ArticleDrug metabolism and disposition: the biological fate of chemicals2026
High-level expression of full-length human CYP2E1 in Escherichia coli: Comparison of full-length human CYP2E1 to truncated counterpart shows enhanced association with redox partners.
Article in Drug metabolism and disposition: the biological fate of chemicals, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Few liver microsomal cytochromes P450 (P450s), especially human P450s, are recombinantly expressed in bacteria as full-length proteins. Lack of the N-terminal membrane anchor hinders studies of the interactions of microsomal P450s with redox partners. Herein, we describe the successful expression of full-length human CYP2E1, referred to as hCYP2E1FLAL, in bacteria to give a yield of ∼704 nmol/L culture. This high-level expression was achieved due to the codon optimization strategy employed to reduce free energy for translation and growth temperature. The expressed hCYP2E1FLAL was purified with a single affinity column and contained no P420, the inactive form of P450. Compared with N-terminal truncated human CYP2E1 (hCYP2E1dH), hCYP2E1FLAL exhibits elevated enzyme activity toward prototypic substrates, chlorzoxazone and p-nitrophenol, with ∼2-fold increase in k
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