10-h dark cycle, both in male and in female plants
-
the enzyme is concentrated in the phagocytotic monocytes and polymorphonuclear cells
additional information
-
PHR1 and PHR2 colocalize with the CLOCK protein
additional information
-
level of CsPHR transcripts increase immediately after the start of UV-irradiation and gradually decrease after 4 h. After irradiation for 10 h the transcript level is almost the same as the initial level
additional information
real-time PCR analysis indicate that transcription of PHR2 is induced by UV-C, white light, high salinity, and H2O2
additional information
-
real-time PCR analysis indicate that transcription of PHR2 is induced by UV-C, white light, high salinity, and H2O2
additional information
-
lymphocytes, erythrocytes, spleen, and serum contain little if any enzyme activity
additional information
-
expression of phrA is upregulated in response to light. Furthermore, it is shown that singlet oxygen and hydrogen peroxide dependent signals are transmitted by the sigmaE factor and the anti-sigmaE factor ChrR affecting phrA expression, while superoxide anions do not stimulate phrA expression
additional information
-
phr1 mRNA expression is rapidly induced by blue and UVA light; the 2-kb 5’ upstream region of phr1, with putative light-regulated elements, confers blue light regulation on a reporter gene. It is suggested that PHR1 regulate its expression in a light-dependent manner
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
non-fused PHR1-EGFP is distributed homogeneously over the cytoplasm and the nucleus at all time points analysed, as shown for 96 h post-transfection. PHR2-EGFP fusion protein is distributed over the cytoplasm and nucleus but, over time, it becomes localized predominantly in the nucleus
additional information
-
contains a relatively high proportion of the phosphorylated CPD photolyase
-
contains a relatively high proportion of the phosphorylated CPD photolyase
-
-
contains a relatively high proportion of the phosphorylated CPD photolyase
-
-
CPD photolyase functions in chloroplasts. Nuclei and chloroplasts have a relatively high proportion of the phosphorylated protein form
contains a relatively high proportion of the phosphorylated CPD photolyase
Oryza sativa Japonica Group Sasanishiki
-
contains a relatively high proportion of the phosphorylated CPD photolyase
-
-
contains a high proportion of unphosphorylated CPD photolyase
-
contains a high proportion of unphosphorylated CPD photolyase
-
-
contains a high proportion of unphosphorylated CPD photolyase
-
-
CPD photolyase functions in mitochondria. Mitochondria show a high proportion of non-phosphorylated CPD photolyase
contains a high proportion of unphosphorylated CPD photolyase
Oryza sativa Japonica Group Sasanishiki
-
contains a high proportion of unphosphorylated CPD photolyase
-