06/01/2009
DOE Synchrotron Light Sources Reveal Structure of Key Enzyme in Metabolism of Carbohydrates
Summary
Acetoacetate decarboxylase is used by bacteria for a critical step in the conversion of starches to alcohols and acetone, a key step in biofuels production. Now the structure of the enzyme in three dimensions has been solved, allowing scientists to understand the mechanism by which the conversion takes place. This, in turn, will help development of improved enzyme variants through protein engineering, including enzymes that could be used in the production of biofuels. The studies were carried out by a research group based at Boston University using x-ray crystallography stations at the National Synchrotron Light Source and a small angle x-ray scattering station at the Stanford Synchrotron Radiation Lights Source.
References
Meng-Chiao Ho, Jean-François Ménétret, Hiro Tsuruta and Karen N. Allen, “The origin of the electrostatic perturbation in Acetoacetate decarboxylase,” Nature, 459, 393-397 (21 May 2009)