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Controlling the Substrate Specificity of an Enzyme through Structural Flexibility by Varying the Salt-Bridge Density
2021
Molecules
Many enzymes, particularly in one single family, with highly conserved structures and folds exhibit rather distinct substrate specificities. The underlying mechanism remains elusive, the resolution of which is of great importance for biochemistry, biophysics, and bioengineering. Here, we performed a neutron scattering experiment and molecular dynamics (MD) simulations on two structurally similar CYP450 proteins; CYP101 primarily catalyzes one type of ligands, then CYP2C9 can catalyze a large
doi:10.3390/molecules26185693
pmid:34577164
pmcid:PMC8470667
fatcat:b5jheekkfjddtefyjiclh7curu