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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页码：4120 / +

页数：3

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