A purine nucleoside phosphorylase from the alkaliphile Bacillus halodurans Alk36 has been cloned and over expressed in E. coli. The purified enzyme had a kcat of 2.03 x 10-9 s-1 and a km of 206 µM on guanosine. The optimal pH range was between 5.7 and 8.4, with an optimal temperature of 70ºC and a half life at 60ºC of 20.8 hours.
Reference:
Visser, DF, et al. 2010. Cloning, purification and characterisation of a recombinant purine nucleoside phosphorylase from Bacillus halodurans Alk36 . Extremophiles, Vol. 14(2), pp 185-192
Visser, D. F., Hennessy, F., Rashamuse, K., Louw, M., & Brady, D. (2010). Cloning, purification and characterisation of a recombinant purine nucleoside phosphorylase from Bacillus halodurans Alk36. http://hdl.handle.net/10204/4349
Visser, Daniel F, F Hennessy, KJ Rashamuse, ME Louw, and D Brady "Cloning, purification and characterisation of a recombinant purine nucleoside phosphorylase from Bacillus halodurans Alk36." (2010) http://hdl.handle.net/10204/4349
Visser DF, Hennessy F, Rashamuse K, Louw M, Brady D. Cloning, purification and characterisation of a recombinant purine nucleoside phosphorylase from Bacillus halodurans Alk36. 2010; http://hdl.handle.net/10204/4349.
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