Suggested General Literature
1. I. G. Denisov, T. M. Makris, S. G. Sligar, I. Schlichting, Chem. Rev. 2005, 105. 2253-2278.
2. P. R. Ortiz de Montellano, J. J. De Voss, in Cytochrome P450: Structure, Mechanism and Biochemistry, ed. P. R. Ortiz de Montellano. Springer-Verlag: New York, 3rd edn., 2008.
3. M. J. Cryle, J. E. Stok, J. J. De Voss, Aus. J. Chem. 2003, 56. 749-762.
4. A. W. Munro, H. M. Girvan, J. P. McVey, K. J. McLean, Mod. Biooxid. 2007. 123-153.
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Examples of P450 substrates and the transformations that P450 enzymes can perform |
The P450s are a growing superfamily of enzymes, not only in the number of identified P450s but also in the chemistry they catalyse, the substrates they bind and the manner in which they effect oxygen activation. This can be seen in the increasing number of different types of redox partners possible for P450s, the identification of P450s capable of using peroxides as oxidants via the peroxide shunt pathway and in the use of carrier proteins as scaffolds for oxidation of substrates. Carrier proteins are four helix
bundles of ~80 amino acids, found either as isolated proteins or as domains in larger multi-domain proteins, such as polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). They share a conserved serine residue that is post-translationally modified with a phosphopantetheine linker.
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