4.1.99.3: deoxyribodipyrimidine photo-lyase
This is an abbreviated version!
For detailed information about deoxyribodipyrimidine photo-lyase, go to the full flat file.
Word Map on EC 4.1.99.3
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4.1.99.3
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single-stranded
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strand
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dsdna
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helicase
-
aptamer
-
fork
-
duplex
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electrochemical
-
electrode
-
nanoparticles
-
viruses
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bacteriophage
-
unwind
-
gold
-
biosensors
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rpa
-
nuclease
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exonuclease
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selex
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photoproducts
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polymerases
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uv-induced
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rad51
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graphene
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single-molecule
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nucleoprotein
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anneal
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primer-template
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telomeres
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biotechnology
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biosensing
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okazaki
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analysis
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recombinases
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aptasensors
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translesion
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anti-dna
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aptamer-based
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dna-dependent
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dnab
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g-quadruplexes
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overhang
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template-primer
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recbcd
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oligoribonucleotides
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replisome
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nanopore
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apobec3g
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loader
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aunps
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mre11
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blue-light
-
medicine
- 4.1.99.3
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single-stranded
- strand
- dsdna
- helicase
- aptamer
- fork
- duplex
-
electrochemical
-
electrode
- nanoparticles
- viruses
- bacteriophage
-
unwind
- gold
-
biosensors
- rpa
- nuclease
-
exonuclease
-
selex
- photoproducts
- polymerases
-
uv-induced
- rad51
-
graphene
-
single-molecule
- nucleoprotein
-
anneal
-
primer-template
-
telomeres
- biotechnology
-
biosensing
-
okazaki
- analysis
-
recombinases
-
aptasensors
-
translesion
-
anti-dna
-
aptamer-based
-
dna-dependent
- dnab
-
g-quadruplexes
-
overhang
-
template-primer
-
recbcd
- oligoribonucleotides
- replisome
-
nanopore
- apobec3g
-
loader
-
aunps
- mre11
-
blue-light
- medicine
Reaction
Synonyms
AMV025, AnPL, AtCry1, AtCry3, AtPL, BcCRY1, BcCRY2, BCIN_05g08060, BCIN_09g01620, BsUvrC, Cc-phr2, CcPL, CDP photolyase, class I CPD photolyase, class I cyclobutane pyrimidine dimer photolyase, class I photolyase, class I PL, class II AtPL, class II CPD photolyase, class II CPD-DNA photolyase, class II CPD-photolyase, class II cyclobutane pyrimidine dimer photolyase, class II DmPL, class II DNA photolyase, class II photolyase, class II PL, class III PL, cold-adapted DNA photolyase, CPD class I photolyase, CPD photolyase, CPD photolyase photolyase, CPD specific photolyase, CPD-class I photolyase, CPD-photolyase, CPD-Phr, CPD-specific DNA photolyase, CPD1, CPD2PHR, CPDI, CPDII, CPDphr, CPH1, CPH1-PHR, CpPL, Cry-DASH, Cry1, Cry2, cry3, CryA, CRYD, cryptochrome 1, cryptochrome 3, CRYPTOCHROME DASH, cryptochrome-3, cryptochrome-DASH, CsPHR, cyclobutane pyrimidine dimer photolyase, cyclobutane pyrimidine dimer PHR, cyclobutane pyrimidine dimer specific photolyase, cyclobutane pyrimidine dimer-class I photolyase, cyclobutane pyrimidine dimer-specific DNA photolyase, cyclobutane pyrimidine dimers photolyase, CYME_CMA044C, cytochrome DASH, DASH cryptochrome, deoxyribodipyrimidine photolyase, deoxyribodipyrimidine photolyase type I enzyme, deoxyribonucleate pyrimidine dimer lyase (photosensitive), deoxyribonucleic cyclobutane dipyrimidine photolyase, deoxyribonucleic photolyase, dipyrimidine photolyase (photosensitive), DmPL, DNA cyclobutane dipyrimidine photolyase, DNA photolyase, DNA photolyase type I enzyme, DNA repair protein photolyase, DNA-photoreactivating enzyme, EcPL, eukaryotic Class II CPD PHR, eukaryotic class II cyclobutane pyrimidine dimer photolyase, lyase, deoxyribonucleate pyrimidine dimer, MmCPDII, MmPL, MM_0852, photolyase, photolyase I, photolyase orthologue, photoreactivating enzyme, PHR, phr A photolyase, PHR1, PHR2, phrA, PhrB, PhrB orthologue, PhrB photolyase, PL, PRE, primase, Saci_1227, ssDNA, ssDNA AtCRY3, ssDNA photolyase, ssDNA PL, SsPL, St-photolyase, tetur12g04440, tetur12g04460, tetur35g00010, tetur35g00030, thymine dimer by photolyase, VcCry1, VcPHR, Ver3Phr, VPA1471, XlCry-DASH
ECTree
4.1.99.3 deoxyribodipyrimidine photo-lyaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 4.1.99.3 - deoxyribodipyrimidine photo-lyase
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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
-
substrate binding and substrate conformation by isothermal titration calorimetry, overview
-
-
?
cis-syn cyclobutadipyrimidine dimer DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in calf thymus DNA
2 pyrimidine residues in calf thymus DNA
-
optimal activity at 400 nm wavelength, no activity at 300 nm, 500 nm and in the dark
-
?
cyclobutadipyrimidine in minichromosomes
2 pyrimidine residues in minichromosomes
-
removes cyclobutane pyrimidine dimers predominantly from the ARS1 region
-
?
cyclobutadipyrimidine in nucleosome DNA
2 pyrimidine residues in nucleosome DNA
-
folding of DNA in nucleosomes efficiently protects DNA from being repaired
-
?
cyclobutadipyrimidine in oligodeoxythymidylates
pyrimidine residues in oligodeoxythymidylates
-
minimum size is about 9 residues
-
?
