Beld, Joris3; Sonnenschein, Eva4; Vickery, Christopher R.3; Noel, Joseph P.5; Burkart, Michael D.3
1 Department of Systems Biology, Technical University of Denmark2 Bacterial Ecophysiology and Biotechnology, Department of Systems Biology, Technical University of Denmark3 University of California4 Bacterial Ecophysiology and Biotechnology, Department of Biotechnology and Biomedicine, Technical University of Denmark5 The Salk Institute for Biological Studies, Jack H. Skirball Center for Chemical Biology and Proteomics
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.
Natural Product Reports, 2013, Vol 31, Issue 1, p. 61-108