Nucleoside 2-deoxyribosyltransferase (NDT)

Nucleoside 2-deoxyribosyltransferase (NDT) is an enzyme found in certain microorganisms that plays a crucial role in the salvage pathway of nucleotide metabolism, catalyzing the exchange of purine or pyrimidine bases between 2'-deoxyribonucleosides through the transfer of the deoxyribose moiety. It belongs to the glycosyltransferase family, specifically the pentosyltransferases, and facilitates a reaction mechanism involving a double displacement pathway with a covalent intermediate. The enzyme is utilized primarily as a biocatalyst to synthesize nucleoside analogs for antiviral or anticancer applications, taking advantage of its substrate flexibility, especially for modified or fluorinated nucleoside analogues. Most research and application focus on its use in microbial and synthetic biotechnology, rather than as a direct therapeutic target in human medicine[1][2][3][4][5][7][9].

Other names

Nucleoside deoxyribosyltransferaseDeoxyribosyltransferase (DRTase)Nucleoside:purine(pyrimidine) deoxyribosyltransferasePurine nucleoside:purine deoxyribosyltransferaseNucleoside trans-N-deoxyribosylaseTrans-deoxyribosylaseTrans-N-glycosidaseTrans-N-deoxyribosylaseNucleoside deoxyribosyltransferase INucleoside deoxyribosyltransferase II

Catalyzes reversible transfer of 2-deoxyribose moiety from one nucleoside to another base (transglycosylation). Proceeds via double displacement (ping-pong-bi-bi mechanism) with a covalent enzyme-deoxyribose intermediate and retention of stereochemistry.