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 AtCRY3 is specific for single-stranded DNA substrates
-
-
?
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)
Caulobacter vibrioides NA1000 / CB15N
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Caulobacter vibrioides NA1000/CB15N
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Colwellia psychrerythraea 34H / ATCC BAA-681
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
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
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
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
-
-
?
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)
-
repair of a single CPD lesion within a double-stranded DNA molecule
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
various CPD substrates, T-T, T-U, U-T, U-U dimers
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the entire catalytic cycle is complete in 1.2 ns, and the enzyme repairs thymine dimer with a quantum yield of 0.9
-
-
?
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
-
-
?
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 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 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
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Saccharolobus solfataricus DSM ATCC 35092 / DSM 1617 / JCM 11322 / P2
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Saccharolobus solfataricus DSM ATCC 35092 / DSM 1617 / JCM 11322 / P2
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
-
-
?
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)
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
-
-
?
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)
Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
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
-
-
?
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 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
-
-
?
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)
Xiphophorus maculatus Jp 163 B
-
-
-
-
?
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
-
?
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
-
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
-
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
-
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
-
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
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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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
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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UV inactivated Haemophilus influenzae DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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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
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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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
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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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
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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catalyzes photorepair of thymine dimers on UV damaged DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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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
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
NMR study of repair mechanism of DNA photolyase by FAD-induced paramagnetic relaxation enhancement
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
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cyclobutadipyrimidine in RNA
2 pyrimidine residues in RNA
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cyclobutadipyrimidine in salmon sperm DNA
2 pyrimidine residues in salmon sperm 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 salmon sperm DNA
2 pyrimidine residues in salmon sperm DNA
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high activity
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cyclobutadipyrimidine in yeast urea3 gene
2 pyrimidine residues in yeast urea3 gene
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fast repair of the non-transcribed strand and slow repair of the transcribed strand
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cyclobutadipyrimidine in yeast urea3 gene
2 pyrimidine residues in yeast urea3 gene
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fast repair of the non-transcribed strand and slow repair of the transcribed strand
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thymine dimers in AnCPDI and Atcry3 complexes
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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
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thymine dimers in AnCPDI and Atcry3 complexes
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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
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additional information
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light-dependent repair of UV-induced damage products in DNA by direct reversal of base damage rather than via excision repair pathways
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additional information
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light-dependent repair of UV-induced damage products in DNA by direct reversal of base damage rather than via excision repair pathways
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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conformational changes in the PHR, infrared spectral analysis and isotope labeling, overview
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additional information
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conformational changes in the PHR, infrared spectral analysis and isotope labeling, overview
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additional information
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CPD-photolyase binds 8-hydroxy-7,8-didemethyl-5-deazariboflavin which is an antenna chromophore present in various photolyases
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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
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additional information
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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
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additional information
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Colwellia psychrerythraea 34H / ATCC BAA-681
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
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additional information
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CPD photolyase, which rapidly repairs CPDs, is essential for plant survival under sunlight containing UVB
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additional information
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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
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additional information
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major pathway to remove UV-induced DNA lesions from the genome
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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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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
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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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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
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electrostatic interactions and protonation are affected by the oxidation state of the required FAD cofactor and substrate conformation
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additional information
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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
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additional information
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anaerobic repair assay in argon atmosphere
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additional information
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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
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additional information
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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
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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
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enzyme in complex with CPD moiety, molecular docking study
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additional information
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photochemistry of wild-type and N378D mutant DNA photolyase with oxidized FAD cofactor studied by transient absorption spectroscopy, overview
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additional information
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photochemistry of wild-type and N378D mutant DNA photolyase with oxidized FAD cofactor studied by transient absorption spectroscopy, overview
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additional information
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enzyme promotes virus survival in the environment
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additional information
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enzyme promotes virus survival in the environment
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additional information
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Cry2 protein binds to ssDNA with high affinity
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additional information
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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
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additional information
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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
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additional information
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enzyme-substrate complex structure of class II PL from Methanosarcina mazei (MmPL)
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additional information
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enzyme-substrate complex structure of class II PL from Methanosarcina mazei (MmPL)
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additional information
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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
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additional information
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PhrB does not function as a photolyase
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additional information
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PhrB does not function as a photolyase
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additional information
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PhrB does not function as a photolyase
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additional information
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the native rice CPD photolyase is phosphorylated, whereas the Escherichia coli-expressed rice CPD photolyase is not
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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
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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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the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry
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additional information
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the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry
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additional information
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Saccharolobus solfataricus DSM ATCC 35092 / DSM 1617 / JCM 11322 / P2
the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry
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additional information
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photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
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additional information
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predominant role of photolyase is CDP repair of an origin or replication
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additional information
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photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
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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 in complex with CPD moiety, molecular docking study
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additional information
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Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
enzyme in complex with CPD moiety, molecular docking study
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additional information
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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)
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additional information
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DNA repair protein
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additional information
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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
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additional information
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enzyme in complex with CPD moiety, molecular docking study
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additional information
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Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1
enzyme in complex with CPD moiety, molecular docking study
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additional information
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enzyme in complex with CPD moiety, molecular docking study
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additional information
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
enzyme in complex with CPD moiety, molecular docking study
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additional information
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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
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additional information
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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
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additional information
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comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
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additional information
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comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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usage of salmon sperm DNA with introduced CPDs (UVC-irradiation) as assay substrate
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additional information
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usage of salmon sperm DNA with introduced CPDs (UVC-irradiation) as assay substrate
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