Enzyme-substrate complementarity governs access to a cationic reaction manifold 
in the P450(BM3)-catalysed oxidation of cyclopropyl fatty acids.

Cryle, Max; Hayes, Patricia Y.; De Voss, James J.

doi:10.1002/chem.201203035

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Enzyme-substrate complementarity governs access to a cationic reaction manifold in the P450(BM3)-catalysed oxidation of cyclopropyl fatty acids.

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Cryle, Max
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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http://dx.doi.org/10.1002/chem.201203035
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Citation

Cryle, M., Hayes, P. Y., & De Voss, J. J. (2012). Enzyme-substrate complementarity governs access to a cationic reaction manifold in the P450(BM3)-catalysed oxidation of cyclopropyl fatty acids. Chemistry - A European Journal, 18(50), 15994-15999. doi:10.1002/chem.201203035.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-1147-8

Abstract

The products of cytochrome P450BM3−catalysed oxidation of cyclopropyl−containing dodecanoic acids are consistent with the presence of a cationic reaction intermediate, which results in efficient dehydrogenation of the rearranged probes by the enzyme. These results highlight the importance of enzyme−substrate complementarity, with a cationic intermediate occurring only when the probes used begin to diverge from ideal substrates for this enzyme. This also aids in reconciling literature reports supporting the presence of cationic intermediates with certain cytochrome P450 enzyme/substrate pairs