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Title 

Functional expression of mammalian NADPH-cytochrome P450 oxidoreductase on the cell surface of Escherichia coli

Authors 

S K YimHeung Chae JungJae Gu PanH S KangT AhnC H Yun

Publisher 

Elsevier

Issue Date 

2006

Citation 

Protein Expression & Purification, vol. 49, no. 2, pp. 292-298

Keywords 

diflavin-containing mammalian enzymeoxidoreductasereductionsurface displaywhole-cell biocatalystcell membraneescherichia coligene expressionNADPH-ferrihemoprotein reductase

Abstract 

To develop a whole-cell oxidoreductase system without the practical limitation of substrate/product transport, easy preparation, stability of enzymes, and low expression levels, we here report the development of a whole cell biocatalyst displaying rat NADPH-cytochrome P450 oxidoreductase (CPR, 77-kDa) on the surface of Escherichia coli by using ice-nucleation protein from Pseudomonas syringae. Surface localization and functionality of the CPR were verified by flow cytometry, electron microscopy, and measurements of enzyme activities. The results of this study comprise the first report of microbial cell-surface display of diflavin-containing mammalian enzymes. This system will allow us to select and develop oxidoreductases, containing bulky and complex prosthetic groups of FAD and FMN, into practically useful whole-cell biocatalysts for broad biological and biotechnological applications including the selective synthesis of new chemicals and pharmaceuticals, bioconversion, bioremediation, and bio-chip development.

ISSN 

1046-5928

Link 

http://dx.doi.org/10.1016/j.pep.2006.05.013

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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