「Biophysics and Physicobiology」に Wataru Tanaka et al. “Molecular mechanisms of substrate specificities of uridine-cytidine kinase”を掲載

2016 June 08 BPPB

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Wataru Tanaka, Mitsuo Shoji, Fumiaki Tomoike,Yuzuru Ujiie, Kyohei Hanaoka, Ryuhei Harada, Megumi Kayanuma,Katsumasa Kamiya, Toyokazu Ishida, Ryoji Masui, Seiki Kuramitsu, Yasuteru Shigeta 
“Molecular mechanisms of substrate specificities of uridine-cytidine kinase”

Important role of hydrogen-bonding interactions with the substrates in the substrate specificity of uridine-cytidine kinase

By using the molecular dynamics (MD) simulations, we revealed that the substrate bindings of uridine-cytidine kinase (UCK) are mainly performed by the three amino acids, i.e. Tyr88, Tyr/His/Gln93 and Arg152 in UCK from Thermus thermophilus HB8 (ttCK). The formations of the hydrogen bonding interactions between the substrates and the three amino acid residues clearly demonstrated the UCK substrate specificity. It was also shown that the substrate uridine is deprotonated when it binds to UCK.

Biophysics and Physicobiology, Vol.13, pp. 77-84


Back to previous page