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Subfunctionalization of a monolignol to a phytoalexin glucosyltransferase is accompanied by substrate inhibition

Plant Communications 2023年第3期4卷 151-170页

作者： Jieren Liao Guangxin Sun Elisabeth Kurze Wieland Steinchen Timothy D.Hoffmann Chuankui Song Zhiwei Zou Thomas Hoffmann Wilfried G.Schwab Biotechnology of Natural Products Technische University at MüunchenLiesel-Beckmann-Str.185354 FreisingGermany Center for Synthetic Microbiology(SYNMIKRO)&Faculty of Chemistry Philipps-University MarburgKarl-von-Frisch-Straße 1435043 MarburgGermany State Key Laboratory of Tea Plant Biology and Utilization International Joint Laboratory on Tea Chemistry and Health EffectsAnhui Agricultural University230036 HefeiAnhuiP.R.China Present address:Department of Molecular Biophysics and Biochemistry Yale UniversityNew HavenCTUSA

Uridine diphosphate-dependent glycosyltransferases(UGTs)mediate the glycosylation of plant metabolites,thereby altering their physicochemical properties and *** possess numerous UGT genes,with the encoded enzymes often glycosylating multiple substrates and some exhibiting substrate inhibition kinetics,but the biological function and molecular basis of these phenomena are not fully *** promiscuous monolignol/phytoalexin glycosyltransferase NbUGT72AY1 exhibits substrate inhibition(Ki)at 4 mM scopoletin,whereas the highly homologous monolignol StUGT72AY2 is inhibited at 190 *** therefore used hydrogen/deuterium exchange mass spectrometry and structure-based mutational analyses of both proteins and introduced NbUGT72AY1 residues into StUGT72AY2 and vice versa to study promiscuity and substrate inhibition of UGTs.A single F87I and chimeric mutant of NbUGT72AY1 showed significantly reducedscopoletin substrate inhibition,whereas its monolignolgly cosylation activity was almost *** mutations in StUGT72AY2 resulted in increased scopoletin glycosylation,leading to enhanced promiscuity,which was accompanied by substrate *** of 3D structures identified open and closed UGT conformers,allowing visualization of the dynamics of conformational changes that occur during *** postulated substrate access tunnels likely serve as drainage *** results suggest a two-site model in which the second substrate molecule binds near the catalytic site and blocks product *** studies showed that minor changes in amino acid sequence can enhance the promiscuity of the enzyme and add new capabilities such as substrate inhibition without affecting existing *** proposed subfunctionalization mechanism of expanded promiscuity may play a role in enzyme evolution and highlights the importance of promiscuous enzymes in providing new functions.

关键词： glycosyltransferase substrate inhibition hydrogen/deuterium exchange mass spectrometry protein morphing protein conformer scopoletin

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