4.1.99.13: (6-4)DNA photolyase
This is an abbreviated version!
For detailed information about (6-4)DNA photolyase, go to the full flat file.
Word Map on EC 4.1.99.13
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4.1.99.13
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photoproducts
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cyclobutane
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uv-induced
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cryptochromes
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photoreactivation
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light-dependent
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pyrimidone
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blue-light
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photorepair
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oxetane
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pyrimidine-pyrimidone
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photoreduction
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photolesion
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dash
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ostreococcus
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four-membered
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fadox
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photoreception
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cry-dashs
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dewar
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cryptochrome-dash
- 4.1.99.13
- photoproducts
-
cyclobutane
-
uv-induced
-
cryptochromes
-
photoreactivation
-
light-dependent
-
pyrimidone
-
blue-light
-
photorepair
-
oxetane
-
pyrimidine-pyrimidone
-
photoreduction
-
photolesion
-
dash
- ostreococcus
-
four-membered
- fadox
-
photoreception
- cry-dashs
-
dewar
- cryptochrome-dash
Reaction
= 2 pyrimidine residues (in DNA)
Synonyms
(6-4) DNA photolyase, (6-4) photolyase, (6-4) PHR, (6-4) PL, (6-4) PP-specific PL, (6-4)-Phr, (6-4)photolyase, 6-4 DNA photolyase, 6-4 photolyase, 6-4CiPhr, 6-4PP-photolyase, animal (6-4) photolyase, At64, At64PHR, bacterial (6-4) photolyase, CmPHR1, Cry1, CryB, deoxyribodipyrimidine photolyase-related protein, Dm64, DNA photolyase, Ds64PHR, H64PRH, human (6-4) photolyase homologous protein, NF-10, OtCPF1, phr (6-4), PhrB, PL-(6-4), prokaryotic (6-4) photolyase, RSP_3077, TRIREDRAFT_77473, XELAEV_18035355mg, Xl64phr
ECTree
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Cofactor
Cofactor on EC 4.1.99.13 - (6-4)DNA photolyase
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[4Fe-4S] cluster
the iron-sulfur cluster is an indispensable cofactor for the structural integrity of the enzyme protein
the PhrB structure contains 6,7-dimethyl-8-ribityllumazine as an antenna chromophore, binding site-structure, overview
6,7-dimethyl-8-ribityllumazine
DMRL, serves as an antenna chromophore for photoreduction and DNA repair in the wild-type enzyme
FAD
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FAD
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Resonance Raman spectra of (6-4) photolyase having neutral semiquinoid and oxidized forms of FAD. Density functional theory (DFT) calculations are carried out on the neutral semiquinone. The marker band of a neutral semiquinone at 1606 cm-1 in H2O, splits into two comparable bands at 1594 and 1608 cm-1 in D2O, and similarly, that at 1522 cm-1 in H2O does into three bands at 1456, 1508, and 1536 cm-1 in D2O. This D2O effect is recognized only after being oxidized once and photoreduced to form a semiquinone again, but not by simple H/D exchange of solvent. Some Raman bands of the oxidized form are observed at significantly low frequencies (1621, 1576 cm-1) and with band splittings (1508/1493, 1346/1320 cm-1). These Raman spectral characteristics indicate strong H-bonding interactions (at N5-H, N1), a fairly hydrophobic environment, and an electron-lacking feature in benzene ring of the FAD cofactor, which seems to specifically control the reactivity of (6-4) photolyase
FAD
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FAD cofactor photoactivation in (64) photolyase occurs via two sequential single-electron reduction steps with a tyrosine residue acting as final electron donor
FAD
non-covalently bound to the enzyme. Flavin to apoprotein molecular ratio of 64%. FAD is present in three different redox states: the fully oxidized form (FADox, 82%), the neutral semiquinone (14%) and the fully reduced anion (4%)
FAD
in the structure of (6-4) photolyase, there is a phosphate anion bound to Glu-243 and Trp-238, close to FAD
FAD
an essential cofactor, the enzyme contains FAD at a concentration of less than 0.2%
FAD
chromophore, assumes a prototypical U-shaped conformation
FAD
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for activation of Xenopus (6-4) PHR, FADox is first converted to a neutral radical form by light-induced one-electron and one-proton transfers and then into a fully reduced form by light-induced one electron transfer, mechanism, overview
FAD
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transition from the oxidized to the semi-reduced form of FAD is characterized by absorbance decreases at around 450 nm and 370 nm, and an increase at 580 nm
a cubane-type Fe-S cluster, residue Tyr424 of PhrB is part of the DNA-binding site and provides an electron link to the Fe-S cluster
additional information
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the enzyme protein expressed in Escherichia coli does not bind a second chromophore, such as 5,10-methenyltetrahydrofolate, MTHF
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additional information
the protein harbors three cofactors: the enzymatically active FAD chromophore, a second chromophore, 6,7-dimethyl-8-ribityllumazine (DMRL) and a cubane-type Fe-S cluster
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additional information
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the protein harbors three cofactors: the enzymatically active FAD chromophore, a second chromophore, 6,7-dimethyl-8-ribityllumazine (DMRL) and a cubane-type Fe-S cluster
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