P450(BM3) (CYP102A1): connecting the dots
| Autor: | Christopher J. C. Whitehouse, Luet-Lok Wong, Stephen Bell |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
biology
Chemistry Drug metabolite Molecular Sequence Data Context (language use) General Chemistry biology.organism_classification Protein Engineering Bacterial Proteins Cytochrome P-450 Enzyme System Anaerobic oxidation of methane Fatty acid hydroxylase Mutation Organic chemistry Animals Humans Amino Acid Sequence Oxidation-Reduction Bacillus megaterium NADPH-Ferrihemoprotein Reductase |
| Popis: | P450(BM3) (CYP102A1), a fatty acid hydroxylase from Bacillus megaterium, has been extensively studied over a period of almost forty years. The enzyme has been redesigned to catalyse the oxidation of non-natural substrates as diverse as pharmaceuticals, terpenes and gaseous alkanes using a variety of engineering strategies. Crystal structures have provided a basis for several of the catalytic effects brought about by mutagenesis, while changes to reduction potentials, inter-domain electron transfer rates and catalytic parameters have yielded functional insights. Areas of active research interest include drug metabolite production, the development of process-scale techniques, unravelling general mechanistic aspects of P450 chemistry, methane oxidation, and improving selectivity control to allow the synthesis of fine chemicals. This review draws together the disparate research themes and places them in a historical context with the aim of creating a resource that can be used as a gateway to the field. |
| Databáze: | OpenAIRE |
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