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Preparative use of isolated CYP102 monooxygenases—A critical appraisal ☆

Paper ID Volume ID Publish Year Pages File Format Full-Text
25336 43568 2006 8 PDF Available
Title
Preparative use of isolated CYP102 monooxygenases—A critical appraisal ☆
Abstract

Isolated P450 monooxygenases have for long been neglected catalysts in enzyme technology. This is surprising as they display a remarkable substrate specificity catalyzing reactions, which represent a challenge for classic organic chemistry. On the other hand, many P450 monooxygenases are membrane bound, depend on rather complicated electron transfer systems and require expensive cofactors such as NAD(P)H. Their activities are low, and stability leaves much to be desired. The use of bacterial P450 monooxygenases from CYP102 family allows overcoming some of these handicaps. They are soluble and their turnovers are high, presumably because their N-terminal heme monooxygenase and their C-terminal diflavin reductase domain are covalently linked. In recent years, protein engineering approaches have been successfully used to turn CYP102 monooxgenases into powerful biocatalysts.

Keywords
P450 monooxygenase; Enzyme technology; Enzyme stability; Co-factor regeneration
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Preparative use of isolated CYP102 monooxygenases—A critical appraisal ☆
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 124, Issue 4, 5 August 2006, Pages 662–669
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
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