The kinome is made up of a large number of functionally diverse enzymes, with the classification indicating very little about the extent of the conserved kinetic mechanisms associated with phosphoryl transfer. It has been demonstrated that C8-H of ATP plays a critical role in the activity of a range of kinase and synthetase enzymes.
Reference:
Kenyon, CP, Roth, RL, Van der Westhuyzen, CW and Parkinson, CJ. 2012. Conserved phosphoryl transfer mechanisms within kinase families and the role of the C8 proton of ATP in the activation of phosphoryl transfer. BMC Research Notes, vol. 5: 131
Kenyon, C., Roth, R. L., Van der Westhuyzen, C. W., & Parkinson, C. (2012). Conserved phosphoryl transfer mechanisms within kinase families and the role of the C8 proton of ATP in the activation of phosphoryl transfer. http://hdl.handle.net/10204/5900
Kenyon, CP, Robyn L Roth, Christiaan W Van der Westhuyzen, and CJ Parkinson "Conserved phosphoryl transfer mechanisms within kinase families and the role of the C8 proton of ATP in the activation of phosphoryl transfer." (2012) http://hdl.handle.net/10204/5900
Kenyon C, Roth RL, Van der Westhuyzen CW, Parkinson C. Conserved phosphoryl transfer mechanisms within kinase families and the role of the C8 proton of ATP in the activation of phosphoryl transfer. 2012; http://hdl.handle.net/10204/5900.
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