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Literature summary for 4.1.99.3 extracted from

  • Liu, Z.; Wang, L.; Zhong, D.
    Dynamics and mechanisms of DNA repair by photolyase (2015), Phys. Chem. Chem. Phys., 17, 11933-11949 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.99.3

Protein Variants

Protein Variants Comment Organism
E274A site-directed mutagenesis of an active site residue near the substrate side, has critical effect on repair efficiency Escherichia coli
M345A site-directed mutagenesis of an active site residue, has a poor effect on repair efficiency Escherichia coli
N378C site-directed mutagenesis of an active site residue near the cofactor side, has critical effect on repair efficiency Escherichia coli
R226A site-directed mutagenesis of an active site residue, has a poor effect on repair efficiency Escherichia coli
R342A site-directed mutagenesis of an active site residue, has a poor effect on repair efficiency Escherichia coli

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)
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P00914
-
-

Reaction

Reaction Comment Organism Reaction ID
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) dynamics and mechanism of CPD repair by photolyase, detailed overview. In contrast to the computational reaction model the thymine dimer splits by a sequential pathway Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclobutadipyrimidine (in DNA)
-
 Escherichia coli 2 pyrimidine residues (in DNA)
-
 ?
additional information 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 Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
CPD photolyase
-
 Escherichia coli
cyclobutane pyrimidine dimer photolyase
-
 Escherichia coli
DNA photolyase
-
 Escherichia coli
photolyase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD steady-state spectra of flavin at various redox states and active-site solvation dynamics in photolyases, overview Escherichia coli

General Information

General Information Comment Organism
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 Escherichia coli
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 Escherichia coli