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- W2313854513 abstract "The role of the nonreacting phosphodianion group of 1-deoxy-d-xylulose-5-phosphate (DXP) in catalysis by DXP reductoisomerase (DXR) was investigated for the reaction of the substrate in pieces. The truncated substrate 1-deoxy-l-erythrulose is converted by DXR to 2-C-methylglycerol with a kcat/Km that is 10(6)-fold lower than that for DXP. Phosphite dianion was found to be a nonessential activator, providing 3.2 kcal/mol of transition state stabilization for the truncated substrate. These results implicate a phosphate-driven conformational change involving loop closure over the DXR active site to generate an environment poised for catalysis." @default.
- W2313854513 created "2016-06-24" @default.
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- W2313854513 date "2013-03-20" @default.
- W2313854513 modified "2023-09-27" @default.
- W2313854513 title "DXP Reductoisomerase: Reaction of the Substrate in Pieces Reveals a Catalytic Role for the Nonreacting Phosphodianion Group" @default.
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- W2313854513 doi "https://doi.org/10.1021/bi400092n" @default.
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