Inhibition of Maize Caffeate 3- O -Methyltransferase by Nitecapone as a Possible Approach to Reduce Lignocellulosic Biom
- PDF / 2,683,657 Bytes
- 13 Pages / 595.276 x 790.866 pts Page_size
- 3 Downloads / 148 Views
ORIGINAL ARTICLE
Inhibition of Maize Caffeate 3-O-Methyltransferase by Nitecapone as a Possible Approach to Reduce Lignocellulosic Biomass Recalcitrance Angela Valderrama Parizotto 1 & Ana Paula Ferro 1 & Rogério Marchiosi 1 & Aline Finger-Teixeira 1 & Jennifer Munik Bevilaqua 1 & Wanderley Dantas dos Santos 1 & Flavio Augusto Vicente Seixas 2 & Osvaldo Ferrarese-Filho 1
# Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract Maize (Zea mays) caffeate 3-O-methyltransferase (ZmaysCOMT, EC 2.1.1.68), a key enzyme of the phenylpropanoid pathway, catalyzes the O-methylation of caffeic acid to ferulic acid, a precursor of lignin polymer and a crucial component of the cell wall structure. Plant cell wall recalcitrance is due to lignin, and the discovery of specific inhibitors of ZmaysCOMT could be useful to increase the digestibility of the lignocellulose biomass and improve the production of cellulosic biofuels. In this work, we have modeled the three-dimensional structure of ZmaysCOMT and prospected promising inhibitors by using virtual screening techniques. A set of 1668 putative candidates was screened from a virtual library and docked in the active site of the enzyme, and nitecapone was selected as one of the most promising enzyme inhibitors. Details of the mode of inhibition were assessed by in silico simulation and in vitro assays of nitecapone on the enzyme. In comparison with the nitecapone-free control, kinetics parameters showed different values of Vmax and KM, suggesting a kinetic profile such as mixed inhibition of the ZmaysCOMT. In brief, we suggest that the nitecapone-induced inhibition of ZmaysCOMT may serve as a non-transgenic strategy to explore the biosynthesis of ferulic acid and lignin, their relationships with the recalcitrance of lignocellulosic biomass, and, possibly, to improve bioethanol production. Keywords COMT . Virtual screening . Molecular docking . Nitrocatechol . Phenylpropanoid pathway . Zea mays
Introduction Key Message • Three-dimensional structure of maize (Zea mays) caffeate 3-Omethyltransferase was modeled • A set of 1668 putative inhibitors of ZmaysCOMT was screened from a virtual library • Nitecapone was selected as one of most promising enzyme inhibitors • A mixed inhibition of the ZmaysCOMT was obtained with nitecapone Electronic supplementary material The online version of this article (https://doi.org/10.1007/s11105-020-01242-x) contains supplementary material, which is available to authorized users. * Osvaldo Ferrarese-Filho [email protected] 1
Department of Biochemistry, Laboratory of Plant Biochemistry, State University of Maringá, Maringá, PR 87020-900, Brazil
2
Department of Technology, Laboratory of Structural Biochemistry, State University of Maringá, Maringá, PR 87506-370, Brazil
The recent economic and environmental scenario has strengthened the need to produce substitutes for fossil fuels in a sustainable manner, and lignocellulosic biomass is an important reservoir for the production of biofuels (Marriott et al. 2016). Lignocellulos
Data Loading...
