Peroxidase activity of bacterial cytochrome P450 enzymes: modulation by fatty acids and organic solvents

Biotechnology Journal
Kersten S RabeChristof M Niemeyer

Abstract

The modulation of peroxidase activity by fatty acid additives and organic cosolvents was determined and compared for four bacterial cytochrome P450 enzymes, thermostable P450 CYP119A1, the P450 domain of CYP102A1 (BMP), CYP152A1 (P450(bsbeta)), and CYP101A1 (P450(cam)). Utilizing a high-throughput microplate assay, we were able to readily screen more than 100 combinations of enzymes, additives and cosolvents in a convenient and highly reproducible assay format. We found that, in general, CYP119A1 and BMP showed an increase in peroxidative activity in the presence of fatty acids, whereas CYP152A1 revealed a decrease in activity and CYP101A1 was only slightly affected. In particular, we observed that the conversion of the fluorogenic peroxidase substrate Amplex Red by CYP119A1 and BMP was increased by a factor of 38 or 11, respectively, when isopropanol and lauric acid were present in the reaction mixture. The activity of CYP119A1 could thus be modulated to reach more than 90% of the activity of CYP152A1 without effectors, which is the system with the highest peroxidative activity. For all P450s investigated we found distinctive reactivity patterns, which suggest similarities in the binding site of CYP119A1 and BMP in contrast wi...Continue Reading

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Citations

Mar 10, 2011·Angewandte Chemie·Felipe E ZillyManfred T Reetz
Aug 5, 2016·Chemical Record : an Official Publication of the Chemical Society of Japan ... [et Al.]·Yi-Ru LiangXian-Fu Lin
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Oct 17, 2014·Bioconjugate Chemistry·Jae Hyung LeeKi Jun Jeong
Aug 26, 2021·Biotechnology and Applied Biochemistry·Tugce Sakalli, Nur Basak Surmeli

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