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EC Number Organic Solvent Commentary Reference
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7urea the urea-induced unfolding of the enzyme is a three-state process, where a metastable intermediate conformation state is populated between 3.0-4.0 M. Above 6.0 M urea, the enzyme gets completely unfolded. The transition from the native structure to the partially unfolded metastable state involves about 30% loss of native contacts but little change in the radius of gyration or core hydration properties. The intermediate-to-unfolded state transition is characterized by a large increase in the radius of gyration. Molecular dynamics trajectories simulated in different unfolding conditions suggest that urea destabilizes the enzyme structure weakening hydrophobic interactions and the hydrogen bond network 759343
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