Enzyme-substrate complementarity governs access to a cationic reaction manifold in the P450(BM3)-catalysed oxidation of cyclopropyl fatty acids.
| Autor: | Cryle MJ; School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia Brisbane, 4072, Australia., Hayes PY, De Voss JJ |
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| Jazyk: | angličtina |
| Zdroj: | Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2012 Dec 07; Vol. 18 (50), pp. 15994-9. Date of Electronic Publication: 2012 Oct 29. |
| DOI: | 10.1002/chem.201203035 |
| Abstrakt: | The products of cytochrome P450(BM3)-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. (Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.) |
| Databáze: | MEDLINE |
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