N2665
Nucleoside Deoxyribosyltransferase II from Lactobacillus leichmanii
lyophilized powder, recombinant, expressed in E. coli
Synonym(s):
Nucleoside Deoxyribosyltransferase II from Lactobacillus leichmanii, DRTase, Deoxyribose transferase, NDT, nucleoside:purine(pyrimidine) deoxy-D-ribosyltransferase
recombinant
expressed in E. coli
Quality Level
Assay
≥80% protein basis (biuret)
form
lyophilized powder
specific activity
≥1.0 units/mg protein
sequence note
MPKKTIYFGAGWFTDRQNKAYKEAMEALKENPTIDLENSYVPLDNQYKGIRVDEHPEYLHDKVWATATYNNDLNGIKTNDIMLGVYIPDEEDVGLGMELGYALSQGKYVLLVIPDEDYGKPINLMSWGVSDNVIKMSQLKDFNFNKPRFDFYEGAVY
storage temp.
−20°C
Application
Nucleoside deoxyribosyltransferase II has been used in a study that assessed its enzymatic synthesis with 2′-deoxyguanosine. Nucleoside deoxyribosyltransferase II has also been used in studies to investigate its molecular cloning, expression and specificity.
Suitable for the enzymatic nucleoside synthesis.
Biochem/physiol Actions
Enzymatic nucleoside synthesis is an attractive alternative to traditional chemical methods which require multiple chemical reactions and the use of chemicals that are both expensive and environmentally harmful. Class II Nucleoside Deoxyribosyltransferases exhibit multiple characteristics that make them suitable as biocatalysts for the synthesis of natural and nonnatural nucleosides. They are specific for 2′-deoxyribonucleosides, regioselective (N-1 glycosylation in pyrimidine and N-9 in purine), and stereoselective (forming only β-anomers).
Class II N-Deoxyribosyltranferases, DRTases, catalyze the transfer of a 2′-deoxyribosyl group between purines or pyrimidines. In the absence of an acceptor nucleobase, these enzymes display hydrolase activity, converting the nucleoside to its base and a deoxyribose. In lactobacilli species, Nucleoside Deoxyribosyltransferase enzymes are part of the nucleoside salvage pathway for DNA synthesis.
Class II N-Deoxyribosyltranferases, DRTases, catalyze the transfer of a 2′-deoxyribosyl group between purines or pyrimidines. In the absence of an acceptor nucleobase, these enzymes display hydrolase activity, converting the nucleoside to its base and a deoxyribose. In lactobacilli species, Nucleoside Deoxyribosyltransferase enzymes are part of the nucleoside salvage pathway for DNA synthesis.
Preparation Note
Produced using animal component-free materials.
Other Notes
One unit of enzyme produces 1 μM of hypoxanthine in 1 minute at 40°C, pH 6.0.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Pierre Alexandre Kaminski et al.
Nucleic acids symposium series (2004), (52)(52), 495-496 (2008-09-09)
Nucleoside 2'-deoxyribosyltransferase (NDT) is used to synthesize unnatural 2'-deoxyribonucleosides, modified mostly on the heterocyclic base. Here we describe a strategy for improving 2,3-dideoxyribosyl(ddR) transfer activity of NDT by combining mutagenesis and in vivo selection in E. coli.
Yukiko Miyamoto et al.
Biochimica et biophysica acta, 1774(10), 1323-1330 (2007-09-21)
A nucleoside N-deoxyribosyltransferase-homologous gene was detected by homological search in the genomic DNA of Lactococcus lactis subsp. lactis. The gene yejD is composed of 477 nucleotides encoding 159 amino acids with only 25% identity, which is low in comparison to
Jesús Fernández-Lucas et al.
Applied microbiology and biotechnology, 91(2), 317-327 (2011-04-09)
Covalent attachment of recombinant Lactobacillus reuteri 2'-deoxyribosyltransferase to Sepabeads EC-EP303 leads to the immobilized biocatalyst SLrNDT4, which displayed an enzymatic activity of 65.4 IU/g of wet biocatalyst in 2'-deoxyadenosine synthesis from 2'-deoxyuridine and adenine at 40°C and pH 6.5. Response surface methodology
Jesús Fernández-Lucas et al.
Bioresource technology, 115, 63-69 (2011-12-27)
The effect of several water-miscible cosolvents on activity and stability of soluble and immobilized 2'-deoxyribosyltransferase from Lactobacillus reuteri on Sepabeads® has been studied in order to establish optimal conditions for enzymatic synthesis of nucleosides using purine bases with low solubility
R L Walter et al.
Structure (London, England : 1993), 3(8), 835-844 (1995-08-15)
Synchrotron radiation sources have made impressive contributions to macromolecular crystallography. The delay in development of appropriate X-ray detectors has, however, been a significant limitation to their efficient use. New technologies, based on charge-coupled devices (CCDs), provide capabilities for faster, more
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