P450(BM3) (CYP102A1): connecting the dots.
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...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2012
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| _version_ | 1826292389197643776 |
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| author | Whitehouse, C Bell, S Wong, L |
| author_facet | Whitehouse, C Bell, S Wong, L |
| author_sort | Whitehouse, C |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T03:13:56Z |
| format | Journal article |
| id | oxford-uuid:b5250b6e-2307-4b36-ade2-b129c43a5251 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:13:56Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:b5250b6e-2307-4b36-ade2-b129c43a52512022-03-27T04:31:15ZP450(BM3) (CYP102A1): connecting the dots.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b5250b6e-2307-4b36-ade2-b129c43a5251EnglishSymplectic Elements at Oxford2012Whitehouse, CBell, SWong, LP450(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. |
| spellingShingle | Whitehouse, C Bell, S Wong, L P450(BM3) (CYP102A1): connecting the dots. |
| title | P450(BM3) (CYP102A1): connecting the dots. |
| title_full | P450(BM3) (CYP102A1): connecting the dots. |
| title_fullStr | P450(BM3) (CYP102A1): connecting the dots. |
| title_full_unstemmed | P450(BM3) (CYP102A1): connecting the dots. |
| title_short | P450(BM3) (CYP102A1): connecting the dots. |
| title_sort | p450 bm3 cyp102a1 connecting the dots |
| work_keys_str_mv | AT whitehousec p450bm3cyp102a1connectingthedots AT bells p450bm3cyp102a1connectingthedots AT wongl p450bm3cyp102a1connectingthedots |