5'-deoxyribose-5-phosphate lyase activity

Definition

Target type: molecularfunction

Catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site. [PMID:11251121, PMID:16120966]

5'-Deoxyribose-5-phosphate lyase activity is a crucial enzyme activity involved in the breakdown of deoxyribose-5-phosphate (dRP), a product of DNA damage. This enzymatic activity specifically cleaves the carbon-oxygen bond between the 5' carbon of deoxyribose and the phosphate group, resulting in the release of free phosphate and a 5-deoxy-D-ribose molecule. The reaction is essential for DNA repair pathways, particularly the base excision repair (BER) pathway, as it removes damaged nucleotides from DNA.

The mechanism of this enzymatic activity involves the formation of an enzyme-substrate complex, where the enzyme binds to dRP and facilitates the cleavage of the carbon-oxygen bond. The active site of the enzyme often contains a metal ion, typically magnesium, which aids in the catalytic process. The enzyme may also utilize a nucleophile, like a cysteine or lysine residue, to attack the phosphate group, ultimately leading to the bond breakage and the release of the products.

5'-Deoxyribose-5-phosphate lyase activity plays a vital role in maintaining the integrity of DNA. By removing damaged nucleotides, this activity prevents mutations and genomic instability. Defects in this enzyme activity can lead to an accumulation of DNA damage, potentially contributing to various diseases, including cancer. This activity is also a target for drug development, aiming to enhance DNA repair mechanisms and combat diseases associated with DNA damage.'
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Proteins (3)

Compounds (30)