Researchers discover how tooth decay enzyme functions

Researchers from the U.K. and Japan used the Diamond Light Source synchrotron in Oxfordshire and the Photon Factory synchotron in Tsukuba, Japan, to solve the 3D structure of an enzyme that plays a key role in tooth decay caused by sugar (Journal of Molecular Biology, April 29, 2011, Vol. 408:2, pp. 177-186).

Noting that glucansucrase (GSase) from Streptococcus mutans is an essential agent in dental caries pathogenesis, the researchers examined the crystal structure of S. mutans glycosyltransferase (GTF-SI), which synthesizes soluble and insoluble glucans. The structural information derived from this research provides critical insight into how GTF-SI forms glucan and should be extremely useful in the design of novel inhibitors that prevent the biofilm formation by GTF-SI, the study authors noted.

"With the use of the Diamond synchrotron and the Photon Factory, we have been able to solve not only the structure of the enzyme alone but also its structure when bound to an existing inhibitor," said Sohei Ito, PhD, lead researcher on the project, in a press release.

Several inhibitors that prevent this type of enzyme forming glucan have been identified, but to date there has been little structural information available, Ito added.

"With the data we collected at Diamond and the Photon Factory, we now have a better understanding of how the enzyme functions and how it can be stopped," he said. "This structural information should be useful in the design of novel inhibitors that will prevent the biofilm formation by glucansucrases and reduce the risk of possible side effects such as hypoglycemia."

These novel inhibitors could be incorporated into toothpaste and mouthwash, making them more effective at preventing tooth decay, Ito added.

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