Issue 8, 2010

Mechanism-based crosslinking as a gauge for functional interaction of modular synthases

Abstract

Protein-protein interactions between domains within fatty acid and polyketide synthases are critical to catalysis, but their contributions remain incompletely characterized. A practical, quantitative system for establishing functional interactions between modifying enzymes and the acyl carrier protein that tethers the nascent polymer would offer a valuable tool for understanding and engineering these enzyme systems. Mechanism-based crosslinking of modular domains offers a potential diagnostic to highlight selective interactions between modular pairs. Here kinetic activity analysis and isothermal titration calorimetry are shown to correlate the efficiency of a ketosynthase-carrier protein crosslinking method to the binding affinity and transacylase activity that occurs in ketosynthase chain elongation.

Graphical abstract: Mechanism-based crosslinking as a gauge for functional interaction of modular synthases

Supplementary files

Article information

Article type
Communication
Submitted
09 Dec 2009
Accepted
09 Feb 2010
First published
17 Feb 2010

Org. Biomol. Chem., 2010,8, 1769-1772

Mechanism-based crosslinking as a gauge for functional interaction of modular synthases

A. S. Worthington, D. F. Porter and M. D. Burkart, Org. Biomol. Chem., 2010, 8, 1769 DOI: 10.1039/B925966J

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