Kinase and synthetase enzymes utilise C8D-ATP in preference to non-deuterated ATP. The KIE obtained at low ATP concentrations is clearly a primary KIE demonstrating strong evidence that the bond to the isotopically substituted hydrogen is being broken. The effect of the ATP concentration profile on the KIE was used to develop a model whereby the C8H of ATP plays a role in the overall regulation of phosphoryl transfer. This role of the C8H of ATP in the regulation appears to have been conserved in all kinase and synthetase enzymes as one of the mechanisms associated with binding of ATP. The induction of the C8H to be labile by active site residues coordinated to the ATP purine ring may play a significant role in explaining the broad range of Km associated with kinase enzymes.
Reference:
Kenyon, CP, Steyn, A, Roth, RL, Steenkamp, PA, Nkosi, TC and Oldfield, LC. 2011. The role of the C8 proton of ATP in the regulation of phosphoryl transfer within kinases and synthetases. BMC Biochemistry, vol. 12(36), DOI:10.1186/1471-2091-12-36
Kenyon, C., Steyn, A., Roth, R. L., Steenkamp, P., Nkosi, T., & Oldfield, L. (2011). The role of the C8 proton of ATP in the regulation of phosphoryl transfer within kinases and synthetases. http://hdl.handle.net/10204/5985
Kenyon, CP, A Steyn, Robyn L Roth, PA Steenkamp, TC Nkosi, and LC Oldfield "The role of the C8 proton of ATP in the regulation of phosphoryl transfer within kinases and synthetases." (2011) http://hdl.handle.net/10204/5985
Kenyon C, Steyn A, Roth RL, Steenkamp P, Nkosi T, Oldfield L. The role of the C8 proton of ATP in the regulation of phosphoryl transfer within kinases and synthetases. 2011; http://hdl.handle.net/10204/5985.
Copyright: 2011 Kenyon et al. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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