The field of P450 research is progressing rapidly. The active sites of structurally characterized bacterial P450 enzymes have been rationally re-engineered to alter both substrate specificity and selectivity of substrate oxidation. Many human P450 enzymes have been functionally expressed and new met
Cytochrome P450 monooxygenases: perspectives for synthetic application
β Scribed by Vlada B. Urlacher; Sabine Eiben
- Book ID
- 113931995
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 201 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0167-7799
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## Abstract Recently, cytochrome P450 170A1 (CYP170A1) has been found to be a bifunctional protein, which catalyzes both monooxygenase activity and terpene synthase activity by two distinct active sites in the wellβestablished P450 protein structure. Therefore, CYP170A1 is identified clearly as a m
## Abstract Cytochrome P450 monooxygenases (CYPs) are important enzymes in the metabolism of xenobiotics. Therefore, several approaches to clone and overexpress the human isoforms have been made. In addition to microsomes or S9 preparations, these recombinant human isoforms have found diverse appli