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Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase.

Analytical biochemistry (2009-03-31)
Feng Rao, Swathi Pasunooti, Yinglu Ng, Weichao Zhuo, Lishi Lim, Angeline Weixian Liu, Zhao-Xun Liang

The cyclic dinucleotide c-di-GMP is a widespread bacterial messenger molecule with potential application as a therapeutic agent for treating bacterial infection. Current enzymatic synthesis of c-di-GMP using mesophilic diguanylate cyclase (DGC) proteins suffers from low production yield due to protein instability and strong product inhibition. Here we report the overexpression and characterization of a stand-alone thermophilic diguanylate cyclase domain (tDGC) protein with enhanced thermostability. The product inhibition that severely limited production yield was significantly alleviated by mutation of a conserved residue in the putative regulatory I-site. With the mutant tDGC, we demonstrated that hundreds of milligrams of c-di-GMP can be readily prepared by using the optimized procedures for enzymatic reaction and product purification. The thermophilic enzyme will be a valuable tool for other research laboratories for c-di-GMP synthesis as well as the preparation of c-di-GMP derivatives.

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Product Description

Guanosine 5′-triphosphate sodium salt hydrate, ≥95% (HPLC), powder

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