News and Views
Nature Chemical Biology 5, 454 - 455 (2009)
doi:10.1038/nchembio0709-454
Acetoacetate decarboxylase: hydrophobics, not electrostatics
John A Gerlt1
-
John A. Gerlt is in the Departments of Biochemistry and Chemistry, University of Illinois, Urbana-Champaign, Urbana, Illinois, USA.
e-mail: j-gerlt@uiuc.edu
Abstract
Westheimer's classical proposal that the decreased pKa of Lys115 in the active site of acetoacetate decarboxylase is the result of its unfavorable electrostatic juxtaposition with Lys116 has been evaluated by X-ray crystallography. The long-awaited structure reveals that Lys115 is positioned in a hydrophobic pocket that lowers its pKa.
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
RESEARCH
The origin of the electrostatic perturbation in acetoacetate decarboxylaseNature Article (21 May 2009)
