Focus on phosphoaspartate and phosphoglutamate
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Protein phosphorylation is a common signalling mechanism in both prokaryotic and eukaryotic organisms. Whilst the focus of protein phosphorylation research has primarily been on protein serine/threonine or tyrosine phosphorylation, there are other phosphoamino acids that are also biologically important. Two of the phosphoamino acids that are functionally involved in the biochemistry of protein phosphorylation and signalling pathways are phosphoaspartate and phosphoglutamate, and this review focuses on their chemistry and biochemistry. In particular, we cover the biological aspects of phosphoaspartate and phosphoglutamate in signalling pathways and as phosphoenzyme intermediates. In addition, we examine the synthesis of both of these phosphoamino acids and the chemistry of the acyl phosphate group. Although phosphoaspartate is a major component of prokaryotic two-component signalling pathways, this review casts its net wider to include reports of phosphoaspartate in eukaryotic cells. Reports of phosphoglutamate, although limited, appear to be more common as free phosphoglutamate than those found in phosphoprotein form.
KeywordsPhosphoaspartate Phosphoglutamate Phosphoanhydride Acyl phosphate Response regulator
- Baxter NJ, Bowler MW et al (2010) Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF3− rather than by phosphoranes. Proc Natl Acad Sci USA 107:4555–4560, S4555/1–S4555/6Google Scholar
- Farkas E, Brown DA et al (1993) Metal complexes of glutamic acid-gamma-hydroxamic acid (Glu-gamma-ha) (N-hydroxyglutamine) in aqueous solution. J Chem Soc Dalton Trans: Inorg Chem (1972–1999)18:2803–2807Google Scholar
- Farkas E, Buglyo P (1990) Complex formation between transition metals and dl-aspartic acid-beta-hydroxamic acid (N-hydroxyasparagine) J Chem Soc Dalton Trans: Inorg Chem (1972–1999)5:1549–1551Google Scholar
- Wurmser R (1967) Biochemical energetics. II. Experimental determination of free energies. 3:28–35Google Scholar