Eunjeong Lee

ORCID: 0000-0003-0560-2943
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About
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Research Areas
  • Heme Oxygenase-1 and Carbon Monoxide
  • Biofuel production and bioconversion
  • Metabolism and Genetic Disorders
  • Neonatal Health and Biochemistry
  • Enzyme Production and Characterization
  • Pneumonia and Respiratory Infections
  • Coal and Coke Industries Research
  • Streptococcal Infections and Treatments
  • Porphyrin Metabolism and Disorders

University of Colorado Anschutz Medical Campus
2024

Royal London Hospital
1931

University of Toronto
1931

Serine proteases have been proposed to dynamically sample inactive and active conformations, but direct evidence at atomic resolution has remained elusive. Using nuclear magnetic resonance (NMR), we identified a single residue, D164, in exfoliative toxin A (ETA) that acts as molecular “switch” regulate global dynamic sampling. Mutations this site shift the balance between states, correlating directly with catalytic activity. Beyond identifying switch, demonstrate how it works concert other...

10.1126/sciadv.adu7447 article EN Science Advances 2025-04-09

Biliverdin IXβ reductase (BLVRB) is an NADPH-dependent enzyme previously implicated in a redox-regulated mechanism of thrombopoiesis distinct from the thrombopoietin (TPO)/c-MPL axis. Here, we apply computational modeling to inform molecule design, followed by de novo syntheses and screening unique small molecules retaining capacity for selective BLVRB inhibition as novel platelet-enhancing strategy. Two classes are identified, NMR spectroscopy co-crystallization studies confirm binding...

10.1038/s41467-025-58497-9 article EN cc-by-nc-nd Nature Communications 2025-04-11

10.1016/s0021-9258(18)76605-2 article EN cc-by Journal of Biological Chemistry 1931-04-01

Biliverdin reductase B (BLVRB) is a redox regulator that catalyzes nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reductions of multiple substrates, including flavins and biliverdin-β. BLVRB has emerging roles in regulation post-translational modifications, highlighting its importance various physiological contexts. In this study, we explore the structural functional differences between human hyrax homologue, focusing on evolutionary adaptations at active site allosteric...

10.3390/ijms252413233 article EN International Journal of Molecular Sciences 2024-12-10

Streptococcus pneumoniae (S. pneumoniae) employs various metabolic pathways to generate nicotinamide adenine dinucleotide phosphate (NADPH), which is essential for redox balance, fatty acid synthesis, and energy production. GAPN, a non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, plays role in this process by directly reducing NADP

10.1002/pro.5253 article EN cc-by Protein Science 2024-12-11
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