The structure of human phosphoglucose isomerase complexed with a transition-state analogue

被引：27

作者：

Davies, C ^{[1
]}

Muirhead, H

Chirgwin, J

机构：

[1] Med Univ S Carolina, Dept Biochem & Mol Biol, Charleston, SC 29425 USA

[2] Univ Bristol, Sch Med Sci, Bristol BS8 1TD, Avon, England

[3] Univ Virginia, Dept Med, Charlottesville, VA 22908 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷

关键词：

D O I：

10.1107/S0907444903007352

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Phosphoglucose isomerase (PGI) is a workhorse enzyme of carbohydrate metabolism that interconverts glucose 6-phosphate and fructose 6-phosphate. Outside the cell, however, the protein appears to function as a cytokine. A crystal structure of human PGI bound with 5-phosphoarabinonate, a strong inhibitor that mimics the cis-enediol(ate) intermediate of the reaction, has been determined at 2.5 Angstrom resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction.

引用

页码：1111 / 1113

页数：3

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