Karen Allen research reported in Nature
Karen Allen research reported in Nature solves how the enzyme acetoacetate decarboxylase (AADase) works in cell environment
Professor Karen Allen, an internationally renown crystallographer in the Department of Chemistry and her colleagues, BU graduate student Meng-Chiao Ho and post-doctoral associate Jean-Francois Menetret, and Hiro Tsuruta of the Stanford Synchrotron Radiation Lightsource of the National Accelerator Laboratory, have published a paper in Nature (on-line May 21) entitled “The origin of the electrostatic perturbation in acetoacetate decarboxylase.”
Using X-ray crystallography, their research reveals the structural underpinnings of a widely-known enzyme — acetoacetate decarboxylase (AADase) — that was first described correctly more than 43 years ago, including how it accelerates its target reaction. Until this paper, however, there has never been a full explanation of how the reactions occur in the environment of the cell. This breakthrough insight will have broad ranging implications from medicine to the protein engineering of new environmentally friendly “green” biofuels. The research reported on in Nature is also featured in Nature Chemical Biology New&Views, C&EN News, and Chemistry World.
The AADase tertiary structure depicted as a ribbon diagram ramped from blue to red (N terminus to C terminus). The catalytic Lys115 (shown as ball and stick) lies at the bottom of a 26.8Å deep funnel formed by the central, cone-shaped seven-stranded b-sheet that is a dominant feature of the fold.
(Source: K Allen)
May 2009
For the BU Press release on the paper by Ron Rosenberg, click here.