Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
phylogenetic analysis and tree, overview
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 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
-
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
evolution
-
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 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
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members. The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
DNA photolyases (PLs) and evolutionarily related cryptochrome (CRY) blue-light receptors form a widespread superfamily of flavoproteins involved in DNA photorepair and signaling functions. They share a flavin adenine dinucleotide (FAD) cofactor and an electron-transfer (ET) chain composed typically of three tryptophan residues that connect the flavin to the protein surface
evolution
the enzyme BcCRY1 belongs to the cryptochrome/photolyase family (CPF), CPD photolyase subfamily
evolution
the enzyme BcCRY2 belongs to the cryptochrome/photolyase family (CPF), cry-DASH subfamily
evolution
the enzyme belongs to the cryptochrome/photolyase family (CPF)
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. The class of the CPF known as CRY-DASHs is found in algae, bacteria, plants and animals. CRY-DASH proteins have photolyase activity. Because they specifically repair CPD photoproducts in single-stranded DNA (ssDNA) rather than double-stranded DNA (dsDNA), they are designated as ssDNA photolyases
evolution
the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. The class of the CPF known as CRY-DASHs is found in algae, bacteria, plants and animals. CRY-DASH proteins have photolyase activity. Because they specifically repair CPD photoproducts in single-stranded DNA (ssDNA) rather than double-stranded DNA (dsDNA), they are designated as ssDNA photolyases
evolution
the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. UV is responsible for the formation of two major types of damage-associated photoproducts on DNA: cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone (6-4) photoproducts (Pyr [6-4] Pyr). Two different types of photolyases were eventually discovered: CPD and (6-4) photolyases (EC 4.1.99.13). CPD photolyases repair pyrimidine dimers, while (6-4) photolyases repair Pyr[6-4]Pyr photoproducts
evolution
-
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
-
evolution
-
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
-
evolution
-
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 enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
-
evolution
-
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
-
evolution
-
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
-
evolution
-
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
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. The class of the CPF known as CRY-DASHs is found in algae, bacteria, plants and animals. CRY-DASH proteins have photolyase activity. Because they specifically repair CPD photoproducts in single-stranded DNA (ssDNA) rather than double-stranded DNA (dsDNA), they are designated as ssDNA photolyases
-
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 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
-
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
-
the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. The class of the CPF known as CRY-DASHs is found in algae, bacteria, plants and animals. CRY-DASH proteins have photolyase activity. Because they specifically repair CPD photoproducts in single-stranded DNA (ssDNA) rather than double-stranded DNA (dsDNA), they are designated as ssDNA photolyases
-
evolution
-
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
-
evolution
-
the enzyme BcCRY1 belongs to the cryptochrome/photolyase family (CPF), CPD photolyase subfamily
-
evolution
-
the enzyme BcCRY2 belongs to the cryptochrome/photolyase family (CPF), cry-DASH subfamily
-
evolution
-
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
-
evolution
-
phylogenetic analysis and tree, overview
-
malfunction
-
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
-
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
-
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
no changes in UV tolerance and therefore in the effectiveness of photoreactivation are observed for bccry2 deletion or overexpression strains. A retarded lesion spreading, 75% of wild-type, is noted for overexpressing OE::bccry2 strains following inoculation with conidia, overabundance of BcCRY2 causes reduced radial growth rates and delayed initiation of vegetative growth of germinating conidia in axenic culture, and this effect occurs independently of the light conditions
malfunction
the DELTAbccry1 mutant is unable to grow after UV exposure for 6 min, absence of photoreactivation. Overexpression of bccry1 increases UV tolerance, OE::bccry1 conidia show more efficient photoreactivation than the wild-type. Reintroduction of bccry1 into the deficient DELTAbccry1 mutant restores the photorepair activity to wild-type levels. Neither deletion nor overexpression of bccry1 affects differentiation under the conditions tested, the strains show wild-type-like conidiation
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
-
