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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Structural determinants of cytochrome P450 substrate specificity, binding affinity and catalytic rate.

The structural characteristics of cytochrome P450 substrates are summarised, showing that molecular descriptors can discriminate between chemicals of differing P450 isozyme specificity. Procedures for the estimation of P450 substrate binding interaction energies and rates of metabolism are described, providing specific examples in both individual compounds binding to P450s, including those of known crystal structure, and within series of structurally related chemicals. It is demonstrated that binding energy components are primarily hydrophobic/desolvation and electrostatic/hydrogen-bonded in nature, whereas electronic factors are of importance in determining variations in reaction rates. It is thus shown that the prediction of P450 substrate binding affinities and catalytic rates may be feasible, provided that sufficient structural information is available for the relevant enzyme-substrate complex.[1]

References

  1. Structural determinants of cytochrome P450 substrate specificity, binding affinity and catalytic rate. Lewis, D.F., Eddershaw, P.J., Dickins, M., Tarbit, M.H., Goldfarb, P.S. Chem. Biol. Interact. (1998) [Pubmed]
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