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Literature summary for 4.1.99.3 extracted from

  • Xu, L.; Zhu, G.
    The roles of several residues of Escherichia coli DNA photolyase in the highly efficient photo-repair of cyclobutane pyrimidine dimers (2010), J. Nucleic Acids, 2010, 794782.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of photolyase shows that a positively charged groove on the surface of the protein which might interact with the DNA backbone and a hydrophobic cavity locates at the center. The cavity has the right dimension to hold a cis,syn cyclobutane pyrimidine dimer, and Trp277 forms one side wall of it. Photolyase binds DNA chain containing a cyclobutane pyrimidine dimer, flips it out into the cavity, and Trp277 stacks with the 5' side of the cyclobutane pyrimidine dimer by pi-pi interaction Escherichia coli

Protein Variants

Protein Variants Comment Organism
N378S mutant shows no stable radical state of the cofactor FADH. Furthermore, catalytic activity is lost Escherichia coli
W277E the binding affinity for CPD substrate is lower for 1000fold, although the photochemical properties and the quantum yields for catalyses (under the irradiation wavelengths at 366nm and 384 nm) of the mutant is indistinguishable from the wild-type enzyme Escherichia coli
W277R the binding affinity for CPD substrate is lower for 300fold, although the photochemical properties and the quantum yields for catalyses (under the irradiation wavelengths at 366nm and 384 nm) of the mutant is indistinguishable from the wild-type enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Synonyms

Synonyms Comment Organism
DNA photolyase
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
5,10-methenyltetrahydropterolypolyglutamate
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Escherichia coli
FAD the physiological form of the enzyme contains a fully reduced FAD (FADH-) that is required for its activity both in vivo and in vitro. It binds a cyclobutane pyrimidine dimer (CPD) in DNA independent of light and flips the dimer out of the double helix into the active site cavity to make a stable enzyme-substrate complex. Enzyme usually purified with FAD in the blue neutral radical form. The purified enzyme can hold its radical flavin cofactor unoxidized in aerobic conditions for several days Escherichia coli