the DELTAbccry1 mutant is unable to grow after UV exposure for 6 min, absence of photoreactivation. Overexpression of bccry1 increases UV tolerance, OE::bccry1 conidia show more efficient photoreactivation than the wild-type. Reintroduction of bccry1 into the deficient DELTAbccry1 mutant restores the photorepair activity to wild-type levels. Neither deletion nor overexpression of bccry1 affects differentiation under the conditions tested, the strains show wild-type-like conidiation
-
malfunction
-
no changes in UV tolerance and therefore in the effectiveness of photoreactivation are observed for bccry2 deletion or overexpression strains. A retarded lesion spreading, 75% of wild-type, is noted for overexpressing OE::bccry2 strains following inoculation with conidia, overabundance of BcCRY2 causes reduced radial growth rates and delayed initiation of vegetative growth of germinating conidia in axenic culture, and this effect occurs independently of the light conditions
-
metabolism
-
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
-
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
-
third electron transfer pathway exists in members of the photolyase family that remained undiscovered so far
metabolism
-
third electron transfer pathway exists in members of the photolyase family, e.g. DASH cryptochrome, that remained undiscovered so far
physiological function
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
-
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
-
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
-
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
-
PHR2 protein plays a role in baculovirus DNA repair
physiological function
-
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
-
structural similarity between the larger N-terminal domain of primase (PriL) with the active site region of DNA photolyase
physiological function
-
very similar to plant cryptochromes
physiological function
-
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
-
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
-
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
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
-
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 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
the enzyme PhrB has a role in maintaining DNA supercoiling that is important for normal cell physiology
physiological function
ambient ultraviolet B (UVB) radiation induces lethal effects in the two-spotted spider mite Tetranychus urticae, whereas photoreactivation by irradiation with ultraviolet A and visible light (VIS) plays an important role to increase survival of mites irradiated by UVB. DNA lesions, cyclobutane pyrimidine dimers (CPDs), photoproducts linearly increase with the UVB dose. The CPDs are repaired after exposure to visible light. DNA damage and CPD photo enzymatic repair (PER) is significant for survival in this mite under ambient UVB radiation, but gene expression of CPD photolyase is unaffected by irradiation with UVB and VIS, while UVB-irradiated larvae survival rate decreases as the UVB cumulative dose increases, CPD frequency increased with the UVB cumulative dose
physiological function
conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. BcCRY2 belongs to the cry-DASH proteins and is dispensable for photorepair but performs regulatory functions by repressing conidiation in white and especially black/NUV light. Neither light nor the White Collar complex (WCC) is essential for the repression of conidiation through BcCRY2 when bccry2 is constitutively expressed. BcCRY2 affects the transcript levels of both WCC-induced and WCC-repressed genes, suggesting a signaling function downstream of the WCC. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY2 acts as a cryptochrome with a signaling function in regulating photomorphogenesis (repression of conidiation). BcCRY2 functions in the regulation of vegetative growth, overview. BcCRY2 has a negative impact on conidiation, the R/G-rich region of BcCRY2 is not essential for the regulation of conidiation. No impact of BcCRY2 on sclerotial development
physiological function
conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. CRY1 (BcCRY1), a cyclobutane pyrimidine dimer (CPD) photolyase, acts as the major enzyme of light-driven DNA repair (photoreactivation) and has no obvious role in signaling. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY1 acts as the major photolyase in photoprotection, BcCRY1 is crucial for photorepair, overview. No impact of BcCRY1 on sclerotial development
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair. Class I photolyase shows electron tunneling and high repair efficiency
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair. Class I photolyase shows electron tunneling and high repair efficiency
physiological function
CRY-DASH proteins have photolyase activity, photolyases repair Pyr<>Pyr dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum
physiological function
CRY-DASH proteins have photolyase activity, photolyases repair Pyr<>Pyr dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum. Consistent with their role in global gene regulation, cryptochrome genes (CmPHR2, CmPHR3 and CmPHR7) are differentially regulated, suggesting that they have a potential role in light-dependent transcriptional regulation in Cyanidioschyzon merolae
physiological function
