Acetoacetate decarboxylase: Hydrophobics, not electrostatics

Research output: Contribution to journalShort survey

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.

Original languageEnglish (US)
Pages (from-to)454-455
Number of pages2
JournalNature chemical biology
Volume5
Issue number7
DOIs
StatePublished - Jul 2009

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acetoacetate decarboxylase
X Ray Crystallography
Static Electricity
Catalytic Domain

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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Acetoacetate decarboxylase : Hydrophobics, not electrostatics. / Gerlt, John Alan.

In: Nature chemical biology, Vol. 5, No. 7, 07.2009, p. 454-455.

Research output: Contribution to journalShort survey

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