P450 enzymes from the bacterium Novosphingobium aromaticivorans.
Twelve of the fifteen potential P450 enzymes from the bacterium Novosphingobium aromaticivorans, which is known to degrade a wide range of aromatic hydrocarbons, have been produced via heterologous expression in Escherichia coli. The enzymes were tested for their ability to bind a range of substrate...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
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2007
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| _version_ | 1797061892216193024 |
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| author | Bell, S Wong, L |
| author_facet | Bell, S Wong, L |
| author_sort | Bell, S |
| collection | OXFORD |
| description | Twelve of the fifteen potential P450 enzymes from the bacterium Novosphingobium aromaticivorans, which is known to degrade a wide range of aromatic hydrocarbons, have been produced via heterologous expression in Escherichia coli. The enzymes were tested for their ability to bind a range of substrates including polyaromatic hydrocarbons. While two of the enzymes were found to bind aromatic compounds (CYP108D1 and CYP203A2), the others show binding with a variety of compounds including linear alkanes (CYP153C1) and mono- and sesqui-terpenoid compounds (CYP101B1, CYP101C1, CYP101D1, CYP101D2, CYP111A1, and CYP219A1). A 2Fe-2S ferredoxin (Arx-A), which is associated with CYP101D2, was also produced. The activity of five of the P450 enzymes (CYP101B1, CYP101C1, CYP101D1, CYP101D2, and CYP111A2) was reconstituted with Arx-A and putidaredoxin reductase (of the P450cam system from Pseudomonas putida) in a Class I type electron transfer system. Preliminary characterisation of the majority of the substrate oxidation products is reported. |
| first_indexed | 2024-03-06T20:37:40Z |
| format | Journal article |
| id | oxford-uuid:332b28b6-b8c6-4f13-b0ea-a0bd9752e249 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:37:40Z |
| publishDate | 2007 |
| record_format | dspace |
| spelling | oxford-uuid:332b28b6-b8c6-4f13-b0ea-a0bd9752e2492022-03-26T13:18:44ZP450 enzymes from the bacterium Novosphingobium aromaticivorans.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:332b28b6-b8c6-4f13-b0ea-a0bd9752e249EnglishSymplectic Elements at Oxford2007Bell, SWong, LTwelve of the fifteen potential P450 enzymes from the bacterium Novosphingobium aromaticivorans, which is known to degrade a wide range of aromatic hydrocarbons, have been produced via heterologous expression in Escherichia coli. The enzymes were tested for their ability to bind a range of substrates including polyaromatic hydrocarbons. While two of the enzymes were found to bind aromatic compounds (CYP108D1 and CYP203A2), the others show binding with a variety of compounds including linear alkanes (CYP153C1) and mono- and sesqui-terpenoid compounds (CYP101B1, CYP101C1, CYP101D1, CYP101D2, CYP111A1, and CYP219A1). A 2Fe-2S ferredoxin (Arx-A), which is associated with CYP101D2, was also produced. The activity of five of the P450 enzymes (CYP101B1, CYP101C1, CYP101D1, CYP101D2, and CYP111A2) was reconstituted with Arx-A and putidaredoxin reductase (of the P450cam system from Pseudomonas putida) in a Class I type electron transfer system. Preliminary characterisation of the majority of the substrate oxidation products is reported. |
| spellingShingle | Bell, S Wong, L P450 enzymes from the bacterium Novosphingobium aromaticivorans. |
| title | P450 enzymes from the bacterium Novosphingobium aromaticivorans. |
| title_full | P450 enzymes from the bacterium Novosphingobium aromaticivorans. |
| title_fullStr | P450 enzymes from the bacterium Novosphingobium aromaticivorans. |
| title_full_unstemmed | P450 enzymes from the bacterium Novosphingobium aromaticivorans. |
| title_short | P450 enzymes from the bacterium Novosphingobium aromaticivorans. |
| title_sort | p450 enzymes from the bacterium novosphingobium aromaticivorans |
| work_keys_str_mv | AT bells p450enzymesfromthebacteriumnovosphingobiumaromaticivorans AT wongl p450enzymesfromthebacteriumnovosphingobiumaromaticivorans |