## 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
Cytochrome P450 monooxygenases
β Scribed by Luet-Lok Wong
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 572 KB
- Volume
- 2
- Category
- Article
- ISSN
- 1367-5931
No coin nor oath required. For personal study only.
β¦ Synopsis
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 methods of substrate turnover described. These developments, arising from our increased understanding of the chemistry and molecular biology of P450 enzymes, open up new and exciting research directions.
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## 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