Carina Grittini
Scripps Research Institute, Joint Center for Structural Genomics
Papers
2
Total Citations
28
H-Index
2
About
Carina Grittini is a structural biologist whose work has illuminated key metabolic enzymes from the hyperthermophilic bacterium *Thermotoga maritima*. Her research centers on determining the three-dimensional architecture of proteins involved in fundamental biosynthetic and catabolic pathways, providing atomic-level insights into how these robust enzymes function at extreme temperatures. Grittini’s major contributions include solving the crystal structure of γ‑glutamyl phosphate reductase (GPR), the enzyme catalyzing the second, NADPH-dependent step of proline biosynthesis. By revealing the fold and active-site geometry of this essential enzyme at 2.0 Å resolution, she laid the groundwork for understanding proline production in thermophiles. She also determined the structure of uronate isomerase, which converts D‑glucuronate to D‑fructuronate in the uronate degradation pathway—a critical step for sugar acid catabolism. Although her citation counts (18 and 10, respectively) reflect the specialized nature of these structural reports, her work has been foundational for subsequent studies on thermostable enzymes and their potential biotechnological applications. Grittini’s precise crystallographic analyses continue to serve as key references for researchers exploring extremophile metabolism and enzyme evolution.
Research Focus
Key Achievements
Top Papers
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- 2