DNA photolyase is a structure-specific DNA repair enzyme that reverses one of the most common types of UV damage in DNA molecules, the cis-syn cyclobutylpyrimidine dimer (CPD)
physiological function
photolyase, a class of flavoproteins, restores damaged DNA through absorption of blue light, CPD photolyase uses blue light to repair ultraviolet-induced DNA damage, cyclobutane pyrimidine dimers (CPDs), repair dynamics and mechanisms, cyclic electron-transfer reaction photocycle, overview
physiological function
photolyases are structure-specific DNA-repair enzymes that repair DNA lesions that have been induced by ultraviolet (UV) light. Escherichia coli DNA photolyase is a DNA-repair enzyme that repairs cyclobutane pyrimidine dimers (CPDs) which are formed on DNA upon exposure of cells to ultraviolet light. The photolyase catalyzes the CPD monomerization by a light-driven electron-transfer mechanism after the enzyme-substrate complex has formed. The enzyme requires flipping of the CPD site into an extrahelical position. The photolyase is unique in that it requires the two dimerized pyrimidine bases to flip rather than just a single damaged base
physiological function
residue Gln336 is important for the repair activity of CPD photolyase in Dunaliella salina and may represent key amino acid residues under salt stress
physiological function
the photoinduced electron transfer (ET) reaction of cyclobutane pyrimidine dimer (CPD) photolyase plays an essential role in its DNA repair reaction
physiological function
UV irradiation converts two adjacent pyrimidines, including thymines, to a cyclobutane pyrimidine dimer (CPD), and the enzyme photolyase uses blue light energy to break the two abnormal bonds joining the thymines and thus converts the thymine dimer to two normal thymines. Photolyase therefore repairs DNA and eliminates the harmful effects of UV light. The blue light-absorbing component of photolyase are chromophores. Photolyase from Escherichia coli contains two chromophores, which are two-electron reduced flavin adenine dinucleotide (FADH-) and methenyltetrahydrofolate (folate). The folate acts like a solar panel, absorbing light and transferring the excitation energy to FADH-. The flavin is the actual catalyst, and upon excitation by energy transfer from folate (and less efficiently by direct absorption of a photon) it carries out the repair reaction on the CPD by a radical mechanism through a cyclic redox reaction
physiological function
UV is responsible for the formation of damage-associated photoproducts on DNA: cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone (6-4) photoproducts (Pyr [6-4] Pyr). CPD photolyases repair pyrimidine dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum
physiological function
UV-induced lesions can be repaired by enzymes called photolyases. DNA photolyases use blue/near-UV light to remove these lesions using a process referred to as photoreactivation. CPD photolyases specifically repair CPD lesions in DNA
physiological function
-
UVB-induced DNA lesions in Xiphophorus fishes are thought to primarily be repaired via light dependent CPD and 6-4PP specific photolyases, cf. EC 4.1.99.13
physiological function
-
UVB-induced DNA lesions in Xiphophorus fishes are thought to primarily be repaired via light dependent CPD and 6-4PP specific photolyases, cf. EC 4.1.99.13
physiological function
-
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
-
physiological function
-
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
-
physiological function
-
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair. Class I photolyase shows electron tunneling and high repair efficiency
-
physiological function
-
the photoinduced electron transfer (ET) reaction of cyclobutane pyrimidine dimer (CPD) photolyase plays an essential role in its DNA repair reaction
-
physiological function
-
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
-
physiological function
-
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
-
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
-
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
-
physiological function
Xiphophorus maculatus Jp 163 B
-
UVB-induced DNA lesions in Xiphophorus fishes are thought to primarily be repaired via light dependent CPD and 6-4PP specific photolyases, cf. EC 4.1.99.13
-
physiological function
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
CRY-DASH proteins have photolyase activity, photolyases repair Pyr<>Pyr dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum
-
physiological function
-
the enzyme PhrB has a role in maintaining DNA supercoiling that is important for normal cell physiology
-
physiological function
-
DNA photolyase is a structure-specific DNA repair enzyme that reverses one of the most common types of UV damage in DNA molecules, the cis-syn cyclobutylpyrimidine dimer (CPD)
-
physiological function
-
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
-
physiological function
-
CRY-DASH proteins have photolyase activity, photolyases repair Pyr<>Pyr dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum. Consistent with their role in global gene regulation, cryptochrome genes (CmPHR2, CmPHR3 and CmPHR7) are differentially regulated, suggesting that they have a potential role in light-dependent transcriptional regulation in Cyanidioschyzon merolae
-
physiological function
-
