Acetoacetate decarboxylase: hydrophobics, not electrostatics

被引：4

作者：

Gerlt, John A. ^{[1
,2
]}

机构：

[1] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

[2] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

来源：

NATURE CHEMICAL BIOLOGY | 2009年 / 5卷 / 07期

关键词：

ACTIVE SITE; IONIZATION CONSTANT; REPORTER GROUP; AMINO GROUP;

D O I：

10.1038/nchembio0709-454

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Westheimer's classical proposal that the decreased pK(a) 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 pK(a).

引用

页码：454 / 455

页数：2

共 6 条

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