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
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
收藏
页码:1111 / 1113
页数:3
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