U.S. Department of Energy Office of Biological and Environmental Research

BER Research Highlights


DOE Synchrotron Light Sources Reveal Structure of Key Enzyme in Metabolism of Carbohydrates
Published: June 01, 2009
Posted: June 08, 2009

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. 

Reference: 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)

Contact: Roland F. Hirsch, SC-23.2, (301) 903-9009
Topic Areas:

  • Research Area: Microbes and Communities
  • Research Area: Sustainable Biofuels and Bioproducts
  • Research Area: Biosystems Design
  • Research Area: Structural Biology, Biomolecular Characterization and Imaging
  • Research Area: Structural Biology Infrastructure

Division: SC-23.2 Biological Systems Science Division, BER

 

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