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Literature summary for 4.1.99.3 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
Search for more literature for 4.1.99.3

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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
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
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
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
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)

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

Synonyms

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

Cofactor

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

General Information

General Information Comment Organism
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
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
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
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
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
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
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
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
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
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