Focus on phosphohistidine

@article{Attwood2006FocusOP,
  title={Focus on phosphohistidine},
  author={Paul V. Attwood and Matthew J. Piggott and Xin Lin Zu and Paul G. Besant},
  journal={Amino Acids},
  year={2006},
  volume={32},
  pages={145-156}
}
Summary.Phosphohistidine has been identified as an enzymic intermediate in numerous biochemical reactions and plays a functional role in many regulatory pathways. Unlike the phosphoester bond of its cousins (phosphoserine, phosphothreonine and phosphotyrosine), the phosphoramidate (P–N) bond of phosphohistidine has a high ΔG° of hydrolysis and is unstable under acidic conditions. This acid-lability has meant that the study of protein histidine phosphorylation and the associated protein kinases… 
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TLDR
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Histidine phosphorylation in metalloprotein binding sites.
P-N bond protein phosphatases.
  • P. Attwood
  • Biology
    Biochimica et biophysica acta
  • 2013
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TLDR
By replacing the phosphate linked to the histidine residue with a thiophosphate, a phosphohistidine derivative with increased stability is formed, which allows the analysis of phosphohistsidine‐containing proteins by established biochemical techniques and will greatly aid in the investigation of the role of this posttranslational modification in cellular processes.
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TLDR
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TLDR
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TLDR
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