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Acetoacetate decarboxylase: hydrophobics, not electrostatics

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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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