High-level heterologous expression of fungal cytochrome P450s in Escherichia coli

18Citations
Citations of this article
60Readers
Mendeley users who have this article in their library.

Abstract

A thorough understanding of the sequence-structure-function relationships of cytochrome P450 (P450) is necessary to better understand the metabolic diversity of living organisms. Significant amounts of pure enzymes are sometimes required for biochemical studies, and their acquisition often relies on the possibility of their heterologous expression. In this study, we performed extensive heterologous expression of fungal P450s in Escherichia coli using 304 P450 isoforms. Using large-scale screening, we confirmed that at least 27 P450s could be expressed with/without simple sequence deletion at the 5' end of cDNAs, which encode the N-terminal hydrophobic domain of the enzyme. Moreover, we identified N-terminal amino acid sequences that can potentially be used to construct chimeric P450s, which could dramatically improve their expression levels even when the expression of the wild-type sequence was unpromising. These findings will help increase the chance of heterologous expression of a variety of fungal and other eukaryotic membrane-bound P450s in E. coli. © 2013 The Authors.

Cite

CITATION STYLE

APA

Ichinose, H., & Wariishi, H. (2013). High-level heterologous expression of fungal cytochrome P450s in Escherichia coli. Biochemical and Biophysical Research Communications, 438(2), 289–294. https://doi.org/10.1016/j.bbrc.2013.07.057

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free