The activity of human CYP2D6 in low water organic solvents
Identifieur interne : 002101 ( Main/Merge ); précédent : 002100; suivant : 002102The activity of human CYP2D6 in low water organic solvents
Auteurs : Jin Zhao [Canada] ; Karine Auclair [Canada]Source :
- Biotechnology and Bioengineering [ 0006-3592 ] ; 2009-03-01.
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Abstract
P450 enzymes are of high interest for synthetic applications due to their ability to catalyze hydroxylation reactions at inactivated C–H bonds. The low solubility of many substrates in buffer, however, is limiting the applications of P450s. Our recent demonstration that the P450 enzymes CYP2D6 and CYP3A4 can function very well in biphasic solvent systems is one step towards overcoming this drawback, but is not practical when substrates or products are unstable in water, or with water‐soluble products. An alternative strategy, which also facilitates enzyme recycling, is to directly resuspend lyophilized enzyme into nearly anhydrous organic solvents. Interestingly, we report here that CYP2D6 colyophilized with trehalose and suspended in n‐decane shows higher activity than in aqueous buffer. This study demonstrates the unexpected high tolerance of CYP2D6 to some low water organic solvents and provides an alternative strategy to facilitate the use of this enzyme in synthesis. Biotechnol. Bioeng. 2009;102: 1268–1272. © 2008 Wiley Periodicals, Inc.
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DOI: 10.1002/bit.22143
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Bioeng.</title><idno type="ISSN">0006-3592</idno><idno type="eISSN">1097-0290</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2009-03-01">2009-03-01</date><biblScope unit="volume">102</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="1268">1268</biblScope><biblScope unit="page" to="1272">1272</biblScope></imprint><idno type="ISSN">0006-3592</idno></series><idno type="istex">1F531F9BCD57915040E6BEABFB3A95937528ABE5</idno><idno type="DOI">10.1002/bit.22143</idno><idno type="ArticleID">BIT22143</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-3592</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>P450</term><term>anhydrous</term><term>decane</term><term>hydroxylation</term><term>monooxygenase</term><term>organic</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">P450 enzymes are of high interest for synthetic applications due to their ability to catalyze hydroxylation reactions at inactivated C–H bonds. The low solubility of many substrates in buffer, however, is limiting the applications of P450s. Our recent demonstration that the P450 enzymes CYP2D6 and CYP3A4 can function very well in biphasic solvent systems is one step towards overcoming this drawback, but is not practical when substrates or products are unstable in water, or with water‐soluble products. An alternative strategy, which also facilitates enzyme recycling, is to directly resuspend lyophilized enzyme into nearly anhydrous organic solvents. Interestingly, we report here that CYP2D6 colyophilized with trehalose and suspended in n‐decane shows higher activity than in aqueous buffer. This study demonstrates the unexpected high tolerance of CYP2D6 to some low water organic solvents and provides an alternative strategy to facilitate the use of this enzyme in synthesis. Biotechnol. Bioeng. 2009;102: 1268–1272. © 2008 Wiley Periodicals, Inc.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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