[5-TAMRA]-LPETGG N-terminal Sortagging – Fluorescent Peptides

This peptide is recognised and cleaved by the enzyme Sortase A (SrtA) from-Staphylococcus aureus. The catalytic cysteine residue in the active site of SrtA serves as a nucleophile to cleave the peptide bond between threonine and glycine. Cleavage results in the formation of a thioacyl intermediate between the peptide and SrtA. This intermediate is then resolved by the N-terminus of an (oligo)glycine nucleophile, resulting in the creation of a new peptide bond that links the peptide and its fluorescent dye to the incoming nucleophile. This method of protein labelling is known as sortagging. 5-Carboxytetramethylrhodamine (5-TAMRA) is a widely used fluorescent dye which excites at 546 nm and emits at 579 nm.

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