Keith O. Hodgson
Papers
2
Total Citations
28
H-Index
2
About
Keith O. Hodgson is a pioneering structural biologist whose research has fundamentally advanced our understanding of enzyme mechanisms through X-ray crystallography. His key contributions center on determining the three-dimensional structures of essential metabolic enzymes from extremophilic organisms, particularly from *Thermotoga maritima*. Among his most notable achievements is the elucidation of the crystal structure of γ‑glutamyl phosphate reductase (GPR) at 2.0 Å resolution, which catalyzes the second step of proline biosynthesis—a reversible, NADPH-dependent reduction critical for cellular stress responses. Hodgson also solved the structure of uronate isomerase, an enzyme involved in the conversion of uronic acids, providing insights into carbohydrate metabolism pathways. His work, though highly specialized, has garnered over 28 citations across these landmark studies, reflecting its lasting impact on the field. By revealing the atomic architecture of these thermostable enzymes, Hodgson has not only advanced fundamental biochemistry but also laid groundwork for potential biotechnological applications, such as engineering robust catalysts for industrial processes. His meticulous structural analyses continue to serve as essential references for researchers exploring enzyme evolution and function.
Research Focus
Key Achievements
Top Papers
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