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Issue 8, 2010
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Mechanism-based crosslinking as a gauge for functional interaction of modular synthases

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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

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Publication details

The article was received on 09 Dec 2009, accepted on 09 Feb 2010 and first published on 17 Feb 2010


Article type: Communication
DOI: 10.1039/B925966J
Citation: Org. Biomol. Chem., 2010,8, 1769-1772
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    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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