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Journal article
The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life
Natural product reports, v 31(1), pp 61-108
01 Jan 2014
PMID: 24292120
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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 at. 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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Details
- Title
- The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life
- Creators
- Joris Beld - University of California SystemEva C. Sonnenschein - University of California, San DiegoChristopher R. Vickery - University of California SystemJoseph P. Noel - Salk Institute for Biological StudiesMichael D. Burkart - University of California System
- Publication Details
- Natural product reports, v 31(1), pp 61-108
- Publisher
- Royal Soc Chemistry
- Number of pages
- 48
- Grant note
- CILMSF 500-10-039 / California Energy Commission EEC-0813570; MCB-0645794 / National Science Foundation; National Science Foundation (NSF) R01GM095970 / NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS) R01GM094924; R01GM095970 / NIH; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA Howard Hughes Medical Institute DE-EE0003373 / DOE; United States Department of Energy (DOE)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:000329887500004
- Scopus ID
- 2-s2.0-84890057926
- Other Identifier
- 991020535057304721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Chemistry, Medicinal
- Chemistry, Organic