Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme

被引：33
|
作者：
Bera, Asim K.
Polovnikova, Lena S.
Roestamadji, Juliatek
Widlanski, Theodore S.
Kenyon, George L.
McLeish, Michael J. [1 ]
Hasson, Miriam S.
机构：
[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
[2] Indiana Univ, Dept Chem, Bloomington, IN 47405 USA
[3] Univ Michigan, Coll Pharm, Ann Arbor, MI 48109 USA
来源：
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2007年 / 129卷 / 14期
关键词：
D O I：
10.1021/ja068636z
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Benzoylformate decarboxylase (BFD) from Pseudomonas putida is a thiamin diphosphate-dependent enzyme that catalyzes the non-oxidative decarboxylation of benzoylformate. Here we report the discovery of a mechanism-based inhibitor of BFD that is unusual in that it covalently modifies the enzyme via active site phosphorylation. Incubation of BFD with benzoylphosphonate results in time- and concentration-dependent inactivation of the enzyme. X-ray crystallography reveals that the inactivation is due to the phosphorylation of an active site serine residue.
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收藏
页码：4120 / +
页数：3
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