Abstract
| Original language | English |
|---|---|
| Journal | Natural Product Reports |
| Volume | 31 |
| Issue number | 1 |
| Pages (from-to) | 61-108 |
| ISSN | 0265-0568 |
| DOIs | |
| Publication status | Published - 2013 |
Cite this
}
The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life. / Beld, Joris; Sonnenschein, Eva; Vickery, Christopher R.; Noel, Joseph P.; Burkart, Michael D.
In: Natural Product Reports, Vol. 31, No. 1, 2013, p. 61-108.Research output: Contribution to journal › Journal article › Research › peer-review
TY - JOUR
T1 - The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life
AU - Beld, Joris
AU - Sonnenschein, Eva
AU - Vickery, Christopher R.
AU - Noel, Joseph P.
AU - Burkart, Michael D.
PY - 2013
Y1 - 2013
N2 - 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.
AB - 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.
U2 - 10.1039/c3np70054b
DO - 10.1039/c3np70054b
M3 - Journal article
VL - 31
SP - 61
EP - 108
JO - Natural Product Reports
JF - Natural Product Reports
SN - 0265-0568
IS - 1
ER -