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Acetoacetate decarboxylase: hydrophobics, not electrostatics

Nature Chemical Biology volume 5, pages 454–455 (2009)Cite this article

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.

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Figure 1: Interactions in the active site of AAD.

References

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  1. John A. Gerlt is in the Departments of Biochemistry and Chemistry, University of Illinois, Urbana-Champaign, Urbana, Illinois, USA. j-gerlt@uiuc.edu,

    John A Gerlt

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  1. John A Gerlt
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Gerlt, J. Acetoacetate decarboxylase: hydrophobics, not electrostatics. Nat Chem Biol 5, 454–455 (2009). https://doi.org/10.1038/nchembio0709-454

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