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
-
physiological function
-
conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. CRY1 (BcCRY1), a cyclobutane pyrimidine dimer (CPD) photolyase, acts as the major enzyme of light-driven DNA repair (photoreactivation) and has no obvious role in signaling. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY1 acts as the major photolyase in photoprotection, BcCRY1 is crucial for photorepair, overview. No impact of BcCRY1 on sclerotial development
-
physiological function
-
conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. BcCRY2 belongs to the cry-DASH proteins and is dispensable for photorepair but performs regulatory functions by repressing conidiation in white and especially black/NUV light. Neither light nor the White Collar complex (WCC) is essential for the repression of conidiation through BcCRY2 when bccry2 is constitutively expressed. BcCRY2 affects the transcript levels of both WCC-induced and WCC-repressed genes, suggesting a signaling function downstream of the WCC. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY2 acts as a cryptochrome with a signaling function in regulating photomorphogenesis (repression of conidiation). BcCRY2 functions in the regulation of vegetative growth, overview. BcCRY2 has a negative impact on conidiation, the R/G-rich region of BcCRY2 is not essential for the regulation of conidiation. No impact of BcCRY2 on sclerotial development
-
physiological function
-
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
-
additional information
-
electron-tunneling pathways and functional role of adenine moiety of wild-type and mutant enzymes, overview
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
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
-
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
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
analysis of flavin in various redox states and the active-site solvation dynamics in photolyases, and dynamics of a similar CPD biomimetic system but with low repair efficiency, overview. High repair quantum yield by CPD photolyases. Ultrafast active-site solvation dynamics in photolyases. Dynamic solvation in binding and active sites plays a critical role in protein recognition and enzyme reaction and such local motions optimize spatial configurations and minimize energetic pathways. X-ray structures and molecular dynamics (MD) simulations show certain water molecules trapped at the active sites besides charged and polar amino acids surrounding the functional chromophore of FADH-. Thus, upon excitation the local polar environments at the active sites proceed to a series of relaxations
additional information
comparison of the photoactive center of wild-type Escherichia coli enzyme with the one from Arabidopsis thaliana CRY1 enzyme
additional information
-
comparison of the photoactive center of wild-type Escherichia coli enzyme with the one from Arabidopsis thaliana CRY1 enzyme
additional information
during purification, the flavin undergoes changes in oxidation state and as a consequence the enzyme may exhibit colors ranging from purple to orange. Three-dimensional structure and structural basis for the proposed reaction mechanism, overview
additional information
-
during purification, the flavin undergoes changes in oxidation state and as a consequence the enzyme may exhibit colors ranging from purple to orange. Three-dimensional structure and structural basis for the proposed reaction mechanism, overview
additional information
enzyme structure comparisons and molecular modeling, overview. The enzyme AnPL from Anacystis nidulans is mesophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Sulfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
additional information
enzyme structure comparisons and molecular modeling, overview. The enzyme EcPL from Escherichia coli is mesophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Sulfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
additional information
enzyme structure comparisons and molecular modeling, overview. The enzyme from Sulfolobus tokodaii is hyperthermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
additional information
enzyme structure comparisons and molecular modeling, overview. The enzyme from Thermus thermophilus is thermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
additional information
homology analysis of PL protein structures spanning 70°C in growth temperature supports the data that the structure of cold-adapted DNA photolyase CpPL is quite different from warm-adapted DNA photolyases. Homology modeling of CpPL using CPD-PL from Sulfolobus tokodaii (StPL, 2E0I. PDB, chain A) as a template
additional information
in class I EcPL, the initial electron injection adopts dominant tunneling pathways directly from LfH- to CPD. Reaction free energy profile along the reaction coordinate for EcPL CPD repair, overview
additional information
light-induced conformational changes in the plant cryptochrome photolyase homology region resolved by selective isotope labeling and infrared spectroscopy
additional information
-
light-induced conformational changes in the plant cryptochrome photolyase homology region resolved by selective isotope labeling and infrared spectroscopy
additional information
