Related Experiment Video
Updated: Dec 26, 2025

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography
Published on: January 17, 2020
Substrate specificity change of a flavonoid prenyltransferase AhPT1 induced by metal ion
Jiali Yang1, Ting Zhou1, Yueming Jiang2
1Key Laboratory of Plant Resource Conservation and Sustainable Utilization, Key Laboratory of Post-Harvest Handling of Fruits, Ministry of Agriculture, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou 510650, China; University of Chinese Academy of Sciences, Beijing 100049, China.
Abstract:
Prenylated flavonoids are good drug candidates due to multiple biological activities and health benefits. Prenyltransferase is an important enzyme involved in the biosynthesis of prenylated flavonoids. In this work, a flavonoid prenyltransferase (AhPT1) from Artocarpus heterophyllus showed an unexpectedly metal ion-induced specificity to flavonoid substrates. AhPT1 could catalyse 6-C-prenylation of genistein when Mg2+ serving as cofactor. Its catalytic activity to 6-hydroxyflavone was undetectable. However, when Mn2+ was used instead of Mg2+, 5-C-prenylated 6-hydroxyflavone was generated with a high conversion rate. Mn2+ altered the regiospecificity of AhPT1 and turned it into a 5-C-prenyltransferase. 2'-Hydroxyl could improve the conversion rate of 6-hydroxyflavone, whereas 3'- or 4'-hydroxyl impaired the catalysis efficiency of AhPT1. NQIFDADID174 and DLTDVEGD305 were active motifs involved in substrate binding and catalysis. Asn166, Asp170, Asp174, Asp298, Asp301 and Asp305 in the active center were critical to the prenylation reaction.
More Related Videos
07:54Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
Published on: August 22, 2018
12:08Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Related Concept Videos
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Ligand Binding and Linkage
Enzyme Inhibition
Introduction to Mechanisms of Enzyme Catalysis
Factors Affecting Drug Biotransformation: Physicochemical and Chemical Properties of Drugs
The drug's acidity or basicity is essential in...
Extraction: Advanced Methods