A model of the transition state in the alkaline phosphatase reaction

被引：153

作者：

Holtz, KM ^{[1
]}

Stec, B ^{[1
]}

Kantrowitz, ER ^{[1
]}

机构：

[1] Boston Coll, Dept Chem, Merkert Chem Ctr, Chestnut Hill, MA 02167 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1999年 / 274卷 / 13期

关键词：

D O I：

10.1074/jbc.274.13.8351

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：

A high resolution crystal structure of Escherichia coli alkaline phosphatase in the presence of vanadate has been refined to 1.9 Angstrom resolution. The vanadate ion takes on a trigonal bipyramidal geometry and is covalently bound by the active site serine nucleophile. A coordinated water molecule occupies the axial position opposite the serine nucleophile, whereas the equatorial oxygen atoms of the vanadate ion are stabilized by interactions with both Arg-166 and the zinc metal ions of the active site. This structural complex supports the in-line displacement mechanism of phosphomonoester hydrolysis by alkaline phosphatase and provides a model for the proposed transition state in the enzyme-catalyzed reaction.

引用

页码：8351 / 8354

页数：4

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