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N2665

Sigma-Aldrich

Nucleoside Deoxyribosyltransferase II from Lactobacillus leichmanii

lyophilized powder, recombinant, expressed in E. coli

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Synonym(s):
Nucleoside Deoxyribosyltransferase II from Lactobacillus leichmanii, DRTase, Deoxyribose transferase, NDT, nucleoside:purine(pyrimidine) deoxy-D-ribosyltransferase
Enzyme Commission number:
UNSPSC Code:
12352204
NACRES:
NA.54

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.

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.

Suitability

Suitable for the enzymatic nucleoside synthesis.

Unit Definition

One unit of enzyme produces 1 μM of hypoxanthine in 1 minute at 40°C, pH 6.0.

Preparation Note

Produced using animal component-free materials.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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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
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
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
Yin Lin et al.
FEMS microbiology letters, 323(2), 132-141 (2011-11-19)
N-deoxyribosyltransferases are essential enzymes in the nucleotide salvage pathway of lactobacilli. They catalyze the exchange between the purine or pyrimidine bases of 2'-deoxyribonucleosides and free pyrimidine or purine bases. In general, N-deoxyribosyltransferases are referred to as cytoplasmic enzymes, although there
D J Porter et al.
The Journal of biological chemistry, 270(26), 15557-15562 (1995-06-30)
Nucleoside 2-deoxyribosyltransferase catalyzes cleavage of a 2'-deoxyribosylnucleoside (A) to a nucleobase (P) with deoxyribosylation of the enzyme. Substrates quenched the intrinsic fluorescence of native enzyme (E) and a catalytically inactive mutant enzyme (E98A enzyme). The time courses of these reactions

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