Papers
2
Total Citations
28
H-Index
2
About
Bill West’s research career has centered on structural biology and enzymology, with a particular focus on elucidating the three-dimensional structures of key metabolic enzymes from extremophilic organisms. His major contributions include solving the crystal structures of γ-glutamyl phosphate reductase (GPR) and uronate isomerase from the hyperthermophilic bacterium *Thermotoga maritima*. The GPR structure (18 citations) revealed the molecular mechanism of the second step in proline biosynthesis, a reversible NADPH-dependent reduction critical for cellular stress responses. Meanwhile, the uronate isomerase structure (10 citations) provided insights into the conversion of uronic acids, an essential pathway for carbohydrate metabolism in thermophiles. By determining these structures at high resolution (2.0–2.85 Å), West advanced our understanding of enzyme adaptation to extreme temperatures and the catalytic strategies employed by these ancient proteins. His work has been foundational for researchers studying proline metabolism, thermostable enzymes, and the evolution of metabolic pathways, making him a notable figure in the field of structural biochemistry.
Research Focus
Key Achievements
Top Papers
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