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

Joris Beld, Eva Sonnenschein, Christopher R. Vickery, Joseph P. Noel, Michael D. Burkart

    Research output: Contribution to journalJournal articleResearchpeer-review

    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.
    Original languageEnglish
    JournalNatural Product Reports
    Volume31
    Issue number1
    Pages (from-to)61-108
    ISSN0265-0568
    DOIs
    Publication statusPublished - 2013

    Cite this

    Beld, Joris ; Sonnenschein, Eva ; Vickery, Christopher R. ; Noel, Joseph P. ; Burkart, Michael D. / The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life. In: Natural Product Reports. 2013 ; Vol. 31, No. 1. pp. 61-108.
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    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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    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 journalJournal articleResearchpeer-review

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    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

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    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.

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