Not always an innocent bystander: the impact of stabilised phosphopantetheine moieties when studying nonribosomal peptide biosynthesis

Author:

Ho Y. T. Candace1234ORCID,Kaczmarski Joe A.56ORCID,Tailhades Julien123ORCID,Izoré Thierry12ORCID,Steer David L.17,Schittenhelm Ralf B.17,Tosin Manuela4ORCID,Jackson Colin J.3568,Cryle Max J.123ORCID

Affiliation:

1. Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia

2. EMBL Australia, Monash University, Clayton, VIC 3800, Australia

3. ARC Centre of Excellence for Innovations in Peptide and Protein Science, Australia

4. Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK

5. ARC Centre of Excellence in Synthetic Biology, Australian National University, Canberra, Australia

6. Research School of Biology, Australian National University, Acton, Australian Capital Territory, Australia

7. Monash Proteomics and Metabolomics Facility, Monash University, Clayton, VIC 3800, Australia

8. Research School of Chemistry, The Australian National University, Acton, ACT 2601, Australia

Abstract

Chemical stabilisation of carrier protein bound substrates in non-ribosomal peptide synthesis can result in a loss in activity of neighbouring catalytic domains.

Funder

Australian Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

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