Issue 3, 2014

Chemoenzymatic exchange of phosphopantetheine on protein and peptide

Abstract

Evaluation of new acyl carrier protein hydrolase (AcpH, EC 3.1.4.14) homologs from proteobacteria and cyanobacteria reveals significant variation in substrate selectivity and kinetic parameters for phosphopantetheine hydrolysis from carrier proteins. Evaluation with carrier proteins from both primary and secondary metabolic pathways reveals an overall preference for acyl carrier protein (ACP) substrates from type II fatty acid synthases, as well as variable activity for polyketide synthase ACPs and peptidyl carrier proteins (PCP) from non-ribosomal peptide synthases. We also demonstrate the kinetic parameters of these homologs for AcpP and the 11-mer peptide substrate YbbR. These findings enable the fully reversible labeling of all three classes of natural product synthase carrier proteins as well as full and minimal fusion protein constructs.

Graphical abstract: Chemoenzymatic exchange of phosphopantetheine on protein and peptide

Supplementary files

Article information

Article type
Edge Article
Submitted
15 Nov 2013
Accepted
24 Dec 2013
First published
02 Jan 2014

Chem. Sci., 2014,5, 1179-1186

Author version available

Chemoenzymatic exchange of phosphopantetheine on protein and peptide

N. M. Kosa, K. M. Pham and M. D. Burkart, Chem. Sci., 2014, 5, 1179 DOI: 10.1039/C3SC53154F

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