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Literature summary extracted from

  • Henry, A.A.; Jimenez, R.; Hanway, D.; Romesberg, F.E.
    Preliminary characterization of light harvesting in E. coli DNA photolyase (2004), ChemBioChem, 5, 1088-1094.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.3 E109D mutant enzyme is unable to bind the methenyltetrahydrofolate cofactor under any conditions examined Escherichia coli
4.1.99.3 E109Q mutant enzyme is unable to bind the methenyltetrahydrofolate cofactor under any conditions examined Escherichia coli
4.1.99.3 H44F binds and retains methenyltetrahydrofolate under normal reconstitution conditions Escherichia coli
4.1.99.3 H44F mutant enzyme retains no methenyltetrahydrofolate upon purification Escherichia coli
4.1.99.3 L375H binds methenyltetrahydrofolate more weakly than wild-type enzyme Escherichia coli
4.1.99.3 N108L binds and retains methenyltetrahydrofolate under normal reconstitution conditions Escherichia coli
4.1.99.3 N108L mutant enzyme retains no methenyltetrahydrofolate upon purification Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.3 Escherichia coli
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-
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Source Tissue

EC Number Source Tissue Comment Organism Textmining

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.3 methenyltetrahydrofolate the enzyme utilizes the the antenna cofactor to harvest light energy for the repair of thymine dimers in DNA. For this purpose, the enzyme evolved to bind the cofactor and red-shift its absorption maximum by 25 nm Escherichia coli