| Literature DB >> 24818001 |
Michael Rothmann1, Nicolas M Kosa1, Michael D Burkart1.
Abstract
The post-translational modifying enzymes phophopantetheinyl transferase and acyl carrier protein hydrolase have shown utility in the functional modification of acyl carrier proteins. Here we develop these tools as immobilized biocatalysts on agarose supports. New utility is imparted through these methods, enabling rapid and label-independent protein purification. Immobilization of acyl carrier protein is also demonstrated for rapid activity assays of these 4'-phosophopantetheine modifying enzymes, displaying a particular advantage in the case of phosphopantetheine removal, where few orthogonal techniques have been demonstrated. These tools further enrich the suite of functional utility of 4'-phosophopantetheine chemistry, with applications to protein functionalization, materials, and natural product biosynthetic studies.Entities:
Year: 2014 PMID: 24818001 PMCID: PMC4012645 DOI: 10.1039/C3RA47847E
Source DB: PubMed Journal: RSC Adv ISSN: 2046-2069 Impact factor: 3.361