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与过渡态类似物复合的人磷酸葡萄糖异构酶的结构。

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

作者信息

Davies Christopher, Muirhead Hilary, Chirgwin John

机构信息

Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1111-3. doi: 10.1107/s0907444903007352. Epub 2003 May 23.

Abstract

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 A resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction.

摘要

磷酸葡萄糖异构酶(PGI)是碳水化合物代谢中的一种主力酶,可催化6-磷酸葡萄糖和6-磷酸果糖之间的相互转化。然而,在细胞外,该蛋白似乎发挥着细胞因子的作用。已确定人PGI与5-磷酸阿拉伯糖酸结合的晶体结构,分辨率为2.5埃,5-磷酸阿拉伯糖酸是一种强效抑制剂,模拟反应的顺式烯二醇(酸根)中间体。该结构有助于确认Glu357作为异构酶反应中碱基催化剂的归属。

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