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Literature summary for 4.1.99.3 extracted from

  • Mueller, P.; Brettel, K.; Grama, L.; Nyitrai, M.; Lukacs, A.
    Photochemistry of wild-type and N378D mutant E. coli DNA photolyase with oxidized FAD cofactor studied by transient absorption spectroscopy (2016), Chemphyschem, 17, 1329-1340 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
N378D site-directed mutagenesis, the asparagine facing the N5 of the FAD isoalloxazine is replaced by aspartic acid, known to protonate FAD- radical (formed by electron transfer from the tryptophan chain) in plant cryptochromes (CRYs). But the mutant protein does not show this protonation. EcPL mutant protein approaches the flavin with similar kinetics to that of the aspartic acid at the corresponding position in plant CRY, but is unable to fully transfer the proton to N5 of the flavin, resulting in a FAD radical with unusual spectral properties. Possibly, the pKa values of FADH radical and/or this aspartic acid in the EcPL N378D mutant protein differ from those in native plant CRY, such that proton transfer is energetically disfavored. Absorption kinetics compared to wild-type Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information reaction kinetics, absorption spectra of wild-type EcPL and MTHF antenna-free mutant E109A/N378D EcPL, transient absorption kinetics on nano- and microsecond time scales at six characteristic wavelengths, spectral analysis of transient absorption kinetics, overview 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
-
-

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 photochemistry of wild-type and N378D mutant DNA photolyase with oxidized FAD cofactor studied by transient absorption spectroscopy, overview Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
DNA photolyase
-
Escherichia coli
EcPL
-
Escherichia coli
PhrB
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD four redox states of FAD are relevant for the various functions of DNA photolyases: fully reduced FADH- required for DNA photorepair, and the two semireduced radical states FAD- radical and FADH radical formed in electron transfer reactions. Absorption spectra of wild-type EcPL and MTHF antenna-free mutant E109A/N378D EcPL, transient absorption kinetics on nano- and microsecond time scales at six characteristic wavelengths, spectral analysis of transient absorption kinetics, overview Escherichia coli

General Information

General Information Comment Organism
evolution DNA photolyases (PLs) and evolutionarily related cryptochrome (CRY) blue-light receptors form a widespread superfamily of flavoproteins involved in DNA photorepair and signaling functions. They share a flavin adenine dinucleotide (FAD) cofactor and an electron-transfer (ET) chain composed typically of three tryptophan residues that connect the flavin to the protein surface Escherichia coli
additional information comparison of the photoactive center of wild-type Escherichia coli enzyme with the one from Arabidopsis thaliana CRY1 enzyme Escherichia coli