Related Experiment Video
Updated: Apr 23, 2026
07:35
Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
6.3K
Mechanistic studies on the indole prenyltransferases
1Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, V6T 1Z1, British Columbia, Canada. mtanner@chem.ubc.ca.
Natural Product Reports
|October 2, 2014
Summary
Prenylated indole alkaloids are diverse natural products with potent biological activities. Recent studies reveal indole prenyltransferases utilize versatile mechanisms, including potential rearrangements after initial prenylation.
Area of Science:
- Natural Product Chemistry
- Enzymology
- Organic Chemistry
Background:
- Prenylated indole alkaloids are a diverse class of natural products known for potent biological activities.
- Prenyltransferases, enzymes that attach prenyl groups to indoles, have been recently discovered.
- These enzymes, though evolutionarily related, exhibit remarkable versatility in prenylation reactions.
Purpose of the Study:
- To highlight recent studies on the mechanisms employed by indole prenyltransferases.
- To explore the structural and reactivity insights into prenylation reactions.
Main Methods:
- Review of recent literature on indole prenyltransferases.
- Analysis of structure-activity relationships.
- Investigation of reaction mechanisms through biochemical studies.
Main Results:
- Indole prenyltransferases demonstrate versatility in catalyzing prenylation at various indole positions.
- While direct electrophilic aromatic substitution is a common mechanism, some reactions may involve initial prenylation at the C-3 position.
- Subsequent rearrangements can lead to the formation of final prenylated indole alkaloid products.
Conclusions:
- Indole prenyltransferases utilize diverse and adaptable mechanisms for prenylation.
- Understanding these mechanisms is crucial for the biosynthesis and potential synthetic applications of prenylated indole alkaloids.
More Related Videos
Related Concept Videos
01:13Induced-fit Model
76.8K
Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
76.8K
01:27Inductive Effects on Chemical Shift: Overview
2.3K
The protons in unsubstituted alkanes are strongly shielded with chemical shifts below 1.8 ppm. Methine, methylene, and methyl protons appear at approximately 1.7, 1.2 and 0.7 ppm, while the proton signal from methane appears at 0.23 ppm. An electronegative substituent, such as chlorine, withdraws the electron density from the protons, increasing their chemical shift. Progressive substitution of the hydrogens in methane by chlorine shifts the proton signals increasingly downfield, to 3.05 ppm in...
2.3K
02:45E2 Reaction: Kinetics and Mechanism
9.9K
SN2 substitutions and E2 eliminations of alkyl halides proceed via a concerted pathway. While the nucleophile attacks the alpha carbon in SN2 reactions, it functions as a strong base and abstracts a beta hydrogen in the E2 mechanism. The rate-limiting transition state in E2 elimination reactions is characterized by partially broken carbon–hydrogen and carbon–halogen bonds and a partially formed pi bond between the alpha and beta carbons. The beta hydrogen and halide are eliminated...
9.9K
02:46E1 Reaction: Kinetics and Mechanism
14.3K
Here, in contrast to the E2 reaction mechanism, we delve into the aspects of the E1 reaction mechanism, which has two steps: rate-limiting loss of the leaving group and abstraction of the beta hydrogen by a weak base. Typically, the experimental proof for the E1 mechanism is via kinetic studies or isotope studies. While the former demonstrates the first-order kinetics—the dependence of the reaction solely on substrate concentration—the latter proves the abstraction of hydrogen only...
14.3K
00:49Ligand Binding and Linkage
4.4K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.4K
01:19Allosteric Proteins-ATCase
4.8K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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...
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...
4.8K