| pubmed-article:10360753 | pubmed:abstractText | Phosphorylated histidine residues occur in a number of signal-transduction pathways in bacteria as well as in eukaryotes. Phosphohistidine is hydrolytically labile and therefore difficult to study, this by contrast to stable phosphoserine, phosphothreonine or phosphotyrosine. Here we report the design and enantioselective synthesis of (4'-phospho-2'-furyl)alanine 1, a non-hydrolyzable analog of 1-phosphohistidine. This novel amino-acid should be useful to synthesize peptides incorporating a stable analog phosphohistidine. | lld:pubmed |
