title: Selective functionalization of the protein N terminus with N-myristoyl transferase for bioconjugation in cell lysate.
abstract: A site to behold: Robust site-specific functionalization of engineered proteins is achieved with N-myristoyl transferase (NMT) in bacterial cells. NMT tolerates non-natural substrate proteins as well as reactive fatty acid tags, rendering it a powerful tool for protein conjugation applications, including the construction of protein microarrays from lysate.
authors.affiliation: Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125 (USA) http://tirrell-lab.caltech.edu.
authors.forename: Chethana
authors.initials: C
authors.lastname: Kulkarni
authors.forename: Tamara L
authors.initials: TL
authors.lastname: Kinzer-Ursem
authors.forename: David A
authors.initials: DA
authors.lastname: Tirrell
mesh_terms: D000217:Acyltransferases / Q000378:metabolism*; D000480:Alkynes / Q000737:chemistry; D001386:Azides / Q000737:chemistry; D016923:Cell Death; D004926:Escherichia coli / Q000166:cytology / Q000201:enzymology; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*
chemical_list: D000480:Alkynes; D001386:Azides; D000217:Acyltransferases; C050480:glycylpeptide N-tetradecanoyltransferase
keywords: N-myristoyl transferase; chemoenzymatic; click chemistry; microarrays; protein engineering