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Updated: May 5, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
Published on: May 30, 2025
The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life
Joris Beld1, Eva C Sonnenschein, Christopher R Vickery
1Department of Chemistry and Biochemistry, University of California-San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358, USA. mburkart@ucsd.edu.
Abstract:
Covering: up to 2013. Although holo-acyl carrier protein synthase, AcpS, a phosphopantetheinyl transferase (PPTase), was characterized in the 1960s, it was not until the publication of the landmark paper by Lambalot et al. in 1996 that PPTases garnered wide-spread attention being classified as a distinct enzyme superfamily. In the past two decades an increasing number of papers have been published on PPTases ranging from identification, characterization, structure determination, mutagenesis, inhibition, and engineering in synthetic biology. In this review, we comprehensively discuss all current knowledge on this class of enzymes that post-translationally install a 4'-phosphopantetheine arm on various carrier proteins.
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