Chemoenzymatic Transfer of Fluorescent Non‐natural Amino Acids to the N Terminus of a Protein/Peptide
Identifieur interne : 000200 ( Main/Exploration ); précédent : 000199; suivant : 000201Chemoenzymatic Transfer of Fluorescent Non‐natural Amino Acids to the N Terminus of a Protein/Peptide
Auteurs : Masumi Taki [États-Unis, Japon] ; Hiroyuki Kuroiwa ; Masahiko Sisido [Japon]Source :
- ChemBioChem [ 1439-4227 ] ; 2008-03-25.
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Abstract
Non‐natural fluorescence extension. Leucyl/phenylalanyl‐tRNA–protein transferase from E. coli catalyzes the transfer of hydrophobic amino acids from tRNA to the N terminus of proteins. Here, we have expanded this enzymatic reaction to allow attachment of large fluorescent amino acids to peptides and proteins. Furthermore, we minimized the tRNA structure to microhelices or even to pdCpA. Thus, we provide a novel method for N‐terminal specific fluorescence labeling of proteins as shown in the figure.
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DOI: 10.1002/cbic.200700721
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Leucyl/phenylalanyl‐tRNA–protein transferase from E. coli catalyzes the transfer of hydrophobic amino acids from tRNA to the N terminus of proteins. Here, we have expanded this enzymatic reaction to allow attachment of large fluorescent amino acids to peptides and proteins. Furthermore, we minimized the tRNA structure to microhelices or even to pdCpA. 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