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Literature summary extracted from

  • Zhang, M.; Wang, L.; Shu, S.; Sancar, A.; Zhong, D.
    Bifurcating electron-transfer pathways in DNA photolyases determine the repair quantum yield (2016), Science, 354, 209-213 .
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.99.3 chloroplast
-
 Arabidopsis thaliana 9507
-
4.1.99.3 mitochondrion
-
 Arabidopsis thaliana 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.3 cyclobutadipyrimidine (in DNA) Escherichia coli
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Arabidopsis thaliana
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Synechococcus elongatus PCC 7942 = FACHB-805
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Caulobacter vibrioides
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Drosophila melanogaster
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Caulobacter vibrioides NA1000 / CB15N
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1
-
 2 pyrimidine residues (in DNA)
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.3 Arabidopsis thaliana Q84KJ5
-
-
4.1.99.3 Arabidopsis thaliana Q9SB00
-
-
4.1.99.3 Caulobacter vibrioides A0A0H3C7H5 i.e. Caulobacter riboides
-
4.1.99.3 Caulobacter vibrioides NA1000 / CB15N A0A0H3C7H5 i.e. Caulobacter riboides
-
4.1.99.3 Drosophila melanogaster Q24443
-
-
4.1.99.3 Escherichia coli P00914
-
-
4.1.99.3 Synechococcus elongatus PCC 7942 = FACHB-805 P05327 i.e. Synechocystis sp.
-
4.1.99.3 Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1 P05327 i.e. Synechocystis sp.
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.99.3 cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview Escherichia coli
a
4.1.99.3 cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview Arabidopsis thaliana
a
4.1.99.3 cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview Synechococcus elongatus PCC 7942 = FACHB-805
a
4.1.99.3 cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview Caulobacter vibrioides
a
4.1.99.3 cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview Drosophila melanogaster
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Escherichia coli 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Arabidopsis thaliana 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Synechococcus elongatus PCC 7942 = FACHB-805 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Caulobacter vibrioides 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Drosophila melanogaster 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) enzyme AtCRY3 is specific for single-stranded DNA substrates Arabidopsis thaliana 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Caulobacter vibrioides NA1000 / CB15N 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1 2 pyrimidine residues (in DNA)
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.3 AnPL
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 AtCry3
-
 Arabidopsis thaliana
4.1.99.3 AtPL
-
 Arabidopsis thaliana
4.1.99.3 CcPL
-
 Caulobacter vibrioides
4.1.99.3 class I PL
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 class II AtPL
-
 Arabidopsis thaliana
4.1.99.3 class II DmPL
-
 Drosophila melanogaster
4.1.99.3 class II PL
-
 Arabidopsis thaliana
4.1.99.3 class II PL
-
 Drosophila melanogaster
4.1.99.3 class III PL
-
 Caulobacter vibrioides
4.1.99.3 CPD photolyase
-
 Escherichia coli
4.1.99.3 CPD photolyase
-
 Arabidopsis thaliana
4.1.99.3 CPD photolyase
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 CPD photolyase
-
 Caulobacter vibrioides
4.1.99.3 CPD photolyase
-
 Drosophila melanogaster
4.1.99.3 DmPL
-
 Drosophila melanogaster
4.1.99.3 DNA photolyase
-
 Escherichia coli
4.1.99.3 DNA photolyase
-
 Arabidopsis thaliana
4.1.99.3 DNA photolyase
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 DNA photolyase
-
 Caulobacter vibrioides
4.1.99.3 DNA photolyase
-
 Drosophila melanogaster
4.1.99.3 EcPL
-
 Escherichia coli
4.1.99.3 PHR
-
 Drosophila melanogaster
4.1.99.3 phrA
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 ssDNA
-
 Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.3 FAD the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions Escherichia coli
4.1.99.3 FAD the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions Arabidopsis thaliana
4.1.99.3 FAD the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 FAD the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions Caulobacter vibrioides
4.1.99.3 FAD the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions Drosophila melanogaster

General Information

EC Number General Information Comment Organism
4.1.99.3 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 Escherichia coli
4.1.99.3 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 Arabidopsis thaliana
4.1.99.3 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 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 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 Caulobacter vibrioides
4.1.99.3 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 Drosophila melanogaster
4.1.99.3 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 Escherichia coli
4.1.99.3 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 Arabidopsis thaliana
4.1.99.3 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 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 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 Caulobacter vibrioides
4.1.99.3 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 Drosophila melanogaster