Focus on phosphohistidine

Paul Attwood, Matthew Piggott, X.L. Zu, Paul Besant

Research output: Contribution to journalReview article

102 Citations (Scopus)

Abstract

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 Delta G degrees 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 has been slower to progress than other protein phosphorylation studies.Histidine phosphorylation is a crucial component of cell signalling in prokaryotes and lower eukaryotes. It is also now becoming widely reported in mammalian signalling pathways and implicated in certain human disease states. This review covers the chemistry of phosphohistidine in terms of its isomeric forms and chemical derivatives, how they can be synthesized, purified, identified and the relative stabilities of each of these forms. Furthermore, we highlight how this chemistry relates to the role of phosphohistidine in its various biological functions.
Original languageEnglish
Pages (from-to)145-156
JournalAmino Acids
Volume32
Issue number1
DOIs
Publication statusPublished - 2007

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Phosphorylation
Histidine
Phosphothreonine
Cell signaling
Phosphoserine
Phosphotyrosine
Cellular Structures
Eukaryota
Protein Kinases
Hydrolysis
Proteins
Derivatives
Acids
phosphohistidine

Cite this

Attwood, Paul ; Piggott, Matthew ; Zu, X.L. ; Besant, Paul. / Focus on phosphohistidine. In: Amino Acids. 2007 ; Vol. 32, No. 1. pp. 145-156.
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Focus on phosphohistidine. / Attwood, Paul; Piggott, Matthew; Zu, X.L.; Besant, Paul.

In: Amino Acids, Vol. 32, No. 1, 2007, p. 145-156.

Research output: Contribution to journalReview article

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T1 - Focus on phosphohistidine

AU - Attwood, Paul

AU - Piggott, Matthew

AU - Zu, X.L.

AU - Besant, Paul

PY - 2007

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AB - 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 Delta G degrees 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 has been slower to progress than other protein phosphorylation studies.Histidine phosphorylation is a crucial component of cell signalling in prokaryotes and lower eukaryotes. It is also now becoming widely reported in mammalian signalling pathways and implicated in certain human disease states. This review covers the chemistry of phosphohistidine in terms of its isomeric forms and chemical derivatives, how they can be synthesized, purified, identified and the relative stabilities of each of these forms. Furthermore, we highlight how this chemistry relates to the role of phosphohistidine in its various biological functions.

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