phrB E.Coli
Description
Product Specs
Product Science Overview
The primary function of deoxyribodipyrimidine photo-lyase is to catalyze the light-dependent monomerization of cyclobutyl pyrimidine dimers (CPDs) that form between adjacent pyrimidine bases on the same DNA strand upon exposure to UV radiation . These CPDs are a major form of DNA damage induced by UV light, and their presence can lead to mutations and disruptions in DNA replication and transcription.
The enzyme absorbs visible light in the range of 300-600 nm, which provides the energy required for the catalytic process . Upon absorption of light, electrons are transferred from tryptophan residues (Trp-307, Trp-360, and Trp-383) to the flavin adenine dinucleotide (FAD) cofactor, resulting in the fully reduced catalytic form of FAD (FADH^-) . This reduced form of FAD then facilitates the cleavage of the cyclobutyl ring of the CPD, restoring the original pyrimidine bases and thereby repairing the DNA .
Deoxyribodipyrimidine photo-lyase is a flavoprotein that contains several cofactor binding sites . The enzyme binds one molecule of FAD per subunit, which is essential for its catalytic activity . Additionally, it binds one molecule of 5,10-methenyltetrahydrofolate (MTHF) non-covalently per subunit . MTHF acts as a light-harvesting cofactor, absorbing light and transferring the energy to FAD for the photoreactivation process .
Recombinant deoxyribodipyrimidine photo-lyase is produced by cloning the phrB gene into an expression vector and transforming it into a suitable host, such as E. coli . The recombinant enzyme is then purified for research and industrial applications. This recombinant form is used to study the enzyme’s structure, function, and potential applications in biotechnology and medicine .
In summary, deoxyribodipyrimidine photo-lyase is a critical enzyme for DNA repair in E. coli, utilizing light energy to reverse UV-induced DNA damage. Its recombinant form allows for detailed studies and potential biotechnological applications.
