Evolution cytochrome P450 enzymes

Duffy JE, Hay ME (2001) The ecology and evolution of marine consumer-prey interactions. In Bertness MD, Gaines SD, Hay ME (eds) Marine community ecology. Sinauer, Sunderland, pp 131-158 Duisken M, Sandner F, Blomeke B, Hollender J (2005) Metabolism of 1,8-cineole by human cytochrome P450 enzymes identification of a new hydroxylated metabolite. Biochim Biophys Acta 1722 304-311... 

Comparative biochemistry. Some researchers believe that the proper role of comparative biochemistry is to put evolution on a molecular basis, and that detoxication enzymes, like other enzymes, are suitable subjects for study. Xenobiotic-metabolizing enzymes were probably essential in the early stages of animal evolution because secondary plant products, even those of low toxicity, are frequently lipophilic and as a consequence would, in the absence of such enzymes, accumulate in lipid membranes and lipid depots. The evolution of cytochrome P450 isoforms, with more than 2000 isoform cDNA sequences known, is proving a useful tool for the study of biochemical evolution. 

These screens have been used to direct the evolution of cytochrome P450 BM-3, a soluble enzyme from Bacillus megaterium that contains its reductase and hydroxylase domains on a single polypeptide chain. P450 BM-3 primarily catalyzes the hydroxylation of fatty acids ( 12 to 18 carbons long) at the a>-1, a>-2, and m-3 positions, but also... 

An example of the use of isolated enzymes is the work on directed evolution by random mutagenesis of the fatty acid hydroxylase cytochrome P450 BM-3 by the group of Arnold [254] (Table 1.10). The target reaction was the enantioselective... 

Class III peroxidases have been the subject of numerous studies [10] and applications [11], since their extraordinary catalytic properties make them a valuable catalytic tool in the plant cell chemical factory, and in organic synthesis. In fact, class III peroxidases, together with other oxidative enzymes, such as cytochrome P450s and oxygenases [12], appear to be the main driving force in the evolution of plant metabolic pathways because individual enzymes can typically accept multiple substrates and form several products. This metabolic plasticity of class III peroxidases, paradoxically, has frequently led to misunderstanding of its vital function in the plant cell biochemical factory. 

Kumar S, Halpert JR (2005) Use of directed evolution of mammalian cytochromes P450 for investigating the molecular basis of enzyme function and generating novel biocatalysts. Biochem Biophys Res Commun 338 456 64... 

Lentz, O., Li, Q.S., Schwaneberg, U., Lutz-Wahl, S., Fischer, P., and Schmid, R.D. (2001) Modification of the fatty acid specificity of cytochrome P450 BM-3 from BaciUus megaterium by directed evolution a validated assay. J. Md. Catal B Enzym., 15, 123 133. 

Axarli I, Prigipaki A, Labrou NE (2005) Engineering the substrate specificity of cytochrome P450 CYP102A2 by directed evolution production of an efficient enzyme for bioconversion of fine chemicals. Biomol Eng 22 81-88... 

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