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Journal article

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

From

University of California at San Diego1

Department of Systems Biology, Technical University of Denmark2

Bacterial Ecophysiology and Biotechnology, Department of Systems Biology, Technical University of Denmark3

Salk Institute for Biological Studies4

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.

Language: English
Publisher: The Royal Society of Chemistry
Year: 2013
Pages: 61-108
ISSN: 14604752 and 02650568
Types: Journal article
DOI: 10.1039/c3np70054b
ORCIDs: Sonnenschein, Eva

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