Enzymes
Product List
UNG E.Coli Active
Recombinant E.Coli Uracil DNA Glycosylase, Active
UNG E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide UNG is purified by proprietary chromatographic techniques.
UNG Heat Labile
Recombinant Psychrophilic Marine Bacterium Uracil DNA Glycosylase, Heat Labile
UNG psychrophilic marine bacterium Recombinant produced in E.Coli is a single, non-glycosylated polypeptide. UNG is purified by proprietary chromatographic techniques.
Introduction
Glycosylases are a class of enzymes that hydrolyze glycosyl compounds. They are a type of hydrolase (EC 3.2) and are divided into two main groups: glycosidases, which hydrolyze O- and S-glycosyl compounds (EC 3.2.1), and enzymes that hydrolyze N-glycosyl compounds (EC 3.2.2) . Glycosylases play a crucial role in the base excision repair (BER) pathway, which is responsible for repairing damaged DNA bases .
Glycosylases are widely expressed across different tissues and organisms. They are found in all kingdoms of life, from bacteria to humans . In humans, glycosylases are involved in various cellular processes, including DNA repair and the regulation of gene expression . They are typically localized in the nucleus and cytoplasm, where they interact with DNA and other cellular components .
The primary function of glycosylases is to recognize and excise damaged bases from DNA, initiating the BER pathway . This process is essential for maintaining genome stability and preventing mutations that could lead to diseases such as cancer . Glycosylases also play a role in immune responses by recognizing and repairing DNA damage caused by pathogens . Additionally, they are involved in the regulation of gene expression through the removal of methylated bases, which can affect chromatin structure and transcription .
Glycosylases operate by flipping the damaged base out of the DNA helix into an active site pocket, where it is excised . This mechanism allows for the sensitive detection of even minor base irregularities . Monofunctional glycosylases use an activated water molecule to cleave the N-glycosidic bond, while bifunctional glycosylases use an amine residue as a nucleophile . The excised base is then replaced through a series of downstream signaling cascades involving other BER enzymes .
The expression and activity of glycosylases are tightly regulated at multiple levels. Transcriptional regulation involves various transcription factors that bind to the promoter regions of glycosylase genes . Post-translational modifications, such as phosphorylation and ubiquitination, also play a role in modulating glycosylase activity and stability . Additionally, glycosylases can be regulated through interactions with other proteins and cellular components .
Glycosylases have numerous applications in biomedical research and clinical settings. They are used as diagnostic tools for detecting DNA damage and mutations . In therapeutic strategies, glycosylase inhibitors are being explored as potential anticancer agents . These enzymes are also employed in the study of gene expression and epigenetic modifications .
Throughout the life cycle, glycosylases play a critical role in maintaining genome integrity from development to aging . During development, they ensure the proper repair of DNA damage, which is crucial for normal growth and differentiation . In aging, glycosylases help mitigate the accumulation of DNA damage that can lead to age-related diseases . Their activity is also essential in preventing the onset and progression of various diseases, including cancer .
