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Please use this identifier to cite or link to this item: http://hdl.handle.net/10204/4384

Title: High yielding cascade enzymatic synthesis of 5-methyluridine using a novel Purine Nucleoside Phosphorylase, from Bacillus halodurans Alk36
Authors: Vissser, D
Hennessy, F
Rashamuse, K
Van Zyl, P
Gordon, G
Mathiba, K
Bode, M
Pletschke, B
Brady, D
Keywords: 5-Methyluridine
Biocatalysis
Purine nucleoside phosphorylas
Highly active anti-retroviral treatment
HAART
Bacillus halodurans Alk36
HIV
AIDS
Issue Date: Sep-2010
Publisher: biocat2010
Citation: Vissser, D, Hennessy, F, Rashamuse, K et al. 2010. High yielding cascade enzymatic synthesis of 5-methyluridine using a novel Purine Nucleoside Phosphorylase, from Bacillus halodurans Alk36. 5th International Congress on Biocatalysis, Hamburg University of Technology, Germany, August 29-September 2, 2010, pp 1
Abstract: 5-Methyluridine(5-MU) is a non-natural nucleoside that can be used as an intermediate in the synthesis of thymidine, and in the synthesis of nucleoside analogues AZT and stavudine, both of which are used in Highly Active Anti-Retroviral Treatment (HAART) of HIV/AIDS patients. 5-MU can be synthesised through the transglycosylation of D-ribose-1-phosphate, using guanosine as a donor, and thymine as receptor. However,the reagents guanosine and thymine are relatively insoluble, resulting in particulate substrates with poor reaction kinetics, and the most effective method of solubilising these materials is in hot aqueous solutions. It would therefore be preferable to utilize thermostable enzymes. The present work investigated the purine nucleoside phosphorylase (BHPNP1) present in the moderately thermophilic and alkaliphilic organism, Bacillus halodurans Alk361,2. The authors report on the combination of that enzyme with the uridine phosphorylase from E.coli in a one-pot cascade reaction to produce 5-methyl uridine in high yield.
Description: 5th International Congress on Biocatalysis, Hamburg University of Technology, Germany, August 29-September 2, 2010
URI: http://hdl.handle.net/10204/4384
Appears in Collections:Enzyme technologies
General science, engineering & technology

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