reduced anionic flavin adenine dinucleotide (FADH-) is the critical cofactor in DNA photolyase (PL) for the repair of cyclobutane pyrimidine dimers (CPD) in UV-damaged DNA. The initial step involves photoinduced electron transfer from FADH- radical to the CPD. The adenine (Ade) moiety is nearly stacked with the flavin ring, an unusual conformation compared to other FAD-dependent proteins
additional information
the crystal structure of Anacystis nidulans photolyase with CPD complex shows that the Ade moiety of FADH- is at van der Waals distances with both base moieties of CPD, 3.1 A to the 5' side and 3.2 A to 3'. The first carbon atom is linked to the isoalloxazine ring at 3.6 A
additional information
the enzymatic activity and thermodynamics of substrate binding for the enzyme from Sulfolobus solfataricus are directly compared to the enzyme from Escherichia coli, overview. Turnover numbers and catalytic activity are virtually identical, but organic co-solvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by about 2 kJ/mol. The enthalpy of binding is about 10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding is observed when ionic strength studies are used to separate binding interactions into electrostatic and nonelectrostatic contributions, DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein. Reported differences between mesophilic and thermophilic enzymes include an increase in the number of ion pairs/salt bridges, better packing of hydrophobic amino acids, and increased hydrogen bonding for the thermophilic proteins. Comparison of the enthalpy of binding. Analysis of enzyme-substrate interactions, overview
additional information
-
the enzymatic activity and thermodynamics of substrate binding for the enzyme from Sulfolobus solfataricus are directly compared to the enzyme from Escherichia coli, overview. Turnover numbers and catalytic activity are virtually identical, but organic co-solvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by about 2 kJ/mol. The enthalpy of binding is about 10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding is observed when ionic strength studies are used to separate binding interactions into electrostatic and nonelectrostatic contributions, DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein. Reported differences between mesophilic and thermophilic enzymes include an increase in the number of ion pairs/salt bridges, better packing of hydrophobic amino acids, and increased hydrogen bonding for the thermophilic proteins. Comparison of the enthalpy of binding. Analysis of enzyme-substrate interactions, overview
additional information
to analyze the UV-induced DNA lesion repair mechanism, the excited states of the active site (including the electron donor and acceptor) is calculated
additional information
-
to analyze the UV-induced DNA lesion repair mechanism, the excited states of the active site (including the electron donor and acceptor) is calculated
additional information
-
homology analysis of PL protein structures spanning 70°C in growth temperature supports the data that the structure of cold-adapted DNA photolyase CpPL is quite different from warm-adapted DNA photolyases. Homology modeling of CpPL using CPD-PL from Sulfolobus tokodaii (StPL, 2E0I. PDB, chain A) as a template
-
additional information
-
the crystal structure of Anacystis nidulans photolyase with CPD complex shows that the Ade moiety of FADH- is at van der Waals distances with both base moieties of CPD, 3.1 A to the 5' side and 3.2 A to 3'. The first carbon atom is linked to the isoalloxazine ring at 3.6 A
-
additional information
-
enzyme structure comparisons and molecular modeling, overview. The enzyme AnPL from Anacystis nidulans is mesophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Sulfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
-
additional information
-
to analyze the UV-induced DNA lesion repair mechanism, the excited states of the active site (including the electron donor and acceptor) is calculated
-
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
-
the enzymatic activity and thermodynamics of substrate binding for the enzyme from Sulfolobus solfataricus are directly compared to the enzyme from Escherichia coli, overview. Turnover numbers and catalytic activity are virtually identical, but organic co-solvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by about 2 kJ/mol. The enthalpy of binding is about 10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding is observed when ionic strength studies are used to separate binding interactions into electrostatic and nonelectrostatic contributions, DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein. Reported differences between mesophilic and thermophilic enzymes include an increase in the number of ion pairs/salt bridges, better packing of hydrophobic amino acids, and increased hydrogen bonding for the thermophilic proteins. Comparison of the enthalpy of binding. Analysis of enzyme-substrate interactions, overview
-
additional information
-
enzyme structure comparisons and molecular modeling, overview. The enzyme from Thermus thermophilus is thermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
-
additional information
-
enzyme structure comparisons and molecular modeling, overview. The enzyme from Sulfolobus tokodaii is hyperthermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
-