Literature DB >> 20859643

Focus on phosphoaspartate and phosphoglutamate.

P V Attwood1, P G Besant, Matthew J Piggott.   

Abstract

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.

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Year:  2010        PMID: 20859643     DOI: 10.1007/s00726-010-0738-5

Source DB:  PubMed          Journal:  Amino Acids        ISSN: 0939-4451            Impact factor:   3.520


  15 in total

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7.  Use of restrained molecular dynamics to predict the conformations of phosphorylated receiver domains in two-component signaling systems.

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9.  A pan-specific antibody for direct detection of protein histidine phosphorylation.

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Journal:  Nat Chem Biol       Date:  2013-05-26       Impact factor: 15.040

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