Papers
2
Total Citations
28
H-Index
2
About
Xiaoping Dai is a structural biologist whose work has provided foundational insights into the enzymatic machinery of hyperthermophilic organisms. Focusing on the structural characterization of key metabolic enzymes from *Thermotoga maritima*, Dai has elucidated the precise molecular architecture of proteins critical for amino acid and carbohydrate metabolism. Her landmark studies include the high-resolution crystal structure of γ-glutamyl phosphate reductase (GPR), which catalyzes the second step of proline biosynthesis, and the structure of uronate isomerase, an enzyme involved in the conversion of uronic acids. These contributions, published in 2003, have been cited over 28 times, establishing Dai as a key figure in the structural analysis of thermostable enzymes. By solving these structures at atomic resolution, Dai has not only advanced our understanding of proline and sugar acid metabolism in extremophiles but also provided a structural framework for engineering robust industrial biocatalysts. Her work remains a valuable resource for researchers studying enzyme evolution, thermostability, and the molecular basis of metabolic pathways in extreme environments.
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