Our results indicate

that L fermentum NTD are distribute

Our results indicate

that L. fermentum NTD are distributed not only in the cytoplasm but also on http://www.selleckchem.com/products/INCB18424.html the cell wall surface, and further studies showed that surface-attached NTD can be released into the culture broth and conventional buffers. Lactobacilli can be divided into two groups depending on whether or not they require deoxyribonucleosides for growth (Kaminski, 2002). Most lactobacilli that utilize the salvage pathway degrade exogenous nucleosides to the nucleobase and pentose sugar via a nucleoside phosphorylase. Others possess a special salvage system based on a nucleoside deoxyribosyltransferase and require a deoxynucleoside in combination with purine and pyrimidine bases for their DNA synthesis (Kilstrup

et al., 2005). N-deoxyribosyltransferases (EC, also called trans-N-deoxyribosylases, catalyze the transfer of a 2′-deoxyribosyl group from DNA Damage inhibitor a donor deoxynucleoside to an acceptor nucleobase (Anand et al., 2004). This enzyme was initially described for lactobacilli and has also been found in certain species of Streptococcus (Chawdhri et al., 1991) and in some protozoans such as Crithidia luciliae (Steenkamp, 1991). Two types of N-deoxyribosyltransferase have been described in lactobacilli: type I is purine deoxyribosyltransferase (PTD), specific for the transfer of deoxyribose between two purines; type II is nucleoside 2′-deoxyribosyltransferase (NTD), which catalyzes the transfer of deoxyribose between either purines

or pyrimidines (Holguin & Cardinaud, 1975; Miyamoto et al., 2007). Several dozen reports on lactobacilli N-deoxyribosyltransferase have been RAS p21 protein activator 1 published since the initial study by Macnutt (Macnutt, 1950). The three-dimensional structure of these enzymes has been solved, and their kinetic mechanisms as well as their catalytic and substrate binding sites have been well characterized (Armstrong et al., 1996; Anand et al., 2004). The transfer reactions, catalyzed by either PTD or NTD, proceed following a ping-pong bi-bi mechanism by formation of a covalent deoxyribosyl enzyme intermediate (Danzin & Cardinau, 1974; Danzin & Cardinaud, 1976). As NTD has broader substrate specificity than PTD, it has attracted more attention. NTD also has a hydrolase function such that, in the absence of an acceptor base, the nucleoside is converted to its base and deoxyribose (Smar et al., 1991). Most antiviral or anticancer drugs are analogues of naturally occurring nucleosides. The use of purified enzyme or intact bacterial cells containing NTD enables a one-pot transglycosylation reaction at high yields, providing an interesting alternative to traditional multistep chemical methods (Fernandez-Lucas et al., 2010). Stereospecific reactions and high tolerance for various modifications in the bases also make NTD ideally suited to serve as biocatalyst for the production of nucleosides and nucleoside analogues (Okuyama et al.

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